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class="vector-toc-link" href="#Polar_charged_side_chains"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.2.1</span> <span>Polar charged side chains</span> </div> </a> <ul id="toc-Polar_charged_side_chains-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Polar_uncharged_side_chains" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Polar_uncharged_side_chains"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.2.2</span> <span>Polar uncharged side chains</span> </div> </a> <ul id="toc-Polar_uncharged_side_chains-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Hydrophobic_side_chains" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Hydrophobic_side_chains"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.2.3</span> <span>Hydrophobic side chains</span> </div> </a> <ul id="toc-Hydrophobic_side_chains-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Special_case_side_chains" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Special_case_side_chains"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.2.4</span> <span>Special case side chains</span> </div> </a> <ul id="toc-Special_case_side_chains-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-β-_and_γ-amino_acids" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#β-_and_γ-amino_acids"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.2.5</span> <span>β- and γ-amino acids</span> </div> </a> <ul id="toc-β-_and_γ-amino_acids-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Zwitterions" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Zwitterions"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.3</span> <span>Zwitterions</span> </div> </a> <ul id="toc-Zwitterions-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Isoelectric_point" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Isoelectric_point"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.4</span> <span>Isoelectric point</span> </div> </a> <ul id="toc-Isoelectric_point-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Physicochemical_properties" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Physicochemical_properties"> <div class="vector-toc-text"> <span class="vector-toc-numb">3</span> <span>Physicochemical properties</span> </div> </a> <button aria-controls="toc-Physicochemical_properties-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Physicochemical properties subsection</span> </button> <ul id="toc-Physicochemical_properties-sublist" class="vector-toc-list"> <li id="toc-Table_of_standard_amino_acid_abbreviations_and_properties" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Table_of_standard_amino_acid_abbreviations_and_properties"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.1</span> <span>Table of standard amino acid abbreviations and properties</span> </div> </a> <ul id="toc-Table_of_standard_amino_acid_abbreviations_and_properties-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Occurrence_and_functions_in_biochemistry" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Occurrence_and_functions_in_biochemistry"> <div class="vector-toc-text"> <span class="vector-toc-numb">4</span> <span>Occurrence and functions in biochemistry</span> </div> </a> <button aria-controls="toc-Occurrence_and_functions_in_biochemistry-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Occurrence and functions in biochemistry subsection</span> </button> <ul id="toc-Occurrence_and_functions_in_biochemistry-sublist" class="vector-toc-list"> <li id="toc-Proteinogenic_amino_acids" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Proteinogenic_amino_acids"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.1</span> <span>Proteinogenic amino acids</span> </div> </a> <ul id="toc-Proteinogenic_amino_acids-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Standard_vs_nonstandard_amino_acids" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Standard_vs_nonstandard_amino_acids"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.2</span> <span>Standard vs nonstandard amino acids</span> </div> </a> <ul id="toc-Standard_vs_nonstandard_amino_acids-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Non-proteinogenic_amino_acids" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Non-proteinogenic_amino_acids"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.3</span> <span>Non-proteinogenic amino acids</span> </div> </a> <ul id="toc-Non-proteinogenic_amino_acids-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-In_mammalian_nutrition" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#In_mammalian_nutrition"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.4</span> <span>In mammalian nutrition</span> </div> </a> <ul id="toc-In_mammalian_nutrition-sublist" class="vector-toc-list"> <li id="toc-Semi-essential_and_conditionally_essential_amino_acids,_and_juvenile_requirements" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Semi-essential_and_conditionally_essential_amino_acids,_and_juvenile_requirements"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.4.1</span> <span>Semi-essential and conditionally essential amino acids, and juvenile requirements</span> </div> </a> <ul id="toc-Semi-essential_and_conditionally_essential_amino_acids,_and_juvenile_requirements-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Non-protein_functions" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Non-protein_functions"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.5</span> <span>Non-protein functions</span> </div> </a> <ul id="toc-Non-protein_functions-sublist" class="vector-toc-list"> <li id="toc-Standard_amino_acids" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Standard_amino_acids"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.5.1</span> <span>Standard amino acids</span> </div> </a> <ul id="toc-Standard_amino_acids-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Roles_for_nonstandard_amino_acids" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Roles_for_nonstandard_amino_acids"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.5.2</span> <span>Roles for nonstandard amino acids</span> </div> </a> <ul id="toc-Roles_for_nonstandard_amino_acids-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> </ul> </li> <li id="toc-Uses_in_industry" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Uses_in_industry"> <div class="vector-toc-text"> <span class="vector-toc-numb">5</span> <span>Uses in industry</span> </div> </a> <button aria-controls="toc-Uses_in_industry-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Uses in industry subsection</span> </button> <ul id="toc-Uses_in_industry-sublist" class="vector-toc-list"> <li id="toc-Animal_feed" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Animal_feed"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.1</span> <span>Animal feed</span> </div> </a> <ul id="toc-Animal_feed-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Food" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Food"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.2</span> <span>Food</span> </div> </a> <ul id="toc-Food-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Chemical_building_blocks" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Chemical_building_blocks"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.3</span> <span>Chemical building blocks</span> </div> </a> <ul id="toc-Chemical_building_blocks-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Aspirational_uses" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Aspirational_uses"> <div class="vector-toc-text"> <span class="vector-toc-numb">6</span> <span>Aspirational uses</span> </div> </a> <button aria-controls="toc-Aspirational_uses-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Aspirational uses subsection</span> </button> <ul id="toc-Aspirational_uses-sublist" class="vector-toc-list"> <li id="toc-Fertilizer" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Fertilizer"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.1</span> <span>Fertilizer</span> </div> </a> <ul id="toc-Fertilizer-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Biodegradable_plastics" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Biodegradable_plastics"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.2</span> <span>Biodegradable plastics</span> </div> </a> <ul id="toc-Biodegradable_plastics-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Synthesis" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Synthesis"> <div class="vector-toc-text"> <span class="vector-toc-numb">7</span> <span>Synthesis</span> </div> </a> <button aria-controls="toc-Synthesis-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Synthesis subsection</span> </button> <ul id="toc-Synthesis-sublist" class="vector-toc-list"> <li id="toc-Chemical_synthesis" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Chemical_synthesis"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.1</span> <span>Chemical synthesis</span> </div> </a> <ul id="toc-Chemical_synthesis-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Biosynthesis" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Biosynthesis"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.2</span> <span>Biosynthesis</span> </div> </a> <ul id="toc-Biosynthesis-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Primordial_synthesis" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Primordial_synthesis"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.3</span> <span>Primordial synthesis</span> </div> </a> <ul id="toc-Primordial_synthesis-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Reactions" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Reactions"> <div class="vector-toc-text"> <span class="vector-toc-numb">8</span> <span>Reactions</span> </div> </a> <button aria-controls="toc-Reactions-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Reactions subsection</span> </button> <ul id="toc-Reactions-sublist" class="vector-toc-list"> <li id="toc-Peptide_bond_formation" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Peptide_bond_formation"> <div class="vector-toc-text"> <span class="vector-toc-numb">8.1</span> <span>Peptide bond formation</span> </div> </a> <ul id="toc-Peptide_bond_formation-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Catabolism" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Catabolism"> <div class="vector-toc-text"> <span class="vector-toc-numb">8.2</span> <span>Catabolism</span> </div> </a> <ul id="toc-Catabolism-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Complexation" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Complexation"> <div class="vector-toc-text"> <span class="vector-toc-numb">8.3</span> <span>Complexation</span> </div> </a> <ul id="toc-Complexation-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Chemical_analysis" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Chemical_analysis"> <div class="vector-toc-text"> <span class="vector-toc-numb">9</span> <span>Chemical analysis</span> </div> </a> <ul id="toc-Chemical_analysis-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-See_also" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#See_also"> <div class="vector-toc-text"> <span class="vector-toc-numb">10</span> <span>See also</span> </div> </a> <ul id="toc-See_also-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Notes" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Notes"> <div class="vector-toc-text"> <span class="vector-toc-numb">11</span> <span>Notes</span> </div> </a> <ul id="toc-Notes-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-References" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> <span class="vector-toc-numb">12</span> <span>References</span> </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Further_reading" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Further_reading"> <div class="vector-toc-text"> <span class="vector-toc-numb">13</span> <span>Further reading</span> </div> </a> <ul id="toc-Further_reading-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-External_links" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#External_links"> <div class="vector-toc-text"> <span class="vector-toc-numb">14</span> <span>External links</span> </div> </a> <ul id="toc-External_links-sublist" class="vector-toc-list"> </ul> </li> </ul> </div> </div> </nav> </div> </div> <div class="mw-content-container"> <main id="content" class="mw-body"> <header class="mw-body-header vector-page-titlebar"> <nav aria-label="Contents" class="vector-toc-landmark"> <div id="vector-page-titlebar-toc" class="vector-dropdown vector-page-titlebar-toc vector-button-flush-left" > <input type="checkbox" id="vector-page-titlebar-toc-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-page-titlebar-toc" class="vector-dropdown-checkbox " aria-label="Toggle the table of contents" > <label id="vector-page-titlebar-toc-label" for="vector-page-titlebar-toc-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" ><span class="vector-icon mw-ui-icon-listBullet mw-ui-icon-wikimedia-listBullet"></span> <span class="vector-dropdown-label-text">Toggle the table of contents</span> </label> <div class="vector-dropdown-content"> <div id="vector-page-titlebar-toc-unpinned-container" class="vector-unpinned-container"> </div> </div> </div> </nav> <h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">Amino acid</span></h1> <div id="p-lang-btn" class="vector-dropdown mw-portlet mw-portlet-lang" > <input type="checkbox" id="p-lang-btn-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-p-lang-btn" class="vector-dropdown-checkbox mw-interlanguage-selector" aria-label="Go to an article in another language. Available in 110 languages" > <label id="p-lang-btn-label" for="p-lang-btn-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--action-progressive mw-portlet-lang-heading-110" aria-hidden="true" ><span class="vector-icon mw-ui-icon-language-progressive mw-ui-icon-wikimedia-language-progressive"></span> <span class="vector-dropdown-label-text">110 languages</span> </label> <div class="vector-dropdown-content"> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="interlanguage-link interwiki-af mw-list-item"><a href="https://af.wikipedia.org/wiki/Aminosuur" title="Aminosuur – Afrikaans" lang="af" hreflang="af" data-title="Aminosuur" data-language-autonym="Afrikaans" data-language-local-name="Afrikaans" class="interlanguage-link-target"><span>Afrikaans</span></a></li><li class="interlanguage-link interwiki-ar mw-list-item"><a href="https://ar.wikipedia.org/wiki/%D8%AD%D9%85%D8%B6_%D8%A3%D9%85%D9%8A%D9%86%D9%8A" title="حمض أميني – Arabic" lang="ar" hreflang="ar" data-title="حمض أميني" data-language-autonym="العربية" data-language-local-name="Arabic" class="interlanguage-link-target"><span>العربية</span></a></li><li class="interlanguage-link interwiki-as mw-list-item"><a href="https://as.wikipedia.org/wiki/%E0%A6%8F%E0%A6%AE%E0%A6%BF%E0%A6%A8%E2%80%99_%E0%A6%8F%E0%A6%9B%E0%A6%BF%E0%A6%A1" title="এমিন’ এছিড – Assamese" lang="as" hreflang="as" data-title="এমিন’ এছিড" data-language-autonym="অসমীয়া" data-language-local-name="Assamese" class="interlanguage-link-target"><span>অসমীয়া</span></a></li><li class="interlanguage-link interwiki-ast mw-list-item"><a href="https://ast.wikipedia.org/wiki/Amino%C3%A1cidu" title="Aminoácidu – Asturian" lang="ast" hreflang="ast" data-title="Aminoácidu" data-language-autonym="Asturianu" data-language-local-name="Asturian" class="interlanguage-link-target"><span>Asturianu</span></a></li><li class="interlanguage-link interwiki-az mw-list-item"><a href="https://az.wikipedia.org/wiki/Amintur%C5%9Fular" title="Aminturşular – Azerbaijani" lang="az" hreflang="az" data-title="Aminturşular" data-language-autonym="Azərbaycanca" data-language-local-name="Azerbaijani" class="interlanguage-link-target"><span>Azərbaycanca</span></a></li><li class="interlanguage-link interwiki-azb mw-list-item"><a href="https://azb.wikipedia.org/wiki/%D8%A2%D9%85%DB%8C%D9%86%D9%88_%D8%A7%D8%B3%DB%8C%D8%AF" title="آمینو اسید – South Azerbaijani" lang="azb" hreflang="azb" data-title="آمینو اسید" data-language-autonym="تۆرکجه" data-language-local-name="South Azerbaijani" class="interlanguage-link-target"><span>تۆرکجه</span></a></li><li class="interlanguage-link interwiki-bn mw-list-item"><a href="https://bn.wikipedia.org/wiki/%E0%A6%85%E0%A7%8D%E0%A6%AF%E0%A6%BE%E0%A6%AE%E0%A6%BF%E0%A6%A8%E0%A7%8B_%E0%A6%85%E0%A7%8D%E0%A6%AF%E0%A6%BE%E0%A6%B8%E0%A6%BF%E0%A6%A1" title="অ্যামিনো অ্যাসিড – Bangla" lang="bn" hreflang="bn" data-title="অ্যামিনো অ্যাসিড" data-language-autonym="বাংলা" data-language-local-name="Bangla" class="interlanguage-link-target"><span>বাংলা</span></a></li><li class="interlanguage-link interwiki-zh-min-nan mw-list-item"><a href="https://zh-min-nan.wikipedia.org/wiki/An-ki-sng" title="An-ki-sng – Minnan" lang="nan" hreflang="nan" data-title="An-ki-sng" data-language-autonym="閩南語 / Bân-lâm-gú" data-language-local-name="Minnan" class="interlanguage-link-target"><span>閩南語 / Bân-lâm-gú</span></a></li><li class="interlanguage-link interwiki-be mw-list-item"><a href="https://be.wikipedia.org/wiki/%D0%90%D0%BC%D1%96%D0%BD%D0%B0%D0%BA%D1%96%D1%81%D0%BB%D0%BE%D1%82%D1%8B" title="Амінакіслоты – Belarusian" lang="be" hreflang="be" data-title="Амінакіслоты" data-language-autonym="Беларуская" data-language-local-name="Belarusian" class="interlanguage-link-target"><span>Беларуская</span></a></li><li class="interlanguage-link interwiki-be-x-old mw-list-item"><a href="https://be-tarask.wikipedia.org/wiki/%D0%90%D0%BC%D1%96%D0%BD%D0%B0%D0%BA%D1%96%D1%81%D1%8C%D0%BB%D1%96" title="Амінакісьлі – Belarusian (Taraškievica orthography)" lang="be-tarask" hreflang="be-tarask" data-title="Амінакісьлі" data-language-autonym="Беларуская (тарашкевіца)" data-language-local-name="Belarusian (Taraškievica orthography)" class="interlanguage-link-target"><span>Беларуская (тарашкевіца)</span></a></li><li class="interlanguage-link interwiki-bcl mw-list-item"><a href="https://bcl.wikipedia.org/wiki/Asidong_amino" title="Asidong amino – Central Bikol" lang="bcl" hreflang="bcl" data-title="Asidong amino" data-language-autonym="Bikol Central" data-language-local-name="Central Bikol" class="interlanguage-link-target"><span>Bikol Central</span></a></li><li class="interlanguage-link interwiki-bg mw-list-item"><a href="https://bg.wikipedia.org/wiki/%D0%90%D0%BC%D0%B8%D0%BD%D0%BE%D0%BA%D0%B8%D1%81%D0%B5%D0%BB%D0%B8%D0%BD%D0%B0" title="Аминокиселина – Bulgarian" lang="bg" hreflang="bg" data-title="Аминокиселина" data-language-autonym="Български" data-language-local-name="Bulgarian" class="interlanguage-link-target"><span>Български</span></a></li><li class="interlanguage-link interwiki-bs mw-list-item"><a href="https://bs.wikipedia.org/wiki/Aminokiselina" title="Aminokiselina – Bosnian" lang="bs" hreflang="bs" data-title="Aminokiselina" data-language-autonym="Bosanski" data-language-local-name="Bosnian" class="interlanguage-link-target"><span>Bosanski</span></a></li><li class="interlanguage-link interwiki-ca mw-list-item"><a href="https://ca.wikipedia.org/wiki/Amino%C3%A0cid" title="Aminoàcid – Catalan" lang="ca" hreflang="ca" data-title="Aminoàcid" data-language-autonym="Català" data-language-local-name="Catalan" class="interlanguage-link-target"><span>Català</span></a></li><li class="interlanguage-link interwiki-cv mw-list-item"><a href="https://cv.wikipedia.org/wiki/%D0%90%D0%BC%D0%B8%D0%BD%D0%BE%D0%B9%D3%B3%C3%A7%D0%B5%D0%BA" title="Аминойӳçек – Chuvash" lang="cv" hreflang="cv" data-title="Аминойӳçек" data-language-autonym="Чӑвашла" data-language-local-name="Chuvash" class="interlanguage-link-target"><span>Чӑвашла</span></a></li><li class="interlanguage-link interwiki-cs mw-list-item"><a href="https://cs.wikipedia.org/wiki/Aminokyselina" title="Aminokyselina – Czech" lang="cs" hreflang="cs" data-title="Aminokyselina" data-language-autonym="Čeština" data-language-local-name="Czech" class="interlanguage-link-target"><span>Čeština</span></a></li><li class="interlanguage-link interwiki-cy mw-list-item"><a href="https://cy.wikipedia.org/wiki/Asid_amino" title="Asid amino – Welsh" lang="cy" hreflang="cy" data-title="Asid amino" data-language-autonym="Cymraeg" data-language-local-name="Welsh" class="interlanguage-link-target"><span>Cymraeg</span></a></li><li class="interlanguage-link interwiki-da mw-list-item"><a href="https://da.wikipedia.org/wiki/Aminosyre" title="Aminosyre – Danish" lang="da" hreflang="da" data-title="Aminosyre" data-language-autonym="Dansk" data-language-local-name="Danish" class="interlanguage-link-target"><span>Dansk</span></a></li><li class="interlanguage-link interwiki-se mw-list-item"><a href="https://se.wikipedia.org/wiki/Aminosivra" title="Aminosivra – Northern Sami" lang="se" hreflang="se" data-title="Aminosivra" data-language-autonym="Davvisámegiella" data-language-local-name="Northern Sami" class="interlanguage-link-target"><span>Davvisámegiella</span></a></li><li class="interlanguage-link interwiki-de mw-list-item"><a href="https://de.wikipedia.org/wiki/Aminos%C3%A4uren" title="Aminosäuren – German" lang="de" hreflang="de" data-title="Aminosäuren" data-language-autonym="Deutsch" data-language-local-name="German" class="interlanguage-link-target"><span>Deutsch</span></a></li><li class="interlanguage-link interwiki-et mw-list-item"><a href="https://et.wikipedia.org/wiki/Aminohapped" title="Aminohapped – Estonian" lang="et" hreflang="et" data-title="Aminohapped" data-language-autonym="Eesti" data-language-local-name="Estonian" class="interlanguage-link-target"><span>Eesti</span></a></li><li class="interlanguage-link interwiki-el mw-list-item"><a href="https://el.wikipedia.org/wiki/%CE%91%CE%BC%CE%B9%CE%BD%CE%BF%CE%BE%CE%AD%CE%B1" title="Αμινοξέα – Greek" lang="el" hreflang="el" data-title="Αμινοξέα" data-language-autonym="Ελληνικά" data-language-local-name="Greek" class="interlanguage-link-target"><span>Ελληνικά</span></a></li><li class="interlanguage-link interwiki-es mw-list-item"><a href="https://es.wikipedia.org/wiki/Amino%C3%A1cido" title="Aminoácido – Spanish" lang="es" hreflang="es" data-title="Aminoácido" data-language-autonym="Español" data-language-local-name="Spanish" class="interlanguage-link-target"><span>Español</span></a></li><li class="interlanguage-link interwiki-eo mw-list-item"><a href="https://eo.wikipedia.org/wiki/Aminoacido" title="Aminoacido – Esperanto" lang="eo" hreflang="eo" data-title="Aminoacido" data-language-autonym="Esperanto" data-language-local-name="Esperanto" class="interlanguage-link-target"><span>Esperanto</span></a></li><li class="interlanguage-link interwiki-eu mw-list-item"><a href="https://eu.wikipedia.org/wiki/Aminoazido" title="Aminoazido – Basque" lang="eu" hreflang="eu" data-title="Aminoazido" data-language-autonym="Euskara" data-language-local-name="Basque" class="interlanguage-link-target"><span>Euskara</span></a></li><li class="interlanguage-link interwiki-fa mw-list-item"><a href="https://fa.wikipedia.org/wiki/%D8%A2%D9%85%DB%8C%D9%86%D9%88_%D8%A7%D8%B3%DB%8C%D8%AF" title="آمینو اسید – Persian" lang="fa" hreflang="fa" data-title="آمینو اسید" data-language-autonym="فارسی" data-language-local-name="Persian" class="interlanguage-link-target"><span>فارسی</span></a></li><li class="interlanguage-link interwiki-fo mw-list-item"><a href="https://fo.wikipedia.org/wiki/Aminos%C3%BDra" title="Aminosýra – Faroese" lang="fo" hreflang="fo" data-title="Aminosýra" data-language-autonym="Føroyskt" data-language-local-name="Faroese" class="interlanguage-link-target"><span>Føroyskt</span></a></li><li class="interlanguage-link interwiki-fr mw-list-item"><a href="https://fr.wikipedia.org/wiki/Acide_amin%C3%A9" title="Acide aminé – French" lang="fr" hreflang="fr" data-title="Acide aminé" data-language-autonym="Français" data-language-local-name="French" class="interlanguage-link-target"><span>Français</span></a></li><li class="interlanguage-link interwiki-ga mw-list-item"><a href="https://ga.wikipedia.org/wiki/Aim%C3%ADonaig%C3%A9ad" title="Aimíonaigéad – Irish" lang="ga" hreflang="ga" data-title="Aimíonaigéad" data-language-autonym="Gaeilge" data-language-local-name="Irish" class="interlanguage-link-target"><span>Gaeilge</span></a></li><li class="interlanguage-link interwiki-gl mw-list-item"><a href="https://gl.wikipedia.org/wiki/Amino%C3%A1cido" title="Aminoácido – Galician" lang="gl" hreflang="gl" data-title="Aminoácido" data-language-autonym="Galego" data-language-local-name="Galician" class="interlanguage-link-target"><span>Galego</span></a></li><li class="interlanguage-link interwiki-hak mw-list-item"><a href="https://hak.wikipedia.org/wiki/%C3%94n-k%C3%AE-s%C3%B4n" title="Ôn-kî-sôn – Hakka Chinese" lang="hak" hreflang="hak" data-title="Ôn-kî-sôn" data-language-autonym="客家語 / Hak-kâ-ngî" data-language-local-name="Hakka Chinese" class="interlanguage-link-target"><span>客家語 / Hak-kâ-ngî</span></a></li><li class="interlanguage-link interwiki-ko mw-list-item"><a href="https://ko.wikipedia.org/wiki/%EC%95%84%EB%AF%B8%EB%85%B8%EC%82%B0" title="아미노산 – Korean" lang="ko" hreflang="ko" data-title="아미노산" data-language-autonym="한국어" data-language-local-name="Korean" class="interlanguage-link-target"><span>한국어</span></a></li><li class="interlanguage-link interwiki-ha mw-list-item"><a href="https://ha.wikipedia.org/wiki/Amino_acid" title="Amino acid – Hausa" lang="ha" hreflang="ha" data-title="Amino acid" data-language-autonym="Hausa" data-language-local-name="Hausa" class="interlanguage-link-target"><span>Hausa</span></a></li><li class="interlanguage-link interwiki-hy mw-list-item"><a href="https://hy.wikipedia.org/wiki/%D4%B1%D5%B4%D5%AB%D5%B6%D5%A1%D5%A9%D5%A9%D5%B8%D6%82" title="Ամինաթթու – Armenian" lang="hy" hreflang="hy" data-title="Ամինաթթու" data-language-autonym="Հայերեն" data-language-local-name="Armenian" class="interlanguage-link-target"><span>Հայերեն</span></a></li><li class="interlanguage-link interwiki-hi mw-list-item"><a href="https://hi.wikipedia.org/wiki/%E0%A4%85%E0%A4%AE%E0%A5%80%E0%A4%A8%E0%A5%8B_%E0%A4%85%E0%A4%AE%E0%A5%8D%E0%A4%B2" title="अमीनो अम्ल – Hindi" lang="hi" hreflang="hi" data-title="अमीनो अम्ल" data-language-autonym="हिन्दी" data-language-local-name="Hindi" class="interlanguage-link-target"><span>हिन्दी</span></a></li><li class="interlanguage-link interwiki-hr mw-list-item"><a href="https://hr.wikipedia.org/wiki/Aminokiselina" title="Aminokiselina – Croatian" lang="hr" hreflang="hr" data-title="Aminokiselina" data-language-autonym="Hrvatski" data-language-local-name="Croatian" class="interlanguage-link-target"><span>Hrvatski</span></a></li><li class="interlanguage-link interwiki-io mw-list-item"><a href="https://io.wikipedia.org/wiki/Aminoacido" title="Aminoacido – Ido" lang="io" hreflang="io" data-title="Aminoacido" data-language-autonym="Ido" data-language-local-name="Ido" class="interlanguage-link-target"><span>Ido</span></a></li><li class="interlanguage-link interwiki-id mw-list-item"><a href="https://id.wikipedia.org/wiki/Asam_amino" title="Asam amino – Indonesian" lang="id" hreflang="id" data-title="Asam amino" data-language-autonym="Bahasa Indonesia" data-language-local-name="Indonesian" class="interlanguage-link-target"><span>Bahasa Indonesia</span></a></li><li class="interlanguage-link interwiki-ia mw-list-item"><a href="https://ia.wikipedia.org/wiki/Aminoacido" title="Aminoacido – Interlingua" lang="ia" hreflang="ia" data-title="Aminoacido" data-language-autonym="Interlingua" data-language-local-name="Interlingua" class="interlanguage-link-target"><span>Interlingua</span></a></li><li class="interlanguage-link interwiki-is mw-list-item"><a href="https://is.wikipedia.org/wiki/Am%C3%ADn%C3%B3s%C3%BDra" title="Amínósýra – Icelandic" lang="is" hreflang="is" data-title="Amínósýra" data-language-autonym="Íslenska" data-language-local-name="Icelandic" class="interlanguage-link-target"><span>Íslenska</span></a></li><li class="interlanguage-link interwiki-it mw-list-item"><a href="https://it.wikipedia.org/wiki/Amminoacido" title="Amminoacido – Italian" lang="it" hreflang="it" data-title="Amminoacido" data-language-autonym="Italiano" data-language-local-name="Italian" class="interlanguage-link-target"><span>Italiano</span></a></li><li class="interlanguage-link interwiki-he mw-list-item"><a href="https://he.wikipedia.org/wiki/%D7%97%D7%95%D7%9E%D7%A6%D7%AA_%D7%90%D7%9E%D7%99%D7%A0%D7%95" title="חומצת אמינו – Hebrew" lang="he" hreflang="he" data-title="חומצת אמינו" data-language-autonym="עברית" data-language-local-name="Hebrew" class="interlanguage-link-target"><span>עברית</span></a></li><li class="interlanguage-link interwiki-jv mw-list-item"><a href="https://jv.wikipedia.org/wiki/Asem_amino" title="Asem amino – Javanese" lang="jv" hreflang="jv" data-title="Asem amino" data-language-autonym="Jawa" data-language-local-name="Javanese" class="interlanguage-link-target"><span>Jawa</span></a></li><li class="interlanguage-link interwiki-kn mw-list-item"><a href="https://kn.wikipedia.org/wiki/%E0%B2%85%E0%B2%AE%E0%B2%BF%E0%B2%A8%E0%B3%8A_%E0%B2%86%E0%B2%AE%E0%B3%8D%E0%B2%B2" title="ಅಮಿನೊ ಆಮ್ಲ – Kannada" lang="kn" hreflang="kn" data-title="ಅಮಿನೊ ಆಮ್ಲ" data-language-autonym="ಕನ್ನಡ" data-language-local-name="Kannada" class="interlanguage-link-target"><span>ಕನ್ನಡ</span></a></li><li class="interlanguage-link interwiki-ka mw-list-item"><a href="https://ka.wikipedia.org/wiki/%E1%83%90%E1%83%9B%E1%83%98%E1%83%9C%E1%83%9D%E1%83%9B%E1%83%9F%E1%83%90%E1%83%95%E1%83%94%E1%83%91%E1%83%98" title="ამინომჟავები – Georgian" lang="ka" hreflang="ka" data-title="ამინომჟავები" data-language-autonym="ქართული" data-language-local-name="Georgian" class="interlanguage-link-target"><span>ქართული</span></a></li><li class="interlanguage-link interwiki-ks mw-list-item"><a href="https://ks.wikipedia.org/wiki/%D8%A7%D9%8E%D9%85%D9%8E%DB%8C%D9%86%D9%88_%D8%A7%DB%8C%D8%B3%D9%90%DA%88" title="اَمَینو ایسِڈ – Kashmiri" lang="ks" hreflang="ks" data-title="اَمَینو ایسِڈ" data-language-autonym="कॉशुर / کٲشُر" data-language-local-name="Kashmiri" class="interlanguage-link-target"><span>कॉशुर / کٲشُر</span></a></li><li class="interlanguage-link interwiki-kk mw-list-item"><a href="https://kk.wikipedia.org/wiki/%D0%90%D0%BC%D0%B8%D0%BD%D2%9B%D1%8B%D1%88%D2%9B%D1%8B%D0%BB%D0%B4%D0%B0%D1%80" title="Аминқышқылдар – Kazakh" lang="kk" hreflang="kk" data-title="Аминқышқылдар" data-language-autonym="Қазақша" data-language-local-name="Kazakh" class="interlanguage-link-target"><span>Қазақша</span></a></li><li class="interlanguage-link interwiki-sw mw-list-item"><a href="https://sw.wikipedia.org/wiki/Asidi_amino" title="Asidi amino – Swahili" lang="sw" hreflang="sw" data-title="Asidi amino" data-language-autonym="Kiswahili" data-language-local-name="Swahili" class="interlanguage-link-target"><span>Kiswahili</span></a></li><li class="interlanguage-link interwiki-ht mw-list-item"><a href="https://ht.wikipedia.org/wiki/Asid_amine" title="Asid amine – Haitian Creole" lang="ht" hreflang="ht" data-title="Asid amine" data-language-autonym="Kreyòl ayisyen" data-language-local-name="Haitian Creole" class="interlanguage-link-target"><span>Kreyòl ayisyen</span></a></li><li class="interlanguage-link interwiki-ku mw-list-item"><a href="https://ku.wikipedia.org/wiki/As%C3%AEda_am%C3%AEn%C3%AE" title="Asîda amînî – Kurdish" lang="ku" hreflang="ku" data-title="Asîda amînî" data-language-autonym="Kurdî" data-language-local-name="Kurdish" class="interlanguage-link-target"><span>Kurdî</span></a></li><li class="interlanguage-link interwiki-ky mw-list-item"><a href="https://ky.wikipedia.org/wiki/%D0%90%D0%BC%D0%B8%D0%BD_%D0%BA%D1%8B%D1%87%D0%BA%D1%8B%D0%BB%D0%B4%D1%8B%D0%BA%D1%82%D0%B0%D1%80%D1%8B_(%D0%B0%D0%BC%D0%B8%D0%BD%D0%BE%D0%BA%D0%B8%D1%81%D0%BB%D0%BE%D1%82%D0%B0)" title="Амин кычкылдыктары (аминокислота) – Kyrgyz" lang="ky" hreflang="ky" data-title="Амин кычкылдыктары (аминокислота)" data-language-autonym="Кыргызча" data-language-local-name="Kyrgyz" class="interlanguage-link-target"><span>Кыргызча</span></a></li><li class="interlanguage-link interwiki-la mw-list-item"><a href="https://la.wikipedia.org/wiki/Aminoacidum" title="Aminoacidum – Latin" lang="la" hreflang="la" data-title="Aminoacidum" data-language-autonym="Latina" data-language-local-name="Latin" class="interlanguage-link-target"><span>Latina</span></a></li><li class="interlanguage-link interwiki-lv mw-list-item"><a href="https://lv.wikipedia.org/wiki/Aminosk%C4%81bes" title="Aminoskābes – Latvian" lang="lv" hreflang="lv" data-title="Aminoskābes" data-language-autonym="Latviešu" data-language-local-name="Latvian" class="interlanguage-link-target"><span>Latviešu</span></a></li><li class="interlanguage-link interwiki-lb mw-list-item"><a href="https://lb.wikipedia.org/wiki/Aminosaier" title="Aminosaier – Luxembourgish" lang="lb" hreflang="lb" data-title="Aminosaier" data-language-autonym="Lëtzebuergesch" data-language-local-name="Luxembourgish" class="interlanguage-link-target"><span>Lëtzebuergesch</span></a></li><li class="interlanguage-link interwiki-lt mw-list-item"><a href="https://lt.wikipedia.org/wiki/Aminor%C5%ABg%C5%A1tys" title="Aminorūgštys – Lithuanian" lang="lt" hreflang="lt" data-title="Aminorūgštys" data-language-autonym="Lietuvių" data-language-local-name="Lithuanian" class="interlanguage-link-target"><span>Lietuvių</span></a></li><li class="interlanguage-link interwiki-li mw-list-item"><a href="https://li.wikipedia.org/wiki/Aminozoer" title="Aminozoer – Limburgish" lang="li" hreflang="li" data-title="Aminozoer" data-language-autonym="Limburgs" data-language-local-name="Limburgish" class="interlanguage-link-target"><span>Limburgs</span></a></li><li class="interlanguage-link interwiki-lmo mw-list-item"><a href="https://lmo.wikipedia.org/wiki/Aminuacid" title="Aminuacid – Lombard" lang="lmo" hreflang="lmo" data-title="Aminuacid" data-language-autonym="Lombard" data-language-local-name="Lombard" class="interlanguage-link-target"><span>Lombard</span></a></li><li class="interlanguage-link interwiki-hu mw-list-item"><a href="https://hu.wikipedia.org/wiki/Aminosavak" title="Aminosavak – Hungarian" lang="hu" hreflang="hu" data-title="Aminosavak" data-language-autonym="Magyar" data-language-local-name="Hungarian" class="interlanguage-link-target"><span>Magyar</span></a></li><li class="interlanguage-link interwiki-mk mw-list-item"><a href="https://mk.wikipedia.org/wiki/%D0%90%D0%BC%D0%B8%D0%BD%D0%BE%D0%BA%D0%B8%D1%81%D0%B5%D0%BB%D0%B8%D0%BD%D0%B0" title="Аминокиселина – Macedonian" lang="mk" hreflang="mk" data-title="Аминокиселина" data-language-autonym="Македонски" data-language-local-name="Macedonian" class="interlanguage-link-target"><span>Македонски</span></a></li><li class="interlanguage-link interwiki-ml mw-list-item"><a href="https://ml.wikipedia.org/wiki/%E0%B4%85%E0%B4%AE%E0%B4%BF%E0%B4%A8%E0%B5%8B_%E0%B4%85%E0%B4%AE%E0%B5%8D%E0%B4%B2%E0%B4%82" title="അമിനോ അമ്ലം – Malayalam" lang="ml" hreflang="ml" data-title="അമിനോ അമ്ലം" data-language-autonym="മലയാളം" data-language-local-name="Malayalam" class="interlanguage-link-target"><span>മലയാളം</span></a></li><li class="interlanguage-link interwiki-mr mw-list-item"><a href="https://mr.wikipedia.org/wiki/%E0%A4%85%E0%A4%AE%E0%A4%BF%E0%A4%A8%E0%A5%8B_%E0%A4%86%E0%A4%AE%E0%A5%8D%E0%A4%B2" title="अमिनो आम्ल – Marathi" lang="mr" hreflang="mr" data-title="अमिनो आम्ल" data-language-autonym="मराठी" data-language-local-name="Marathi" class="interlanguage-link-target"><span>मराठी</span></a></li><li class="interlanguage-link interwiki-ms mw-list-item"><a href="https://ms.wikipedia.org/wiki/Asid_amino" title="Asid amino – Malay" lang="ms" hreflang="ms" data-title="Asid amino" data-language-autonym="Bahasa Melayu" data-language-local-name="Malay" class="interlanguage-link-target"><span>Bahasa Melayu</span></a></li><li class="interlanguage-link interwiki-mn mw-list-item"><a href="https://mn.wikipedia.org/wiki/%D0%90%D0%BC%D0%B8%D0%BD_%D1%85%D2%AF%D1%87%D0%B8%D0%BB" title="Амин хүчил – Mongolian" lang="mn" hreflang="mn" data-title="Амин хүчил" data-language-autonym="Монгол" data-language-local-name="Mongolian" class="interlanguage-link-target"><span>Монгол</span></a></li><li class="interlanguage-link interwiki-nl mw-list-item"><a href="https://nl.wikipedia.org/wiki/Aminozuur" title="Aminozuur – Dutch" lang="nl" hreflang="nl" data-title="Aminozuur" data-language-autonym="Nederlands" data-language-local-name="Dutch" class="interlanguage-link-target"><span>Nederlands</span></a></li><li class="interlanguage-link interwiki-ja mw-list-item"><a href="https://ja.wikipedia.org/wiki/%E3%82%A2%E3%83%9F%E3%83%8E%E9%85%B8" title="アミノ酸 – Japanese" lang="ja" hreflang="ja" data-title="アミノ酸" data-language-autonym="日本語" data-language-local-name="Japanese" class="interlanguage-link-target"><span>日本語</span></a></li><li class="interlanguage-link interwiki-frr mw-list-item"><a href="https://frr.wikipedia.org/wiki/Aminos%C3%BCren" title="Aminosüren – Northern Frisian" lang="frr" hreflang="frr" data-title="Aminosüren" data-language-autonym="Nordfriisk" data-language-local-name="Northern Frisian" class="interlanguage-link-target"><span>Nordfriisk</span></a></li><li class="interlanguage-link interwiki-no mw-list-item"><a href="https://no.wikipedia.org/wiki/Aminosyre" title="Aminosyre – Norwegian Bokmål" lang="nb" hreflang="nb" data-title="Aminosyre" data-language-autonym="Norsk bokmål" data-language-local-name="Norwegian Bokmål" class="interlanguage-link-target"><span>Norsk bokmål</span></a></li><li class="interlanguage-link interwiki-nn mw-list-item"><a href="https://nn.wikipedia.org/wiki/Aminosyre" title="Aminosyre – Norwegian Nynorsk" lang="nn" hreflang="nn" data-title="Aminosyre" data-language-autonym="Norsk nynorsk" data-language-local-name="Norwegian Nynorsk" class="interlanguage-link-target"><span>Norsk nynorsk</span></a></li><li class="interlanguage-link interwiki-nov mw-list-item"><a href="https://nov.wikipedia.org/wiki/Amino-aside" title="Amino-aside – Novial" lang="nov" hreflang="nov" data-title="Amino-aside" data-language-autonym="Novial" data-language-local-name="Novial" class="interlanguage-link-target"><span>Novial</span></a></li><li class="interlanguage-link interwiki-oc mw-list-item"><a href="https://oc.wikipedia.org/wiki/Aminoacid" title="Aminoacid – Occitan" lang="oc" hreflang="oc" data-title="Aminoacid" data-language-autonym="Occitan" data-language-local-name="Occitan" class="interlanguage-link-target"><span>Occitan</span></a></li><li class="interlanguage-link interwiki-om mw-list-item"><a href="https://om.wikipedia.org/wiki/Aminoo_Asidii" title="Aminoo Asidii – Oromo" lang="om" hreflang="om" data-title="Aminoo Asidii" data-language-autonym="Oromoo" data-language-local-name="Oromo" class="interlanguage-link-target"><span>Oromoo</span></a></li><li class="interlanguage-link interwiki-uz mw-list-item"><a href="https://uz.wikipedia.org/wiki/Aminokislotalar" title="Aminokislotalar – Uzbek" lang="uz" hreflang="uz" data-title="Aminokislotalar" data-language-autonym="Oʻzbekcha / ўзбекча" data-language-local-name="Uzbek" class="interlanguage-link-target"><span>Oʻzbekcha / ўзбекча</span></a></li><li class="interlanguage-link interwiki-pa mw-list-item"><a href="https://pa.wikipedia.org/wiki/%E0%A8%85%E0%A8%AE%E0%A9%80%E0%A8%A8%E0%A9%8B_%E0%A8%A4%E0%A8%BF%E0%A8%9C%E0%A8%BC%E0%A8%BE%E0%A8%AC" title="ਅਮੀਨੋ ਤਿਜ਼ਾਬ – Punjabi" lang="pa" hreflang="pa" data-title="ਅਮੀਨੋ ਤਿਜ਼ਾਬ" data-language-autonym="ਪੰਜਾਬੀ" data-language-local-name="Punjabi" class="interlanguage-link-target"><span>ਪੰਜਾਬੀ</span></a></li><li class="interlanguage-link interwiki-pnb mw-list-item"><a href="https://pnb.wikipedia.org/wiki/%D8%A7%D9%85%DB%8C%D9%86%D9%88_%D8%A7%DB%8C%D8%B3%DA%88" title="امینو ایسڈ – Western Punjabi" lang="pnb" hreflang="pnb" data-title="امینو ایسڈ" data-language-autonym="پنجابی" data-language-local-name="Western Punjabi" class="interlanguage-link-target"><span>پنجابی</span></a></li><li class="interlanguage-link interwiki-ps mw-list-item"><a href="https://ps.wikipedia.org/wiki/%D8%A7%D9%85%D9%8A%D9%86%D9%88_%D8%A7%D8%B3%D9%8A%D8%AF" title="امينو اسيد – Pashto" lang="ps" hreflang="ps" data-title="امينو اسيد" data-language-autonym="پښتو" data-language-local-name="Pashto" class="interlanguage-link-target"><span>پښتو</span></a></li><li class="interlanguage-link interwiki-km mw-list-item"><a href="https://km.wikipedia.org/wiki/%E1%9E%A2%E1%9E%B6%E1%9E%9F%E1%9F%8A%E1%9E%B8%E1%9E%8F%E1%9E%A2%E1%9E%B6%E1%9E%98%E1%9E%B8%E1%9E%93%E1%9F%81" title="អាស៊ីតអាមីនេ – Khmer" lang="km" hreflang="km" data-title="អាស៊ីតអាមីនេ" data-language-autonym="ភាសាខ្មែរ" data-language-local-name="Khmer" class="interlanguage-link-target"><span>ភាសាខ្មែរ</span></a></li><li class="interlanguage-link interwiki-pl mw-list-item"><a href="https://pl.wikipedia.org/wiki/Aminokwasy" title="Aminokwasy – Polish" lang="pl" hreflang="pl" data-title="Aminokwasy" data-language-autonym="Polski" data-language-local-name="Polish" class="interlanguage-link-target"><span>Polski</span></a></li><li class="interlanguage-link interwiki-pt mw-list-item"><a href="https://pt.wikipedia.org/wiki/Amino%C3%A1cido" title="Aminoácido – Portuguese" lang="pt" hreflang="pt" data-title="Aminoácido" data-language-autonym="Português" data-language-local-name="Portuguese" class="interlanguage-link-target"><span>Português</span></a></li><li class="interlanguage-link interwiki-kaa mw-list-item"><a href="https://kaa.wikipedia.org/wiki/Aminokislotalar" title="Aminokislotalar – Kara-Kalpak" lang="kaa" hreflang="kaa" data-title="Aminokislotalar" data-language-autonym="Qaraqalpaqsha" data-language-local-name="Kara-Kalpak" class="interlanguage-link-target"><span>Qaraqalpaqsha</span></a></li><li class="interlanguage-link interwiki-ro mw-list-item"><a href="https://ro.wikipedia.org/wiki/Aminoacid" title="Aminoacid – Romanian" lang="ro" hreflang="ro" data-title="Aminoacid" data-language-autonym="Română" data-language-local-name="Romanian" class="interlanguage-link-target"><span>Română</span></a></li><li class="interlanguage-link interwiki-ru mw-list-item"><a href="https://ru.wikipedia.org/wiki/%D0%90%D0%BC%D0%B8%D0%BD%D0%BE%D0%BA%D0%B8%D1%81%D0%BB%D0%BE%D1%82%D1%8B" title="Аминокислоты – Russian" lang="ru" hreflang="ru" data-title="Аминокислоты" data-language-autonym="Русский" data-language-local-name="Russian" class="interlanguage-link-target"><span>Русский</span></a></li><li class="interlanguage-link interwiki-stq mw-list-item"><a href="https://stq.wikipedia.org/wiki/Aminos%C3%BC%C3%BCren" title="Aminosüüren – Saterland Frisian" lang="stq" hreflang="stq" data-title="Aminosüüren" data-language-autonym="Seeltersk" data-language-local-name="Saterland Frisian" class="interlanguage-link-target"><span>Seeltersk</span></a></li><li class="interlanguage-link interwiki-sq mw-list-item"><a href="https://sq.wikipedia.org/wiki/Aminoacidet" title="Aminoacidet – Albanian" lang="sq" hreflang="sq" data-title="Aminoacidet" data-language-autonym="Shqip" data-language-local-name="Albanian" class="interlanguage-link-target"><span>Shqip</span></a></li><li class="interlanguage-link interwiki-si mw-list-item"><a href="https://si.wikipedia.org/wiki/%E0%B6%87%E0%B6%B8%E0%B6%BA%E0%B7%92%E0%B6%B1%E0%B7%9D_%E0%B6%85%E0%B6%B8%E0%B7%8A%E0%B6%BD" title="ඇමයිනෝ අම්ල – Sinhala" lang="si" hreflang="si" data-title="ඇමයිනෝ අම්ල" data-language-autonym="සිංහල" data-language-local-name="Sinhala" class="interlanguage-link-target"><span>සිංහල</span></a></li><li class="interlanguage-link interwiki-simple mw-list-item"><a href="https://simple.wikipedia.org/wiki/Amino_acid" title="Amino acid – Simple English" lang="en-simple" hreflang="en-simple" data-title="Amino acid" data-language-autonym="Simple English" data-language-local-name="Simple English" class="interlanguage-link-target"><span>Simple English</span></a></li><li class="interlanguage-link interwiki-sk mw-list-item"><a href="https://sk.wikipedia.org/wiki/Aminokyselina" title="Aminokyselina – Slovak" lang="sk" hreflang="sk" data-title="Aminokyselina" data-language-autonym="Slovenčina" data-language-local-name="Slovak" class="interlanguage-link-target"><span>Slovenčina</span></a></li><li class="interlanguage-link interwiki-sl mw-list-item"><a href="https://sl.wikipedia.org/wiki/Aminokislina" title="Aminokislina – Slovenian" lang="sl" hreflang="sl" data-title="Aminokislina" data-language-autonym="Slovenščina" data-language-local-name="Slovenian" class="interlanguage-link-target"><span>Slovenščina</span></a></li><li class="interlanguage-link interwiki-ckb mw-list-item"><a href="https://ckb.wikipedia.org/wiki/%D8%AA%D8%B1%D8%B4%DB%8C_%D8%A6%DB%95%D9%85%DB%8C%D9%86%DB%8C" title="ترشی ئەمینی – Central Kurdish" lang="ckb" hreflang="ckb" data-title="ترشی ئەمینی" data-language-autonym="کوردی" data-language-local-name="Central Kurdish" class="interlanguage-link-target"><span>کوردی</span></a></li><li class="interlanguage-link interwiki-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/%D0%90%D0%BC%D0%B8%D0%BD%D0%BE%D0%BA%D0%B8%D1%81%D0%B5%D0%BB%D0%B8%D0%BD%D0%B0" title="Аминокиселина – Serbian" lang="sr" hreflang="sr" data-title="Аминокиселина" data-language-autonym="Српски / srpski" data-language-local-name="Serbian" class="interlanguage-link-target"><span>Српски / srpski</span></a></li><li class="interlanguage-link interwiki-sh mw-list-item"><a href="https://sh.wikipedia.org/wiki/Aminokiselina" title="Aminokiselina – Serbo-Croatian" lang="sh" hreflang="sh" data-title="Aminokiselina" data-language-autonym="Srpskohrvatski / српскохрватски" data-language-local-name="Serbo-Croatian" class="interlanguage-link-target"><span>Srpskohrvatski / српскохрватски</span></a></li><li class="interlanguage-link interwiki-su mw-list-item"><a href="https://su.wikipedia.org/wiki/Asam_amino" title="Asam amino – Sundanese" lang="su" hreflang="su" data-title="Asam amino" data-language-autonym="Sunda" data-language-local-name="Sundanese" class="interlanguage-link-target"><span>Sunda</span></a></li><li class="interlanguage-link interwiki-fi mw-list-item"><a href="https://fi.wikipedia.org/wiki/Aminohapot" title="Aminohapot – Finnish" lang="fi" hreflang="fi" data-title="Aminohapot" data-language-autonym="Suomi" data-language-local-name="Finnish" class="interlanguage-link-target"><span>Suomi</span></a></li><li class="interlanguage-link interwiki-sv mw-list-item"><a href="https://sv.wikipedia.org/wiki/Aminosyror" title="Aminosyror – Swedish" lang="sv" hreflang="sv" data-title="Aminosyror" data-language-autonym="Svenska" data-language-local-name="Swedish" class="interlanguage-link-target"><span>Svenska</span></a></li><li class="interlanguage-link interwiki-tl mw-list-item"><a href="https://tl.wikipedia.org/wiki/Asidong_amino" title="Asidong amino – Tagalog" lang="tl" hreflang="tl" data-title="Asidong amino" data-language-autonym="Tagalog" data-language-local-name="Tagalog" class="interlanguage-link-target"><span>Tagalog</span></a></li><li class="interlanguage-link interwiki-ta mw-list-item"><a href="https://ta.wikipedia.org/wiki/%E0%AE%85%E0%AE%AE%E0%AE%BF%E0%AE%A9%E0%AF%8B_%E0%AE%85%E0%AE%AE%E0%AE%BF%E0%AE%B2%E0%AE%AE%E0%AF%8D" title="அமினோ அமிலம் – Tamil" lang="ta" hreflang="ta" data-title="அமினோ அமிலம்" data-language-autonym="தமிழ்" data-language-local-name="Tamil" class="interlanguage-link-target"><span>தமிழ்</span></a></li><li class="interlanguage-link interwiki-te mw-list-item"><a href="https://te.wikipedia.org/wiki/%E0%B0%8E%E0%B0%AE%E0%B1%88%E0%B0%A8%E0%B1%8B_%E0%B0%86%E0%B0%AE%E0%B1%8D%E0%B0%B2%E0%B0%BE%E0%B0%B2%E0%B1%81" title="ఎమైనో ఆమ్లాలు – Telugu" lang="te" hreflang="te" data-title="ఎమైనో ఆమ్లాలు" data-language-autonym="తెలుగు" data-language-local-name="Telugu" class="interlanguage-link-target"><span>తెలుగు</span></a></li><li class="interlanguage-link interwiki-th mw-list-item"><a href="https://th.wikipedia.org/wiki/%E0%B8%81%E0%B8%A3%E0%B8%94%E0%B8%AD%E0%B8%B0%E0%B8%A1%E0%B8%B4%E0%B9%82%E0%B8%99" title="กรดอะมิโน – Thai" lang="th" hreflang="th" data-title="กรดอะมิโน" data-language-autonym="ไทย" data-language-local-name="Thai" class="interlanguage-link-target"><span>ไทย</span></a></li><li class="interlanguage-link interwiki-tg mw-list-item"><a href="https://tg.wikipedia.org/wiki/%D0%90%D0%BC%D0%B8%D0%BD%D0%BE%D0%BA%D0%B8%D1%81%D0%BB%D0%BE%D1%82%D0%B0%D2%B3%D0%BE" title="Аминокислотаҳо – Tajik" lang="tg" hreflang="tg" data-title="Аминокислотаҳо" data-language-autonym="Тоҷикӣ" data-language-local-name="Tajik" class="interlanguage-link-target"><span>Тоҷикӣ</span></a></li><li class="interlanguage-link interwiki-tr mw-list-item"><a href="https://tr.wikipedia.org/wiki/Amino_asit" title="Amino asit – Turkish" lang="tr" hreflang="tr" data-title="Amino asit" data-language-autonym="Türkçe" data-language-local-name="Turkish" class="interlanguage-link-target"><span>Türkçe</span></a></li><li class="interlanguage-link interwiki-uk mw-list-item"><a href="https://uk.wikipedia.org/wiki/%D0%90%D0%BC%D1%96%D0%BD%D0%BE%D0%BA%D0%B8%D1%81%D0%BB%D0%BE%D1%82%D0%B8" title="Амінокислоти – Ukrainian" lang="uk" hreflang="uk" data-title="Амінокислоти" data-language-autonym="Українська" data-language-local-name="Ukrainian" class="interlanguage-link-target"><span>Українська</span></a></li><li class="interlanguage-link interwiki-ur mw-list-item"><a href="https://ur.wikipedia.org/wiki/%D8%A7%D9%85%DB%8C%D9%86%D9%88_%D8%A7%DB%8C%D8%B3%DA%88" title="امینو ایسڈ – Urdu" lang="ur" hreflang="ur" data-title="امینو ایسڈ" data-language-autonym="اردو" data-language-local-name="Urdu" class="interlanguage-link-target"><span>اردو</span></a></li><li class="interlanguage-link interwiki-vi mw-list-item"><a href="https://vi.wikipedia.org/wiki/Amino_acid" title="Amino acid – Vietnamese" lang="vi" hreflang="vi" data-title="Amino acid" data-language-autonym="Tiếng Việt" data-language-local-name="Vietnamese" class="interlanguage-link-target"><span>Tiếng Việt</span></a></li><li class="interlanguage-link interwiki-zh-classical mw-list-item"><a href="https://zh-classical.wikipedia.org/wiki/%E6%B0%A8%E5%9F%BA%E9%85%B8" title="氨基酸 – Literary Chinese" lang="lzh" hreflang="lzh" data-title="氨基酸" data-language-autonym="文言" data-language-local-name="Literary Chinese" class="interlanguage-link-target"><span>文言</span></a></li><li class="interlanguage-link interwiki-vls mw-list-item"><a href="https://vls.wikipedia.org/wiki/Aminozuur" title="Aminozuur – West Flemish" lang="vls" hreflang="vls" data-title="Aminozuur" data-language-autonym="West-Vlams" data-language-local-name="West Flemish" class="interlanguage-link-target"><span>West-Vlams</span></a></li><li class="interlanguage-link interwiki-war mw-list-item"><a href="https://war.wikipedia.org/wiki/Aminoasido" title="Aminoasido – Waray" lang="war" hreflang="war" 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Click here for more information."><img alt="This is a good article. Click here for more information." src="//upload.wikimedia.org/wikipedia/en/thumb/9/94/Symbol_support_vote.svg/19px-Symbol_support_vote.svg.png" decoding="async" width="19" height="20" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/9/94/Symbol_support_vote.svg/29px-Symbol_support_vote.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/9/94/Symbol_support_vote.svg/39px-Symbol_support_vote.svg.png 2x" data-file-width="180" data-file-height="185" /></a></span></div></div> </div> <div id="siteSub" class="noprint">From Wikipedia, the free encyclopedia</div> </div> <div id="contentSub"><div id="mw-content-subtitle"></div></div> <div id="mw-content-text" class="mw-body-content"><div class="mw-content-ltr mw-parser-output" lang="en" dir="ltr"><div class="shortdescription nomobile noexcerpt noprint searchaux" style="display:none">Organic compounds containing amine and carboxylic groups</div> <style data-mw-deduplicate="TemplateStyles:r1236090951">.mw-parser-output .hatnote{font-style:italic}.mw-parser-output div.hatnote{padding-left:1.6em;margin-bottom:0.5em}.mw-parser-output .hatnote i{font-style:normal}.mw-parser-output .hatnote+link+.hatnote{margin-top:-0.5em}@media print{body.ns-0 .mw-parser-output .hatnote{display:none!important}}</style><div role="note" class="hatnote navigation-not-searchable">This article is about the class of chemicals. For the structures and properties of the standard proteinogenic amino acids, see <a href="/wiki/Proteinogenic_amino_acid" title="Proteinogenic amino acid">Proteinogenic amino acid</a>.</div> <p class="mw-empty-elt"> </p> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:L-amino_acid_structure.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/5/51/L-amino_acid_structure.svg/220px-L-amino_acid_structure.svg.png" decoding="async" width="220" height="144" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/5/51/L-amino_acid_structure.svg/330px-L-amino_acid_structure.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/5/51/L-amino_acid_structure.svg/440px-L-amino_acid_structure.svg.png 2x" data-file-width="128" data-file-height="84" /></a><figcaption>Structure of a typical <small>L</small>-alpha-amino acid in the "neutral" form</figcaption></figure> <p><b>Amino acids</b> are <a href="/wiki/Organic_compound" title="Organic compound">organic compounds</a> that contain both <a href="/wiki/Amino" class="mw-redirect" title="Amino">amino</a> and <a href="/wiki/Carboxylic_acid" title="Carboxylic acid">carboxylic acid</a> <a href="/wiki/Functional_group" title="Functional group">functional groups</a>.<sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> Although over 500 amino acids exist in nature, by far the most important are the <a href="/wiki/Proteinogenic_amino_acid" title="Proteinogenic amino acid">22 α-amino acids</a> incorporated into <a href="/wiki/Protein" title="Protein">proteins</a>.<sup id="cite_ref-2" class="reference"><a href="#cite_note-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> Only these 22 appear in the <a href="/wiki/Genetic_code" title="Genetic code">genetic code</a> of life.<sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid20847933_4-0" class="reference"><a href="#cite_note-pmid20847933-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> </p><p>Amino acids can be classified according to the locations of the core structural functional groups (<a href="/wiki/Alpha_and_beta_carbon" class="mw-redirect" title="Alpha and beta carbon">alpha- <span style="white-space: nowrap">(α-)</span>, beta- <span style="white-space: nowrap">(β-)</span>, gamma- <span style="white-space: nowrap">(γ-)</span></a> amino acids, etc.); other categories relate to <a href="/wiki/Chemical_polarity" title="Chemical polarity">polarity</a>, <a href="/wiki/Ionization" title="Ionization">ionization</a>, and side-chain group type (<a href="/wiki/Aliphatic" class="mw-redirect" title="Aliphatic">aliphatic</a>, <a href="/wiki/Open-chain_compound" title="Open-chain compound">acyclic</a>, <a href="/wiki/Aromatic" class="mw-redirect" title="Aromatic">aromatic</a>, <a href="/wiki/Chemical_polarity" title="Chemical polarity">polar</a>, etc.). In the form of proteins, amino-acid <i><a href="/wiki/Residue_(chemistry)#Biochemistry" title="Residue (chemistry)">residues</a></i> form the second-largest component (<a href="/wiki/Water" title="Water">water</a> being the largest) of human <a href="/wiki/Muscle" title="Muscle">muscles</a> and other <a href="/wiki/Tissue_(biology)" title="Tissue (biology)">tissues</a>.<sup id="cite_ref-5" class="reference"><a href="#cite_note-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> Beyond their role as residues in proteins, amino acids participate in a number of processes such as <a href="/wiki/Neurotransmitter" title="Neurotransmitter">neurotransmitter</a> transport and <a href="/wiki/Biosynthesis" title="Biosynthesis">biosynthesis</a>. It is thought that they played a key role in <a href="/wiki/Abiogenesis" title="Abiogenesis">enabling life on Earth and its emergence</a>.<sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> </p><p>Amino acids are formally named by the <a href="/wiki/International_Union_of_Pure_and_Applied_Chemistry" title="International Union of Pure and Applied Chemistry">IUPAC</a>-<a href="/wiki/International_Union_of_Biochemistry_and_Molecular_Biology" title="International Union of Biochemistry and Molecular Biology">IUBMB</a> <a href="/wiki/Joint_Commission" title="Joint Commission">Joint Commission</a> on Biochemical Nomenclature in terms of the fictitious "neutral" structure shown in the illustration. For example, the systematic name of alanine is 2-aminopropanoic acid, based on the formula <style data-mw-deduplicate="TemplateStyles:r1123817410">.mw-parser-output .template-chem2-su{display:inline-block;font-size:80%;line-height:1;vertical-align:-0.35em}.mw-parser-output .template-chem2-su>span{display:block;text-align:left}.mw-parser-output sub.template-chem2-sub{font-size:80%;vertical-align:-0.35em}.mw-parser-output sup.template-chem2-sup{font-size:80%;vertical-align:0.65em}</style><span class="chemf nowrap">CH<sub class="template-chem2-sub">3</sub>−CH(NH<sub class="template-chem2-sub">2</sub>)−COOH</span>. The Commission justified this approach as follows:<sup id="cite_ref-iupaciub_7-0" class="reference"><a href="#cite_note-iupaciub-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> </p> <blockquote><p>The systematic names and formulas given refer to hypothetical forms in which amino groups are unprotonated and carboxyl groups are undissociated. This convention is useful to avoid various nomenclatural problems but should not be taken to imply that these structures represent an appreciable fraction of the amino-acid molecules. </p></blockquote> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="History">History</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=1" title="Edit section: History"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The first few amino acids were discovered in the early 1800s.<sup id="cite_ref-8" class="reference"><a href="#cite_note-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-9" class="reference"><a href="#cite_note-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> In 1806, French chemists <a href="/wiki/Louis-Nicolas_Vauquelin" class="mw-redirect" title="Louis-Nicolas Vauquelin">Louis-Nicolas Vauquelin</a> and <a href="/wiki/Pierre_Jean_Robiquet" title="Pierre Jean Robiquet">Pierre Jean Robiquet</a> isolated a compound from <a href="/wiki/Asparagus" title="Asparagus">asparagus</a> that was subsequently named <a href="/wiki/Asparagine" title="Asparagine">asparagine</a>, the first amino acid to be discovered.<sup id="cite_ref-10" class="reference"><a href="#cite_note-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Anfinsen_11-0" class="reference"><a href="#cite_note-Anfinsen-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Cystine" title="Cystine">Cystine</a> was discovered in 1810,<sup id="cite_ref-12" class="reference"><a href="#cite_note-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> although its monomer, <a href="/wiki/Cysteine" title="Cysteine">cysteine</a>, remained undiscovered until 1884.<sup id="cite_ref-13" class="reference"><a href="#cite_note-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Anfinsen_11-1" class="reference"><a href="#cite_note-Anfinsen-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-14" class="reference"><a href="#cite_note-14"><span class="cite-bracket">[</span>a<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Glycine" title="Glycine">Glycine</a> and <a href="/wiki/Leucine" title="Leucine">leucine</a> were discovered in 1820.<sup id="cite_ref-15" class="reference"><a href="#cite_note-15"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> The last of the 20 common amino acids to be discovered was <a href="/wiki/Threonine" title="Threonine">threonine</a> in 1935 by <a href="/wiki/William_Cumming_Rose" title="William Cumming Rose">William Cumming Rose</a>, who also determined the <a href="/wiki/Essential_amino_acid" title="Essential amino acid">essential amino acids</a> and established the minimum daily requirements of all amino acids for optimal growth.<sup id="cite_ref-16" class="reference"><a href="#cite_note-16"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-17" class="reference"><a href="#cite_note-17"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> </p><p>The unity of the chemical category was recognized by <a href="/wiki/Charles_Adolphe_Wurtz" title="Charles Adolphe Wurtz">Wurtz</a> in 1865, but he gave no particular name to it.<sup id="cite_ref-18" class="reference"><a href="#cite_note-18"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup> The first use of the term "amino acid" in the English language dates from 1898,<sup id="cite_ref-19" class="reference"><a href="#cite_note-19"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> while the German term, <span title="German-language text"><i lang="de">Aminosäure</i></span>, was used earlier.<sup id="cite_ref-20" class="reference"><a href="#cite_note-20"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Protein" title="Protein">Proteins</a> were found to yield amino acids after enzymatic digestion or acid <a href="/wiki/Hydrolysis" title="Hydrolysis">hydrolysis</a>. In 1902, <a href="/wiki/Hermann_Emil_Fischer" class="mw-redirect" title="Hermann Emil Fischer">Emil Fischer</a> and <a href="/wiki/Franz_Hofmeister" title="Franz Hofmeister">Franz Hofmeister</a> independently proposed that proteins are formed from many amino acids, whereby bonds are formed between the amino group of one amino acid with the carboxyl group of another, resulting in a linear structure that Fischer termed "<a href="/wiki/Peptide" title="Peptide">peptide</a>".<sup id="cite_ref-21" class="reference"><a href="#cite_note-21"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="General_structure">General structure</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=2" title="Edit section: General structure"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure typeof="mw:File/Thumb"><a href="/wiki/File:ProteinogenicAminoAcids.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/4/4f/ProteinogenicAminoAcids.svg/600px-ProteinogenicAminoAcids.svg.png" decoding="async" width="600" height="480" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/4/4f/ProteinogenicAminoAcids.svg/900px-ProteinogenicAminoAcids.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/4/4f/ProteinogenicAminoAcids.svg/1200px-ProteinogenicAminoAcids.svg.png 2x" data-file-width="941" data-file-height="753" /></a><figcaption>The 21 <a href="/wiki/Proteinogenic_amino_acid" title="Proteinogenic amino acid">proteinogenic α-amino acids</a> found in <a href="/wiki/Eukaryote" title="Eukaryote">eukaryotes</a>, grouped according to their side chains' <a href="/wiki/PKa" class="mw-redirect" title="PKa">p<i>K</i><sub>a</sub></a> values and charges carried at <a href="/wiki/PH#Living_systems" title="PH">physiological pH (7.4)</a></figcaption></figure> <p><b>2-</b>, <b>alpha-</b>, or <b>α-amino acids</b><sup id="cite_ref-22" class="reference"><a href="#cite_note-22"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> have the generic <a href="/wiki/Chemical_formula" title="Chemical formula">formula</a> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap">H<sub class="template-chem2-sub">2</sub>NCHRCOOH</span> in most cases,<sup id="cite_ref-23" class="reference"><a href="#cite_note-23"><span class="cite-bracket">[</span>b<span class="cite-bracket">]</span></a></sup> where R is an <a href="/wiki/Organic_chemistry" title="Organic chemistry">organic</a> <a href="/wiki/Substituent" title="Substituent">substituent</a> known as a "<a href="/wiki/Substituent" title="Substituent">side chain</a>".<sup id="cite_ref-24" class="reference"><a href="#cite_note-24"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> </p><p>Of the many hundreds of described amino acids, 22 are <a href="/wiki/Proteinogenic_amino_acid" title="Proteinogenic amino acid">proteinogenic</a> ("protein-building").<sup id="cite_ref-25" class="reference"><a href="#cite_note-25"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-26" class="reference"><a href="#cite_note-26"><span class="cite-bracket">[</span>24<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-27" class="reference"><a href="#cite_note-27"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> It is these 22 compounds that combine to give a vast array of peptides and proteins assembled by <a href="/wiki/Ribosome" title="Ribosome">ribosomes</a>.<sup id="cite_ref-NIGMS_28-0" class="reference"><a href="#cite_note-NIGMS-28"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup> Non-proteinogenic or modified amino acids may arise from <a href="/wiki/Post-translational_modification" title="Post-translational modification">post-translational modification</a> or during <a href="/wiki/Nonribosomal_peptide" title="Nonribosomal peptide">nonribosomal peptide</a> synthesis. </p> <div class="mw-heading mw-heading3"><h3 id="Chirality">Chirality</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=3" title="Edit section: Chirality"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/wiki/Carbon" title="Carbon">carbon</a> atom next to the <a href="/wiki/Carboxyl_group" class="mw-redirect" title="Carboxyl group">carboxyl group</a> is called the <a href="/wiki/Alpha_carbon" class="mw-redirect" title="Alpha carbon">α–carbon</a>. In proteinogenic amino acids, it bears the amine and the R group or <a href="/wiki/Substituent" title="Substituent">side chain</a> specific to each amino acid, as well as a hydrogen atom. With the exception of glycine, for which the side chain is also a hydrogen atom, the α–carbon is <a href="/wiki/Stereogenic" class="mw-redirect" title="Stereogenic">stereogenic</a>. All <a href="/wiki/Chiral" class="mw-redirect" title="Chiral">chiral</a> proteogenic amino acids have the <small>L</small> configuration. They are "left-handed" <a href="/wiki/Enantiomer" title="Enantiomer">enantiomers</a>, which refers to the <a href="/wiki/Stereoisomers" class="mw-redirect" title="Stereoisomers">stereoisomers</a> of the alpha carbon. </p><p>A few <small>D</small>-amino acids ("right-handed") have been found in nature, e.g., in <a href="/wiki/Bacterial_envelope" class="mw-redirect" title="Bacterial envelope">bacterial envelopes</a>, as a <a href="/wiki/Neuromodulation" title="Neuromodulation">neuromodulator</a> (<small>D</small>-<a href="/wiki/Serine" title="Serine">serine</a>), and in some <a href="/wiki/Antibiotic" title="Antibiotic">antibiotics</a>.<sup id="cite_ref-29" class="reference"><a href="#cite_note-29"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Creighton_30-0" class="reference"><a href="#cite_note-Creighton-30"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup> Rarely, <a href="/wiki/D-Amino_acid" title="D-Amino acid"><small>D</small>-amino acid residues</a> are found in proteins, and are converted from the <small>L</small>-amino acid as a <a href="/wiki/Post-translational_modification" title="Post-translational modification">post-translational modification</a>.<sup id="cite_ref-31" class="reference"><a href="#cite_note-31"><span class="cite-bracket">[</span>29<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-34" class="reference"><a href="#cite_note-34"><span class="cite-bracket">[</span>c<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Side_chains">Side chains</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=4" title="Edit section: Side chains"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading4"><h4 id="Polar_charged_side_chains">Polar charged side chains</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=5" title="Edit section: Polar charged side chains"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Five amino acids possess a charge at neutral pH. Often these side chains appear at the surfaces on proteins to enable their solubility in water, and side chains with opposite charges form important electrostatic contacts called <a href="/wiki/Salt_bridge_(protein_and_supramolecular)" title="Salt bridge (protein and supramolecular)">salt bridges</a> that maintain structures within a single protein or between interfacing proteins.<sup id="cite_ref-Garrett-2010_35-0" class="reference"><a href="#cite_note-Garrett-2010-35"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> Many proteins bind metal into their structures specifically, and these interactions are commonly mediated by charged side chains such as <a href="/wiki/Aspartate" class="mw-redirect" title="Aspartate">aspartate</a>, <a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a> and <a href="/wiki/Histidine" title="Histidine">histidine</a>. Under certain conditions, each ion-forming group can be charged, forming double salts.<sup id="cite_ref-36" class="reference"><a href="#cite_note-36"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup> </p><p>The two negatively charged amino acids at neutral pH are <a href="/wiki/Aspartic_acid" title="Aspartic acid">aspartate</a> (Asp, D) and <a href="/wiki/Glutamic_acid" title="Glutamic acid">glutamate</a> (Glu, E). The anionic carboxylate groups behave as <a href="/wiki/Br%C3%B8nsted%E2%80%93Lowry_acid%E2%80%93base_theory" title="Brønsted–Lowry acid–base theory">Brønsted bases</a> in most circumstances.<sup id="cite_ref-Garrett-2010_35-1" class="reference"><a href="#cite_note-Garrett-2010-35"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> Enzymes in very low pH environments, like the aspartic protease <a href="/wiki/Pepsin" title="Pepsin">pepsin</a> in mammalian stomachs, may have catalytic aspartate or glutamate residues that act as Brønsted acids. </p> <figure typeof="mw:File/Thumb"><a href="/wiki/File:Histidine_lysine_arginine_sidechains.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/d/db/Histidine_lysine_arginine_sidechains.png/450px-Histidine_lysine_arginine_sidechains.png" decoding="async" width="450" height="58" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/d/db/Histidine_lysine_arginine_sidechains.png 1.5x" data-file-width="466" data-file-height="60" /></a><figcaption>Functional groups found in histidine (left), lysine (middle) and arginine (right)</figcaption></figure> <p>There are three amino acids with side chains that are cations at neutral pH: <a href="/wiki/Arginine" title="Arginine">arginine</a> (Arg, R), <a href="/wiki/Lysine" title="Lysine">lysine</a> (Lys, K) and <a href="/wiki/Histidine" title="Histidine">histidine</a> (His, H). Arginine has a charged <a href="/wiki/Guanidine" title="Guanidine">guanidino</a> group and lysine a charged alkyl amino group, and are fully protonated at pH 7. Histidine's imidazole group has a pK<sub>a</sub> of 6.0, and is only around 10% protonated at neutral pH. Because histidine is easily found in its basic and conjugate acid forms it often participates in catalytic proton transfers in enzyme reactions.<sup id="cite_ref-Garrett-2010_35-2" class="reference"><a href="#cite_note-Garrett-2010-35"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading4"><h4 id="Polar_uncharged_side_chains">Polar uncharged side chains</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=6" title="Edit section: Polar uncharged side chains"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The polar, uncharged amino acids <a href="/wiki/Serine" title="Serine">serine</a> (Ser, S), <a href="/wiki/Threonine" title="Threonine">threonine</a> (Thr, T), <a href="/wiki/Asparagine" title="Asparagine">asparagine</a> (Asn, N) and <a href="/wiki/Glutamine" title="Glutamine">glutamine</a> (Gln, Q) readily form hydrogen bonds with water and other amino acids.<sup id="cite_ref-Garrett-2010_35-3" class="reference"><a href="#cite_note-Garrett-2010-35"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> They do not ionize in normal conditions, a prominent exception being the catalytic serine in <a href="/wiki/Serine_protease#Catalytic_mechanism" title="Serine protease">serine proteases</a>. This is an example of severe perturbation, and is not characteristic of serine residues in general. Threonine has two chiral centers, not only the <small>L</small> (2<i>S</i>) chiral center at the α-carbon shared by all amino acids apart from achiral glycine, but also (3<i>R</i>) at the β-carbon. The full <a href="/wiki/Stereochemical" class="mw-redirect" title="Stereochemical">stereochemical</a> specification is (2<i>S</i>,3<i>R</i>)-<small>L</small>-<a href="/wiki/Threonine" title="Threonine">threonine</a>. </p> <div class="mw-heading mw-heading4"><h4 id="Hydrophobic_side_chains">Hydrophobic side chains</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=7" title="Edit section: Hydrophobic side chains"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Nonpolar amino acid interactions are the primary driving force behind the processes that <a href="/wiki/Protein_folding" title="Protein folding">fold proteins</a> into their functional three dimensional structures.<sup id="cite_ref-Garrett-2010_35-4" class="reference"><a href="#cite_note-Garrett-2010-35"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> None of these amino acids' side chains ionize easily, and therefore do not have pK<sub>a</sub>s, with the exception of <a href="/wiki/Tyrosine" title="Tyrosine">tyrosine</a> (Tyr, Y). The hydroxyl of tyrosine can deprotonate at high pH forming the negatively charged phenolate. Because of this one could place tyrosine into the polar, uncharged amino acid category, but its very low solubility in water matches the characteristics of hydrophobic amino acids well. </p> <div class="mw-heading mw-heading4"><h4 id="Special_case_side_chains">Special case side chains</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=8" title="Edit section: Special case side chains"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Several side chains are not described well by the charged, polar and hydrophobic categories. <a href="/wiki/Glycine" title="Glycine">Glycine</a> (Gly, G) could be considered a polar amino acid since its small size means that its solubility is largely determined by the amino and carboxylate groups. However, the lack of any side chain provides glycine with a unique flexibility among amino acids with large ramifications to protein folding.<sup id="cite_ref-Garrett-2010_35-5" class="reference"><a href="#cite_note-Garrett-2010-35"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Cysteine" title="Cysteine">Cysteine</a> (Cys, C) can also form hydrogen bonds readily, which would place it in the polar amino acid category, though it can often be found in protein structures forming covalent bonds, called <a href="/wiki/Disulphide_bonds" class="mw-redirect" title="Disulphide bonds">disulphide bonds</a>, with other cysteines. These bonds influence the folding and stability of proteins, and are essential in the formation of <a href="/wiki/Antibody#Structure" title="Antibody">antibodies</a>. <a href="/wiki/Proline" title="Proline">Proline</a> (Pro, P) has an alkyl side chain and could be considered hydrophobic, but because the side chain joins back onto the alpha amino group it becomes particularly inflexible when incorporated into proteins. Similar to glycine this influences protein structure in a way unique among amino acids. <a href="/wiki/Selenocysteine" title="Selenocysteine">Selenocysteine</a> (Sec, U) is a rare amino acid not directly encoded by DNA, but is incorporated into proteins via the ribosome. Selenocysteine has a lower redox potential compared to the similar cysteine, and participates in several unique enzymatic reactions.<sup id="cite_ref-37" class="reference"><a href="#cite_note-37"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Pyrrolysine" title="Pyrrolysine">Pyrrolysine</a> (Pyl, O) is another amino acid not encoded in DNA, but synthesized into protein by ribosomes.<sup id="cite_ref-38" class="reference"><a href="#cite_note-38"><span class="cite-bracket">[</span>35<span class="cite-bracket">]</span></a></sup> It is found in archaeal species where it participates in the catalytic activity of several methyltransferases. </p> <div class="mw-heading mw-heading4"><h4 id="β-_and_γ-amino_acids"><span id=".CE.B2-_and_.CE.B3-amino_acids"></span>β- and γ-amino acids</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=9" title="Edit section: β- and γ-amino acids"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Amino acids with the structure <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap">NH<span class="template-chem2-su"><span>+</span><span>3</span></span>−CXY−CXY−CO<span class="template-chem2-su"><span>−</span><span>2</span></span></span>, such as <a href="/wiki/%CE%92-alanine" class="mw-redirect" title="Β-alanine">β-alanine</a>, a component of <a href="/wiki/Carnosine" title="Carnosine">carnosine</a> and a few other peptides, are β-amino acids. Ones with the structure <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap">NH<span class="template-chem2-su"><span>+</span><span>3</span></span>−CXY−CXY−CXY−CO<span class="template-chem2-su"><span>−</span><span>2</span></span></span> are γ-amino acids, and so on, where X and Y are two substituents (one of which is normally H).<sup id="cite_ref-iupaciub_7-1" class="reference"><a href="#cite_note-iupaciub-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Zwitterions">Zwitterions</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=10" title="Edit section: Zwitterions"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Zwitterion" title="Zwitterion">Zwitterion</a></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Bronsted_character_of_ionizing_groups_in_proteins.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/b/bf/Bronsted_character_of_ionizing_groups_in_proteins.png/400px-Bronsted_character_of_ionizing_groups_in_proteins.png" decoding="async" width="400" height="573" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/b/bf/Bronsted_character_of_ionizing_groups_in_proteins.png 1.5x" data-file-width="571" data-file-height="818" /></a><figcaption>Ionization and Brønsted character of N-terminal amino, C-terminal carboxylate, and side chains of amino acid residues</figcaption></figure> <p>The common natural forms of amino acids have a <a href="/wiki/Zwitterionic" class="mw-redirect" title="Zwitterionic">zwitterionic</a> structure, with <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap">−NH<span class="template-chem2-su"><span>+</span><span>3</span></span></span> (<link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap">−NH<span class="template-chem2-su"><span>+</span><span>2</span></span>−</span> in the case of proline) and <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap">−CO<span class="template-chem2-su"><span>−</span><span>2</span></span></span> functional groups attached to the same C atom, and are thus α-amino acids, and are the only ones found in proteins during translation in the ribosome. In aqueous solution at pH close to neutrality, amino acids exist as <a href="/wiki/Zwitterion" title="Zwitterion">zwitterions</a>, i.e. as dipolar ions with both <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap">NH<span class="template-chem2-su"><span>+</span><span>3</span></span></span> and <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap">CO<span class="template-chem2-su"><span>−</span><span>2</span></span></span> in charged states, so the overall structure is <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap">NH<span class="template-chem2-su"><span>+</span><span>3</span></span>−CHR−CO<span class="template-chem2-su"><span>−</span><span>2</span></span></span>. At <a href="/wiki/Acid%E2%80%93base_homeostasis" title="Acid–base homeostasis">physiological pH</a> the so-called "neutral forms" <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap">−NH<sub class="template-chem2-sub">2</sub>−CHR−CO<sub class="template-chem2-sub">2</sub>H</span> are not present to any measurable degree.<sup id="cite_ref-39" class="reference"><a href="#cite_note-39"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup> Although the two charges in the zwitterion structure add up to zero it is misleading to call a species with a net charge of zero "uncharged". </p><p>In strongly acidic conditions (pH below 3), the carboxylate group becomes protonated and the structure becomes an ammonio carboxylic acid, <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap">NH<span class="template-chem2-su"><span>+</span><span>3</span></span>−CHR−CO<sub class="template-chem2-sub">2</sub>H</span>. This is relevant for enzymes like pepsin that are active in acidic environments such as the mammalian stomach and <a href="/wiki/Lysosomes" class="mw-redirect" title="Lysosomes">lysosomes</a>, but does not significantly apply to intracellular enzymes. In highly basic conditions (pH greater than 10, not normally seen in physiological conditions), the ammonio group is deprotonated to give <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap">NH<sub class="template-chem2-sub">2</sub>−CHR−CO<span class="template-chem2-su"><span>−</span><span>2</span></span></span>. </p><p>Although various definitions of acids and bases are used in chemistry, the only one that is useful for chemistry in aqueous solution is <a href="/wiki/Br%C3%B8nsted%E2%80%93Lowry_acid%E2%80%93base_theory" title="Brønsted–Lowry acid–base theory">that of Brønsted</a>:<sup id="cite_ref-40" class="reference"><a href="#cite_note-40"><span class="cite-bracket">[</span>37<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Vollhardt-2007_41-0" class="reference"><a href="#cite_note-Vollhardt-2007-41"><span class="cite-bracket">[</span>38<span class="cite-bracket">]</span></a></sup> an acid is a species that can donate a proton to another species, and a base is one that can accept a proton. This criterion is used to label the groups in the above illustration. The carboxylate side chains of aspartate and glutamate residues are the principal Brønsted bases in proteins. Likewise, lysine, tyrosine and cysteine will typically act as a Brønsted acid. Histidine under these conditions can act both as a Brønsted acid and a base. </p> <div class="mw-heading mw-heading3"><h3 id="Isoelectric_point">Isoelectric point</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=11" title="Edit section: Isoelectric point"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:Titration_Curves_of_20_Amino_Acids_Organized_by_Side_Chain.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/c/ca/Titration_Curves_of_20_Amino_Acids_Organized_by_Side_Chain.png/360px-Titration_Curves_of_20_Amino_Acids_Organized_by_Side_Chain.png" decoding="async" width="360" height="293" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/c/ca/Titration_Curves_of_20_Amino_Acids_Organized_by_Side_Chain.png/540px-Titration_Curves_of_20_Amino_Acids_Organized_by_Side_Chain.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/c/ca/Titration_Curves_of_20_Amino_Acids_Organized_by_Side_Chain.png/720px-Titration_Curves_of_20_Amino_Acids_Organized_by_Side_Chain.png 2x" data-file-width="960" data-file-height="780" /></a><figcaption>Composite of <a href="/wiki/Titration_curve" title="Titration curve">titration curves</a> of twenty proteinogenic amino acids grouped by side chain category</figcaption></figure> <p>For amino acids with uncharged side-chains the zwitterion predominates at pH values between the two p<i>K</i><sub>a</sub> values, but coexists in <a href="/wiki/Chemical_equilibrium" title="Chemical equilibrium">equilibrium</a> with small amounts of net negative and net positive ions. At the midpoint between the two p<i>K</i><sub>a</sub> values, the trace amount of net negative and trace of net positive ions balance, so that average net charge of all forms present is zero.<sup id="cite_ref-42" class="reference"><a href="#cite_note-42"><span class="cite-bracket">[</span>39<span class="cite-bracket">]</span></a></sup> This pH is known as the <a href="/wiki/Isoelectric_point" title="Isoelectric point">isoelectric point</a> p<i>I</i>, so p<i>I</i> = <style data-mw-deduplicate="TemplateStyles:r1214402035">.mw-parser-output .sfrac{white-space:nowrap}.mw-parser-output .sfrac.tion,.mw-parser-output .sfrac .tion{display:inline-block;vertical-align:-0.5em;font-size:85%;text-align:center}.mw-parser-output .sfrac .num{display:block;line-height:1em;margin:0.0em 0.1em;border-bottom:1px solid}.mw-parser-output .sfrac .den{display:block;line-height:1em;margin:0.1em 0.1em}.mw-parser-output .sr-only{border:0;clip:rect(0,0,0,0);clip-path:polygon(0px 0px,0px 0px,0px 0px);height:1px;margin:-1px;overflow:hidden;padding:0;position:absolute;width:1px}</style><span class="sfrac">⁠<span class="tion"><span class="num">1</span><span class="sr-only">/</span><span class="den">2</span></span>⁠</span>(p<i>K</i><sub>a1</sub> + p<i>K</i><sub>a2</sub>). </p><p>For amino acids with charged side chains, the p<i>K</i><sub>a</sub> of the side chain is involved. Thus for aspartate or glutamate with negative side chains, the terminal amino group is essentially entirely in the charged form <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1123817410"><span class="chemf nowrap">−NH<span class="template-chem2-su"><span>+</span><span>3</span></span></span>, but this positive charge needs to be balanced by the state with just one C-terminal carboxylate group is negatively charged. This occurs halfway between the two carboxylate p<i>K</i><sub>a</sub> values: p<i>I</i> = <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1214402035"><span class="sfrac">⁠<span class="tion"><span class="num">1</span><span class="sr-only">/</span><span class="den">2</span></span>⁠</span>(p<i>K</i><sub>a1</sub> + p<i>K</i><sub>a(R)</sub>), where p<i>K</i><sub>a(R)</sub> is the side chain p<i>K</i><sub>a</sub>.<sup id="cite_ref-Vollhardt-2007_41-1" class="reference"><a href="#cite_note-Vollhardt-2007-41"><span class="cite-bracket">[</span>38<span class="cite-bracket">]</span></a></sup> </p><p>Similar considerations apply to other amino acids with ionizable side-chains, including not only glutamate (similar to aspartate), but also cysteine, histidine, lysine, tyrosine and arginine with positive side chains. </p><p>Amino acids have zero mobility in <a href="/wiki/Electrophoresis" title="Electrophoresis">electrophoresis</a> at their isoelectric point, although this behaviour is more usually exploited for peptides and proteins than single amino acids. Zwitterions have minimum solubility at their isoelectric point, and some amino acids (in particular, with nonpolar side chains) can be isolated by precipitation from water by adjusting the pH to the required isoelectric point. </p> <div class="mw-heading mw-heading2"><h2 id="Physicochemical_properties">Physicochemical properties</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=12" title="Edit section: Physicochemical properties"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The 20 canonical amino acids can be classified according to their properties. Important factors are charge, <a href="/wiki/Hydrophilicity" class="mw-redirect" title="Hydrophilicity">hydrophilicity</a> or <a href="/wiki/Hydrophobicity" class="mw-redirect" title="Hydrophobicity">hydrophobicity</a>, size, and functional groups.<sup id="cite_ref-Creighton_30-1" class="reference"><a href="#cite_note-Creighton-30"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup> These properties influence <a href="/wiki/Protein_structure" title="Protein structure">protein structure</a> and <a href="/wiki/Protein%E2%80%93protein_interaction" title="Protein–protein interaction">protein–protein interactions</a>. The water-soluble proteins tend to have their hydrophobic residues (<a href="/wiki/Leucine" title="Leucine">Leu</a>, <a href="/wiki/Isoleucine" title="Isoleucine">Ile</a>, <a href="/wiki/Valine" title="Valine">Val</a>, <a href="/wiki/Phenylalanine" title="Phenylalanine">Phe</a>, and <a href="/wiki/Tryptophan" title="Tryptophan">Trp</a>) buried in the middle of the protein, whereas hydrophilic side chains are exposed to the aqueous solvent. (In <a href="/wiki/Biochemistry" title="Biochemistry">biochemistry</a>, a residue refers to a specific <a href="/wiki/Monomer" title="Monomer">monomer</a> <i>within</i> the <a href="/wiki/Polymer" title="Polymer">polymeric</a> chain of a <a href="/wiki/Polysaccharide" title="Polysaccharide">polysaccharide</a>, protein or <a href="/wiki/Nucleic_acid" title="Nucleic acid">nucleic acid</a>.) The <a href="/wiki/Integral_membrane_protein" title="Integral membrane protein">integral membrane proteins</a> tend to have outer rings of exposed <a href="/wiki/Hydrophobic" class="mw-redirect" title="Hydrophobic">hydrophobic</a> amino acids that anchor them in the <a href="/wiki/Lipid_bilayer" title="Lipid bilayer">lipid bilayer</a>. Some <a href="/wiki/Peripheral_membrane_protein" title="Peripheral membrane protein">peripheral membrane proteins</a> have a patch of hydrophobic amino acids on their surface that sticks to the membrane. In a similar fashion, proteins that have to bind to positively charged molecules have surfaces rich in negatively charged amino acids such as <a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a> and <a href="/wiki/Aspartate" class="mw-redirect" title="Aspartate">aspartate</a>, while proteins binding to negatively charged molecules have surfaces rich in positively charged amino acids like <a href="/wiki/Lysine" title="Lysine">lysine</a> and <a href="/wiki/Arginine" title="Arginine">arginine</a>. For example, lysine and arginine are present in large amounts in the <a href="/wiki/Low_complexity_regions_in_proteins" title="Low complexity regions in proteins">low-complexity regions</a> of nucleic-acid binding proteins.<sup id="cite_ref-Ntountoumi-2019_43-0" class="reference"><a href="#cite_note-Ntountoumi-2019-43"><span class="cite-bracket">[</span>40<span class="cite-bracket">]</span></a></sup> There are various <a href="/wiki/Hydrophobicity_scale" class="mw-redirect" title="Hydrophobicity scale">hydrophobicity scales</a> of amino acid residues.<sup id="cite_ref-44" class="reference"><a href="#cite_note-44"><span class="cite-bracket">[</span>41<span class="cite-bracket">]</span></a></sup> </p><p>Some amino acids have special properties. Cysteine can form covalent <a href="/wiki/Disulfide_bond" class="mw-redirect" title="Disulfide bond">disulfide bonds</a> to other cysteine residues. <a href="/wiki/Proline" title="Proline">Proline</a> forms <a href="/wiki/Cyclic_compound" title="Cyclic compound">a cycle</a> to the polypeptide backbone, and glycine is more flexible than other amino acids. </p><p>Glycine and proline are strongly present within low complexity regions of both eukaryotic and prokaryotic proteins, whereas the opposite is the case with cysteine, phenylalanine, tryptophan, methionine, valine, leucine, isoleucine, which are highly reactive, or complex, or hydrophobic.<sup id="cite_ref-Ntountoumi-2019_43-1" class="reference"><a href="#cite_note-Ntountoumi-2019-43"><span class="cite-bracket">[</span>40<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-45" class="reference"><a href="#cite_note-45"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-46" class="reference"><a href="#cite_note-46"><span class="cite-bracket">[</span>43<span class="cite-bracket">]</span></a></sup> </p><p>Many proteins undergo a range of <a href="/wiki/Posttranslational_modification" class="mw-redirect" title="Posttranslational modification">posttranslational modifications</a>, whereby additional chemical groups are attached to the amino acid residue side chains sometimes producing <a href="/wiki/Lipoprotein" title="Lipoprotein">lipoproteins</a> (that are hydrophobic),<sup id="cite_ref-47" class="reference"><a href="#cite_note-47"><span class="cite-bracket">[</span>44<span class="cite-bracket">]</span></a></sup> or <a href="/wiki/Glycoprotein" title="Glycoprotein">glycoproteins</a> (that are hydrophilic)<sup id="cite_ref-48" class="reference"><a href="#cite_note-48"><span class="cite-bracket">[</span>45<span class="cite-bracket">]</span></a></sup> allowing the protein to attach temporarily to a membrane. For example, a signaling protein can attach and then detach from a cell membrane, because it contains cysteine residues that can have the fatty acid <a href="/wiki/Palmitic_acid" title="Palmitic acid">palmitic acid</a> added to them and subsequently removed.<sup id="cite_ref-49" class="reference"><a href="#cite_note-49"><span class="cite-bracket">[</span>46<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Table_of_standard_amino_acid_abbreviations_and_properties">Table of standard amino acid abbreviations and properties</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=13" title="Edit section: Table of standard amino acid abbreviations and properties"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">"Amino acid code" redirects here. For base-pair encoding of amino acids, see <a href="/wiki/Genetic_code#Codons" title="Genetic code">Genetic code § Codons</a>.</div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Proteinogenic_amino_acid" title="Proteinogenic amino acid">Proteinogenic amino acid</a></div> <p>Although one-letter symbols are included in the table, IUPAC–IUBMB recommend<sup id="cite_ref-iupaciub_7-2" class="reference"><a href="#cite_note-iupaciub-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> that "Use of the one-letter symbols should be restricted to the comparison of long sequences". </p><p>The one-letter notation was chosen by IUPAC-IUB based on the following rules:<sup id="cite_ref-IUPAC-1968_50-0" class="reference"><a href="#cite_note-IUPAC-1968-50"><span class="cite-bracket">[</span>47<span class="cite-bracket">]</span></a></sup> </p> <ul><li>Initial letters are used where there is no ambuiguity: C cysteine, H histidine, I isoleucine, M methionine, S serine, V valine,<sup id="cite_ref-IUPAC-1968_50-1" class="reference"><a href="#cite_note-IUPAC-1968-50"><span class="cite-bracket">[</span>47<span class="cite-bracket">]</span></a></sup></li> <li>Where arbitrary assignment is needed, the structurally simpler amino acids are given precedence: A Alanine, G glycine, L leucine, P proline, T threonine,<sup id="cite_ref-IUPAC-1968_50-2" class="reference"><a href="#cite_note-IUPAC-1968-50"><span class="cite-bracket">[</span>47<span class="cite-bracket">]</span></a></sup></li> <li>F <i>PH</i>enylalanine and R a<i>R</i>ginine are assigned by being phonetically suggestive,<sup id="cite_ref-IUPAC-1968_50-3" class="reference"><a href="#cite_note-IUPAC-1968-50"><span class="cite-bracket">[</span>47<span class="cite-bracket">]</span></a></sup></li> <li>W tryptophan is assigned based on the double ring being visually suggestive to the bulky letter W,<sup id="cite_ref-IUPAC-1968_50-4" class="reference"><a href="#cite_note-IUPAC-1968-50"><span class="cite-bracket">[</span>47<span class="cite-bracket">]</span></a></sup></li> <li>K lysine and Y tyrosine are assigned as alphabetically nearest to their initials L and T (note that U was avoided for its similarity with V, while X was reserved for undetermined or atypical amino acids); for tyrosine the mnemonic t<i>Y</i>rosine was also proposed,<sup id="cite_ref-Saffran-1998_51-0" class="reference"><a href="#cite_note-Saffran-1998-51"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup></li> <li>D aspartate was assigned arbitrarily, with the proposed mnemonic aspar<i>D</i>ic acid;<sup id="cite_ref-Adoga-1988_52-0" class="reference"><a href="#cite_note-Adoga-1988-52"><span class="cite-bracket">[</span>49<span class="cite-bracket">]</span></a></sup> E glutamate was assigned in alphabetical sequence being larger by merely one <a href="/wiki/Methylene_group" title="Methylene group">methylene</a> –CH2– group,<sup id="cite_ref-Saffran-1998_51-1" class="reference"><a href="#cite_note-Saffran-1998-51"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup></li> <li>N asparagine was assigned arbitrarily, with the proposed mnemonic asparagi<i>N</i>e;<sup id="cite_ref-Adoga-1988_52-1" class="reference"><a href="#cite_note-Adoga-1988-52"><span class="cite-bracket">[</span>49<span class="cite-bracket">]</span></a></sup> Q glutamine was assigned in alphabetical sequence of those still available (note again that O was avoided due to similarity with D), with the proposed mnemonic <i>Q</i>lutamine.<sup id="cite_ref-Adoga-1988_52-2" class="reference"><a href="#cite_note-Adoga-1988-52"><span class="cite-bracket">[</span>49<span class="cite-bracket">]</span></a></sup></li></ul> <table class="wikitable sortable" style="text-align:center;"> <tbody><tr> <th rowspan="2">Amino acid </th> <th colspan="2">3- and 1-letter symbols </th> <th colspan="3">Side chain </th> <th rowspan="2"><a href="/wiki/Hydropathy_index" class="mw-redirect" title="Hydropathy index">Hydropathy <br />index</a><sup id="cite_ref-53" class="reference"><a href="#cite_note-53"><span class="cite-bracket">[</span>50<span class="cite-bracket">]</span></a></sup> </th> <th colspan="2"><a href="/wiki/Molar_absorptivity" class="mw-redirect" title="Molar absorptivity">Molar absorptivity</a><sup id="cite_ref-Freifelder_54-0" class="reference"><a href="#cite_note-Freifelder-54"><span class="cite-bracket">[</span>51<span class="cite-bracket">]</span></a></sup> </th> <th rowspan="2"><a href="/wiki/Molecular_mass" title="Molecular mass">Molecular mass</a> </th> <th rowspan="2">Abundance in<br />proteins (%)<sup id="cite_ref-55" class="reference"><a href="#cite_note-55"><span class="cite-bracket">[</span>52<span class="cite-bracket">]</span></a></sup> </th> <th rowspan="2">Standard genetic coding,<br /><a href="/wiki/Nucleic_acid_notation#IUPAC_notation" title="Nucleic acid notation">IUPAC notation</a> </th></tr> <tr> <th>3 </th> <th>1 </th> <th>Class </th> <th><a href="/wiki/Chemical_polarity" title="Chemical polarity">Chemical polarity</a><sup id="cite_ref-Hausman_56-0" class="reference"><a href="#cite_note-Hausman-56"><span class="cite-bracket">[</span>53<span class="cite-bracket">]</span></a></sup> </th> <th>Net charge<br />at pH 7.4<sup id="cite_ref-Hausman_56-1" class="reference"><a href="#cite_note-Hausman-56"><span class="cite-bracket">[</span>53<span class="cite-bracket">]</span></a></sup> </th> <th>Wavelength,<br /><i>λ</i><sub>max</sub> (nm) </th> <th>Coefficient <i>ε</i><br />(mM<sup>−1</sup>·cm<sup>−1</sup>) </th></tr> <tr> <td><a href="/wiki/Alanine" title="Alanine">Alanine</a> </td> <td>Ala </td> <td>A </td> <td>Aliphatic </td> <td>Nonpolar </td> <td>Neutral </td> <td>1.8 </td> <td> </td> <td> </td> <td>89.094 </td> <td>8.76 </td> <td>GCN </td></tr> <tr> <td><a href="/wiki/Arginine" title="Arginine">Arginine</a> </td> <td>Arg </td> <td>R </td> <td>Fixed cation </td> <td>Basic polar </td> <td>Positive </td> <td>−4.5 </td> <td> </td> <td> </td> <td>174.203 </td> <td>5.78 </td> <td>MGR, CGY<sup id="cite_ref-57" class="reference"><a href="#cite_note-57"><span class="cite-bracket">[</span>54<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td><a href="/wiki/Asparagine" title="Asparagine">Asparagine</a> </td> <td>Asn </td> <td>N </td> <td>Amide </td> <td>Polar </td> <td>Neutral </td> <td>−3.5 </td> <td> </td> <td> </td> <td>132.119 </td> <td>3.93 </td> <td>AAY </td></tr> <tr> <td><a href="/wiki/Aspartate" class="mw-redirect" title="Aspartate">Aspartate</a> </td> <td>Asp </td> <td>D </td> <td>Anion </td> <td><a href="/wiki/Br%C3%B8nsted_base" class="mw-redirect" title="Brønsted base">Brønsted base</a> </td> <td>Negative </td> <td>−3.5 </td> <td> </td> <td> </td> <td>133.104 </td> <td>5.49 </td> <td>GAY </td></tr> <tr> <td><a href="/wiki/Cysteine" title="Cysteine">Cysteine</a> </td> <td>Cys </td> <td>C </td> <td>Thiol </td> <td>Brønsted acid </td> <td>Neutral </td> <td>2.5 </td> <td>250 </td> <td>0.3 </td> <td>121.154 </td> <td>1.38 </td> <td>UGY </td></tr> <tr> <td><a href="/wiki/Glutamine" title="Glutamine">Glutamine</a> </td> <td>Gln </td> <td>Q </td> <td>Amide </td> <td>Polar </td> <td>Neutral </td> <td>−3.5 </td> <td> </td> <td> </td> <td>146.146 </td> <td>3.9 </td> <td>CAR </td></tr> <tr> <td><a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">Glutamate</a> </td> <td>Glu </td> <td>E </td> <td>Anion </td> <td>Brønsted base </td> <td>Negative </td> <td>−3.5 </td> <td> </td> <td> </td> <td>147.131 </td> <td>6.32 </td> <td>GAR </td></tr> <tr> <td><a href="/wiki/Glycine" title="Glycine">Glycine</a> </td> <td>Gly </td> <td>G </td> <td>Aliphatic </td> <td>Nonpolar </td> <td>Neutral </td> <td>−0.4 </td> <td> </td> <td> </td> <td>75.067 </td> <td>7.03 </td> <td>GGN </td></tr> <tr> <td><a href="/wiki/Histidine" title="Histidine">Histidine</a> </td> <td>His </td> <td>H </td> <td>Cationic </td> <td>Brønsted acid and base </td> <td>Positive, 10%<br />Neutral, 90% </td> <td>−3.2 </td> <td>211 </td> <td>5.9 </td> <td>155.156 </td> <td>2.26 </td> <td>CAY </td></tr> <tr> <td><a href="/wiki/Isoleucine" title="Isoleucine">Isoleucine</a> </td> <td>Ile </td> <td>I </td> <td>Aliphatic </td> <td>Nonpolar </td> <td>Neutral </td> <td>4.5 </td> <td> </td> <td> </td> <td>131.175 </td> <td>5.49 </td> <td>AUH </td></tr> <tr> <td><a href="/wiki/Leucine" title="Leucine">Leucine</a> </td> <td>Leu </td> <td>L </td> <td>Aliphatic </td> <td>Nonpolar </td> <td>Neutral </td> <td>3.8 </td> <td> </td> <td> </td> <td>131.175 </td> <td>9.68 </td> <td>YUR, CUY<sup id="cite_ref-58" class="reference"><a href="#cite_note-58"><span class="cite-bracket">[</span>55<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td><a href="/wiki/Lysine" title="Lysine">Lysine</a> </td> <td>Lys </td> <td>K </td> <td>Cation </td> <td>Brønsted acid </td> <td>Positive </td> <td>−3.9 </td> <td> </td> <td> </td> <td>146.189 </td> <td>5.19 </td> <td>AAR </td></tr> <tr> <td><a href="/wiki/Methionine" title="Methionine">Methionine</a> </td> <td>Met </td> <td>M </td> <td>Thioether </td> <td>Nonpolar </td> <td>Neutral </td> <td>1.9 </td> <td> </td> <td> </td> <td>149.208 </td> <td>2.32 </td> <td>AUG </td></tr> <tr> <td><a href="/wiki/Phenylalanine" title="Phenylalanine">Phenylalanine</a> </td> <td>Phe </td> <td>F </td> <td>Aromatic </td> <td>Nonpolar </td> <td>Neutral </td> <td>2.8 </td> <td>257, 206, 188 </td> <td>0.2, 9.3, 60.0 </td> <td>165.192 </td> <td>3.87 </td> <td>UUY </td></tr> <tr> <td><a href="/wiki/Proline" title="Proline">Proline</a> </td> <td>Pro </td> <td>P </td> <td>Cyclic </td> <td>Nonpolar </td> <td>Neutral </td> <td>−1.6 </td> <td> </td> <td> </td> <td>115.132 </td> <td>5.02 </td> <td>CCN </td></tr> <tr> <td><a href="/wiki/Serine" title="Serine">Serine</a> </td> <td>Ser </td> <td>S </td> <td>Hydroxylic </td> <td>Polar </td> <td>Neutral </td> <td>−0.8 </td> <td> </td> <td> </td> <td>105.093 </td> <td>7.14 </td> <td>UCN, AGY </td></tr> <tr> <td><a href="/wiki/Threonine" title="Threonine">Threonine</a> </td> <td>Thr </td> <td>T </td> <td>Hydroxylic </td> <td>Polar </td> <td>Neutral </td> <td>−0.7 </td> <td> </td> <td> </td> <td>119.119 </td> <td>5.53 </td> <td>ACN </td></tr> <tr> <td><a href="/wiki/Tryptophan" title="Tryptophan">Tryptophan</a> </td> <td>Trp </td> <td>W </td> <td>Aromatic </td> <td>Nonpolar </td> <td>Neutral </td> <td>−0.9 </td> <td>280, 219 </td> <td>5.6, 47.0 </td> <td>204.228 </td> <td>1.25 </td> <td>UGG </td></tr> <tr> <td><a href="/wiki/Tyrosine" title="Tyrosine">Tyrosine</a> </td> <td>Tyr </td> <td>Y </td> <td>Aromatic </td> <td>Brønsted acid </td> <td>Neutral </td> <td>−1.3 </td> <td>274, 222, 193 </td> <td>1.4, 8.0, 48.0 </td> <td>181.191 </td> <td>2.91 </td> <td>UAY </td></tr> <tr> <td><a href="/wiki/Valine" title="Valine">Valine</a> </td> <td>Val </td> <td>V </td> <td>Aliphatic </td> <td>Nonpolar </td> <td>Neutral </td> <td>4.2 </td> <td> </td> <td> </td> <td>117.148 </td> <td>6.73 </td> <td>GUN </td></tr></tbody></table> <p>Two additional amino acids are in some species coded for by <a href="/wiki/Codons" class="mw-redirect" title="Codons">codons</a> that are usually interpreted as <a href="/wiki/Stop_codon" title="Stop codon">stop codons</a>: </p> <table class="wikitable" style="text-align:center;"> <tbody><tr> <th>21st and 22nd amino acids </th> <th>3-letter </th> <th>1-letter </th> <th><a href="/wiki/Molecular_mass" title="Molecular mass">Molecular mass</a> </th></tr> <tr> <td><a href="/wiki/Selenocysteine" title="Selenocysteine">Selenocysteine</a> </td> <td>Sec </td> <td>U </td> <td>168.064 </td></tr> <tr> <td><a href="/wiki/Pyrrolysine" title="Pyrrolysine">Pyrrolysine</a> </td> <td>Pyl </td> <td>O </td> <td>255.313 </td></tr></tbody></table> <p>In addition to the specific amino acid codes, placeholders are used in cases where <a href="/wiki/Protein_sequencing" title="Protein sequencing">chemical</a> or <a href="/wiki/X-ray_crystallography" title="X-ray crystallography">crystallographic</a> analysis of a peptide or protein cannot conclusively determine the identity of a residue. They are also used to summarize <a href="/wiki/Conserved_sequence" title="Conserved sequence">conserved protein sequence</a> motifs. The use of single letters to indicate sets of similar residues is similar to the use of <a href="/wiki/Nucleic_acid_notation" title="Nucleic acid notation">abbreviation codes for degenerate bases</a>.<sup id="cite_ref-59" class="reference"><a href="#cite_note-59"><span class="cite-bracket">[</span>56<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-60" class="reference"><a href="#cite_note-60"><span class="cite-bracket">[</span>57<span class="cite-bracket">]</span></a></sup> </p> <table class="wikitable" style="text-align:center;"> <tbody><tr> <th>Ambiguous amino acids </th> <th>3-letter </th> <th>1-letter </th> <th>Amino acids included </th> <th>Codons included </th></tr> <tr> <td>Any / unknown </td> <td>Xaa </td> <td>X </td> <td>All </td> <td>NNN </td></tr> <tr> <td><a href="/wiki/Asparagine" title="Asparagine">Asparagine</a> or <a href="/wiki/Aspartate" class="mw-redirect" title="Aspartate">aspartate</a> </td> <td>Asx </td> <td>B </td> <td>D, N </td> <td>RAY </td></tr> <tr> <td><a href="/wiki/Glutamine" title="Glutamine">Glutamine</a> or <a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a> </td> <td>Glx </td> <td>Z </td> <td>E, Q </td> <td>SAR </td></tr> <tr> <td><a href="/wiki/Leucine" title="Leucine">Leucine</a> or isoleucine </td> <td>Xle </td> <td>J </td> <td>I, L </td> <td>YTR, ATH, CTY<sup id="cite_ref-61" class="reference"><a href="#cite_note-61"><span class="cite-bracket">[</span>58<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td><a href="/wiki/Hydrophobic" class="mw-redirect" title="Hydrophobic">Hydrophobic</a> </td> <td> </td> <td>Φ </td> <td>V, I, L, F, W, Y, M </td> <td>NTN, TAY, TGG </td></tr> <tr> <td><a href="/wiki/Aromatic" class="mw-redirect" title="Aromatic">Aromatic</a> </td> <td> </td> <td>Ω </td> <td>F, W, Y, H </td> <td>YWY, TTY, TGG<sup id="cite_ref-62" class="reference"><a href="#cite_note-62"><span class="cite-bracket">[</span>59<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td><a href="/wiki/Aliphatic" class="mw-redirect" title="Aliphatic">Aliphatic</a> (non-aromatic) </td> <td> </td> <td>Ψ </td> <td>V, I, L, M </td> <td>VTN, TTR<sup id="cite_ref-63" class="reference"><a href="#cite_note-63"><span class="cite-bracket">[</span>60<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td>Small </td> <td> </td> <td>π </td> <td>P, G, A, S </td> <td>BCN, RGY, GGR </td></tr> <tr> <td><a href="/wiki/Hydrophilic" class="mw-redirect" title="Hydrophilic">Hydrophilic</a> </td> <td> </td> <td>ζ </td> <td>S, T, H, N, Q, E, D, K, R </td> <td>VAN, WCN, CGN, AGY<sup id="cite_ref-64" class="reference"><a href="#cite_note-64"><span class="cite-bracket">[</span>61<span class="cite-bracket">]</span></a></sup> </td></tr> <tr> <td><a href="/wiki/Cation" class="mw-redirect" title="Cation">Positively-charged</a> </td> <td> </td> <td>+ </td> <td>K, R, H </td> <td>ARR, CRY, CGR </td></tr> <tr> <td><a href="/wiki/Anion" class="mw-redirect" title="Anion">Negatively-charged</a> </td> <td> </td> <td>− </td> <td>D, E </td> <td>GAN </td></tr></tbody></table> <p><b>Unk</b> is sometimes used instead of <b>Xaa</b>, but is less standard. </p><p><b>Ter</b> or <b>*</b> (from termination) is used in notation for mutations in proteins when a stop codon occurs. It corresponds to no amino acid at all.<sup id="cite_ref-HGSV_recommendations_65-0" class="reference"><a href="#cite_note-HGSV_recommendations-65"><span class="cite-bracket">[</span>62<span class="cite-bracket">]</span></a></sup> </p><p>In addition, many <a href="/wiki/Non-proteinogenic_amino_acids" title="Non-proteinogenic amino acids">nonstandard amino acids</a> have a specific code. For example, several peptide drugs, such as <a href="/wiki/Bortezomib" title="Bortezomib">Bortezomib</a> and <a href="/wiki/MG132" title="MG132">MG132</a>, are <a href="/wiki/Peptide_synthesis" title="Peptide synthesis">artificially synthesized</a> and retain their <a href="/wiki/Protecting_group" title="Protecting group">protecting groups</a>, which have specific codes. Bortezomib is <a href="/wiki/Pyrazinoic_acid" title="Pyrazinoic acid">Pyz</a>–Phe–boroLeu, and MG132 is <a href="/wiki/Carboxybenzyl" class="mw-redirect" title="Carboxybenzyl">Z</a>–Leu–Leu–Leu–al. To aid in the analysis of protein structure, <a href="/wiki/Photo-reactive_amino_acid_analog" title="Photo-reactive amino acid analog">photo-reactive amino acid analogs</a> are available. These include <a href="/w/index.php?title=Photoleucine&action=edit&redlink=1" class="new" title="Photoleucine (page does not exist)">photoleucine</a> (<b>pLeu</b>) and <a href="/wiki/Photomethionine" class="mw-redirect" title="Photomethionine">photomethionine</a> (<b>pMet</b>).<sup id="cite_ref-66" class="reference"><a href="#cite_note-66"><span class="cite-bracket">[</span>63<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Occurrence_and_functions_in_biochemistry">Occurrence and functions in biochemistry</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=14" title="Edit section: Occurrence and functions in biochemistry"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1237032888/mw-parser-output/.tmulti">.mw-parser-output .tmulti .multiimageinner{display:flex;flex-direction:column}.mw-parser-output .tmulti .trow{display:flex;flex-direction:row;clear:left;flex-wrap:wrap;width:100%;box-sizing:border-box}.mw-parser-output .tmulti .tsingle{margin:1px;float:left}.mw-parser-output .tmulti .theader{clear:both;font-weight:bold;text-align:center;align-self:center;background-color:transparent;width:100%}.mw-parser-output .tmulti .thumbcaption{background-color:transparent}.mw-parser-output .tmulti .text-align-left{text-align:left}.mw-parser-output .tmulti .text-align-right{text-align:right}.mw-parser-output .tmulti .text-align-center{text-align:center}@media all and (max-width:720px){.mw-parser-output .tmulti .thumbinner{width:100%!important;box-sizing:border-box;max-width:none!important;align-items:center}.mw-parser-output .tmulti .trow{justify-content:center}.mw-parser-output .tmulti .tsingle{float:none!important;max-width:100%!important;box-sizing:border-box;text-align:center}.mw-parser-output .tmulti .tsingle .thumbcaption{text-align:left}.mw-parser-output .tmulti .trow>.thumbcaption{text-align:center}}@media screen{html.skin-theme-clientpref-night .mw-parser-output .tmulti .multiimageinner img{background-color:white}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .tmulti .multiimageinner img{background-color:white}}</style><div class="thumb tmulti tright"><div class="thumbinner multiimageinner" style="width:332px;max-width:332px"><div class="trow"><div class="tsingle" style="width:330px;max-width:330px"><div class="thumbimage" style="height:201px;overflow:hidden"><span typeof="mw:File"><a href="/wiki/File:Protein_primary_structure.svg" class="mw-file-description"><img alt="A protein depicted as a long unbranched string of linked circles each representing amino acids" src="//upload.wikimedia.org/wikipedia/commons/thumb/3/38/Protein_primary_structure.svg/328px-Protein_primary_structure.svg.png" decoding="async" width="328" height="201" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/3/38/Protein_primary_structure.svg/492px-Protein_primary_structure.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/3/38/Protein_primary_structure.svg/656px-Protein_primary_structure.svg.png 2x" data-file-width="447" data-file-height="274" /></a></span></div><div class="thumbcaption">A <a href="/wiki/Polypeptide" class="mw-redirect" title="Polypeptide">polypeptide</a> is an unbranched chain of amino acids.</div></div></div><div class="trow"><div class="tsingle" style="width:330px;max-width:330px"><div class="thumbimage" style="height:139px;overflow:hidden"><span typeof="mw:File"><a href="/wiki/File:Beta_alanine_comparison.svg" class="mw-file-description"><img alt="Diagrammatic comparison of the structures of β-alanine and α-alanine" src="//upload.wikimedia.org/wikipedia/commons/thumb/9/92/Beta_alanine_comparison.svg/328px-Beta_alanine_comparison.svg.png" decoding="async" width="328" height="140" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/9/92/Beta_alanine_comparison.svg/492px-Beta_alanine_comparison.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/9/92/Beta_alanine_comparison.svg/656px-Beta_alanine_comparison.svg.png 2x" data-file-width="317" data-file-height="135" /></a></span></div><div class="thumbcaption">β-Alanine and its α-alanine isomer</div></div></div><div class="trow"><div class="tsingle" style="width:330px;max-width:330px"><div class="thumbimage" style="height:455px;overflow:hidden"><span typeof="mw:File"><a href="/wiki/File:Selenocysteine_skeletal_3D.svg" class="mw-file-description"><img alt="A diagram showing the structure of selenocysteine" src="//upload.wikimedia.org/wikipedia/commons/thumb/c/c9/Selenocysteine_skeletal_3D.svg/328px-Selenocysteine_skeletal_3D.svg.png" decoding="async" width="328" height="455" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/c/c9/Selenocysteine_skeletal_3D.svg/492px-Selenocysteine_skeletal_3D.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/c/c9/Selenocysteine_skeletal_3D.svg/656px-Selenocysteine_skeletal_3D.svg.png 2x" data-file-width="400" data-file-height="555" /></a></span></div><div class="thumbcaption">The amino acid <a href="/wiki/Selenocysteine" title="Selenocysteine">selenocysteine</a></div></div></div></div></div> <div class="mw-heading mw-heading3"><h3 id="Proteinogenic_amino_acids">Proteinogenic amino acids</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=15" title="Edit section: Proteinogenic amino acids"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Proteinogenic_amino_acid" title="Proteinogenic amino acid">Proteinogenic amino acid</a></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">See also: <a href="/wiki/Protein_primary_structure" title="Protein primary structure">Protein primary structure</a> and <a href="/wiki/Posttranslational_modification" class="mw-redirect" title="Posttranslational modification">Posttranslational modification</a></div> <p>Amino acids are the precursors to proteins.<sup id="cite_ref-NIGMS_28-1" class="reference"><a href="#cite_note-NIGMS-28"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup> They join by condensation reactions to form short polymer chains called peptides or longer chains called either polypeptides or proteins. These chains are linear and unbranched, with each amino acid residue within the chain attached to two neighboring amino acids. In nature, the process of making proteins encoded by RNA genetic material is called <i><a href="/wiki/Translation_(biology)" title="Translation (biology)">translation</a></i> and involves the step-by-step addition of amino acids to a growing protein chain by a <a href="/wiki/Ribozyme" title="Ribozyme">ribozyme</a> that is called a <a href="/wiki/Ribosome" title="Ribosome">ribosome</a>.<sup id="cite_ref-67" class="reference"><a href="#cite_note-67"><span class="cite-bracket">[</span>64<span class="cite-bracket">]</span></a></sup> The order in which the amino acids are added is read through the <a href="/wiki/Genetic_code" title="Genetic code">genetic code</a> from an <a href="/wiki/Messenger_RNA" title="Messenger RNA">mRNA</a> template, which is an <a href="/wiki/RNA" title="RNA">RNA</a> derived from one of the organism's <a href="/wiki/Gene" title="Gene">genes</a>. </p><p>Twenty-two amino acids are naturally incorporated into polypeptides and are called <a href="/wiki/Proteinogenic" class="mw-redirect" title="Proteinogenic">proteinogenic</a> or natural amino acids.<sup id="cite_ref-Creighton_30-2" class="reference"><a href="#cite_note-Creighton-30"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup> Of these, 20 are encoded by the universal genetic code. The remaining 2, <a href="/wiki/Selenocysteine" title="Selenocysteine">selenocysteine</a> and <a href="/wiki/Pyrrolysine" title="Pyrrolysine">pyrrolysine</a>, are incorporated into proteins by unique synthetic mechanisms. Selenocysteine is incorporated when the mRNA being translated includes a <a href="/wiki/SECIS_element" title="SECIS element">SECIS element</a>, which causes the UGA codon to encode selenocysteine instead of a stop codon.<sup id="cite_ref-68" class="reference"><a href="#cite_note-68"><span class="cite-bracket">[</span>65<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Pyrrolysine" title="Pyrrolysine">Pyrrolysine</a> is used by some <a href="/wiki/Methanogen" title="Methanogen">methanogenic</a> <a href="/wiki/Archaea" title="Archaea">archaea</a> in enzymes that they use to produce <a href="/wiki/Methane" title="Methane">methane</a>. It is coded for with the codon UAG, which is normally a stop codon in other organisms.<sup id="cite_ref-69" class="reference"><a href="#cite_note-69"><span class="cite-bracket">[</span>66<span class="cite-bracket">]</span></a></sup> </p><p>Several independent evolutionary studies have suggested that Gly, Ala, Asp, Val, Ser, Pro, Glu, Leu, Thr may belong to a group of amino acids that constituted the early genetic code, whereas Cys, Met, Tyr, Trp, His, Phe may belong to a group of amino acids that constituted later additions of the genetic code.<sup id="cite_ref-70" class="reference"><a href="#cite_note-70"><span class="cite-bracket">[</span>67<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-71" class="reference"><a href="#cite_note-71"><span class="cite-bracket">[</span>68<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-72" class="reference"><a href="#cite_note-72"><span class="cite-bracket">[</span>69<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Standard_vs_nonstandard_amino_acids">Standard vs nonstandard amino acids</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=16" title="Edit section: Standard vs nonstandard amino acids"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The 20 amino acids that are encoded directly by the codons of the universal genetic code are called <i>standard</i> or <i>canonical</i> amino acids. A modified form of methionine (<a href="/wiki/N-Formylmethionine" title="N-Formylmethionine"><i>N</i>-formylmethionine</a>) is often incorporated in place of methionine as the initial amino acid of proteins in bacteria, mitochondria and <a href="/wiki/Plastid" title="Plastid">plastids</a> (including chloroplasts). Other amino acids are called <i>nonstandard</i> or <i>non-canonical</i>. Most of the nonstandard amino acids are also non-proteinogenic (i.e. they cannot be incorporated into proteins during translation), but two of them are proteinogenic, as they can be incorporated translationally into proteins by exploiting information not encoded in the universal genetic code. </p><p>The two nonstandard proteinogenic amino acids are selenocysteine (present in many non-eukaryotes as well as most eukaryotes, but not coded directly by DNA) and <a href="/wiki/Pyrrolysine" title="Pyrrolysine">pyrrolysine</a> (found only in some <a href="/wiki/Archaea" title="Archaea">archaea</a> and at least one <a href="/wiki/Bacterium" class="mw-redirect" title="Bacterium">bacterium</a>). The incorporation of these nonstandard amino acids is rare. For example, 25 human proteins include selenocysteine in their primary structure,<sup id="cite_ref-73" class="reference"><a href="#cite_note-73"><span class="cite-bracket">[</span>70<span class="cite-bracket">]</span></a></sup> and the structurally characterized enzymes (selenoenzymes) employ selenocysteine as the catalytic <a href="/wiki/Moiety_(chemistry)" title="Moiety (chemistry)">moiety</a> in their active sites.<sup id="cite_ref-74" class="reference"><a href="#cite_note-74"><span class="cite-bracket">[</span>71<span class="cite-bracket">]</span></a></sup> Pyrrolysine and selenocysteine are encoded via variant codons. For example, selenocysteine is encoded by stop codon and <a href="/wiki/SECIS_element" title="SECIS element">SECIS element</a>.<sup id="cite_ref-Tjong_75-0" class="reference"><a href="#cite_note-Tjong-75"><span class="cite-bracket">[</span>72<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-VoJw6fIISSkC_p.299_76-0" class="reference"><a href="#cite_note-VoJw6fIISSkC_p.299-76"><span class="cite-bracket">[</span>73<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-url_The_Genetic_Codes_NCBI_77-0" class="reference"><a href="#cite_note-url_The_Genetic_Codes_NCBI-77"><span class="cite-bracket">[</span>74<span class="cite-bracket">]</span></a></sup> </p><p><a href="/wiki/N-Formylmethionine" title="N-Formylmethionine"><i>N</i>-formylmethionine</a> (which is often the initial amino acid of proteins in bacteria, <a href="/wiki/Mitochondrion" title="Mitochondrion">mitochondria</a>, and <a href="/wiki/Chloroplast" title="Chloroplast">chloroplasts</a>) is generally considered as a form of <a href="/wiki/Methionine" title="Methionine">methionine</a> rather than as a separate proteinogenic amino acid. Codon–<a href="/wiki/Transfer_RNA" title="Transfer RNA">tRNA</a> combinations not found in nature can also be used to <a href="/wiki/Expanded_genetic_code" title="Expanded genetic code">"expand" the genetic code</a> and form novel proteins known as <a href="/wiki/Alloprotein" title="Alloprotein">alloproteins</a> incorporating <a href="/wiki/Non-proteinogenic_amino_acid" class="mw-redirect" title="Non-proteinogenic amino acid">non-proteinogenic amino acids</a>.<sup id="cite_ref-pmid16260173_78-0" class="reference"><a href="#cite_note-pmid16260173-78"><span class="cite-bracket">[</span>75<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid19318213_79-0" class="reference"><a href="#cite_note-pmid19318213-79"><span class="cite-bracket">[</span>76<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-isbn0-387-22046-1_80-0" class="reference"><a href="#cite_note-isbn0-387-22046-1-80"><span class="cite-bracket">[</span>77<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Non-proteinogenic_amino_acids">Non-proteinogenic amino acids</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=17" title="Edit section: Non-proteinogenic amino acids"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Non-proteinogenic_amino_acids" title="Non-proteinogenic amino acids">Non-proteinogenic amino acids</a></div> <p>Aside from the 22 <a href="/wiki/Proteinogenic_amino_acid" title="Proteinogenic amino acid">proteinogenic amino acids</a>, many <i>non-proteinogenic</i> amino acids are known. Those either are not found in proteins (for example <a href="/wiki/Carnitine" title="Carnitine">carnitine</a>, <a href="/wiki/Gamma-aminobutyric_acid" class="mw-redirect" title="Gamma-aminobutyric acid">GABA</a>, <a href="/wiki/Levothyroxine" title="Levothyroxine">levothyroxine</a>) or are not produced directly and in isolation by standard cellular machinery. For example, <a href="/wiki/Hydroxyproline" title="Hydroxyproline">hydroxyproline</a>, is synthesised from <a href="/wiki/Proline" title="Proline">proline</a>. Another example is <a href="/wiki/Selenomethionine" title="Selenomethionine">selenomethionine</a>). </p><p>Non-proteinogenic amino acids that are found in proteins are formed by <a href="/wiki/Post-translational_modification" title="Post-translational modification">post-translational modification</a>. Such modifications can also determine the localization of the protein, e.g., the addition of long hydrophobic groups can cause a protein to bind to a <a href="/wiki/Phospholipid" title="Phospholipid">phospholipid</a> membrane.<sup id="cite_ref-81" class="reference"><a href="#cite_note-81"><span class="cite-bracket">[</span>78<span class="cite-bracket">]</span></a></sup> Examples: </p> <ul><li>the <a href="/wiki/Carboxylation" title="Carboxylation">carboxylation</a> of <a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a> allows for better binding of <a href="/wiki/Calcium_in_biology" title="Calcium in biology">calcium cations</a>,<sup id="cite_ref-82" class="reference"><a href="#cite_note-82"><span class="cite-bracket">[</span>79<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Hydroxyproline" title="Hydroxyproline">Hydroxyproline</a>, generated by <a href="/wiki/Hydroxylation" title="Hydroxylation">hydroxylation</a> of <a href="/wiki/Proline" title="Proline">proline</a>, is a major component of the <a href="/wiki/Connective_tissue" title="Connective tissue">connective tissue</a> <a href="/wiki/Collagen" title="Collagen">collagen</a>.<sup id="cite_ref-83" class="reference"><a href="#cite_note-83"><span class="cite-bracket">[</span>80<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Hypusine" title="Hypusine">Hypusine</a> in the <a href="/wiki/Eukaryotic_initiation_factor" title="Eukaryotic initiation factor">translation initiation factor</a> <a href="/wiki/EIF5A" title="EIF5A">EIF5A</a>, contains a modification of lysine.<sup id="cite_ref-84" class="reference"><a href="#cite_note-84"><span class="cite-bracket">[</span>81<span class="cite-bracket">]</span></a></sup></li></ul> <p>Some non-proteinogenic amino acids are not found in proteins. Examples include <a href="/wiki/2-aminoisobutyric_acid" class="mw-redirect" title="2-aminoisobutyric acid">2-aminoisobutyric acid</a> and the neurotransmitter <a href="/wiki/Gamma-aminobutyric_acid" class="mw-redirect" title="Gamma-aminobutyric acid">gamma-aminobutyric acid</a>. Non-proteinogenic amino acids often occur as intermediates in the <a href="/wiki/Metabolic_pathway" title="Metabolic pathway">metabolic pathways</a> for standard amino acids – for example, <a href="/wiki/Ornithine" title="Ornithine">ornithine</a> and <a href="/wiki/Citrulline" title="Citrulline">citrulline</a> occur in the <a href="/wiki/Urea_cycle" title="Urea cycle">urea cycle</a>, part of amino acid <a href="/wiki/Catabolism" title="Catabolism">catabolism</a> (see below).<sup id="cite_ref-85" class="reference"><a href="#cite_note-85"><span class="cite-bracket">[</span>82<span class="cite-bracket">]</span></a></sup> A rare exception to the dominance of α-amino acids in biology is the β-amino acid <a href="/wiki/Beta_alanine" class="mw-redirect" title="Beta alanine">beta alanine</a> (3-aminopropanoic acid), which is used in plants and microorganisms in the synthesis of <a href="/wiki/Pantothenic_acid" title="Pantothenic acid">pantothenic acid</a> (vitamin B<sub>5</sub>), a component of <a href="/wiki/Coenzyme_A" title="Coenzyme A">coenzyme A</a>.<sup id="cite_ref-86" class="reference"><a href="#cite_note-86"><span class="cite-bracket">[</span>83<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="In_mammalian_nutrition">In mammalian nutrition</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=18" title="Edit section: In mammalian nutrition"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:Amino_acids_in_food_and_blood.png" class="mw-file-description"><img alt="Diagram showing the relative occurrence of amino acids in blood serum as obtained from diverse diets." src="//upload.wikimedia.org/wikipedia/commons/thumb/0/05/Amino_acids_in_food_and_blood.png/380px-Amino_acids_in_food_and_blood.png" decoding="async" width="380" height="224" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/0/05/Amino_acids_in_food_and_blood.png/570px-Amino_acids_in_food_and_blood.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/0/05/Amino_acids_in_food_and_blood.png/760px-Amino_acids_in_food_and_blood.png 2x" data-file-width="1648" data-file-height="970" /></a><figcaption>Share of amino acid in various human diets and the resulting mix of amino acids in human blood serum. Glutamate and glutamine are the most frequent in food at over 10%, while alanine, glutamine, and glycine are the most common in blood.</figcaption></figure> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Essential_amino_acid" title="Essential amino acid">Essential amino acid</a></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Further information: <a href="/wiki/Protein_(nutrient)" title="Protein (nutrient)">Protein (nutrient)</a> and <a href="/wiki/Amino_acid_synthesis" title="Amino acid synthesis">Amino acid synthesis</a></div> <p>Amino acids are not typical component of food: animals eat proteins. The protein is broken down into amino acids in the process of digestion. They are then used to synthesize new proteins, other biomolecules, or are oxidized to <a href="/wiki/Urea" title="Urea">urea</a> and <a href="/wiki/Carbon_dioxide" title="Carbon dioxide">carbon dioxide</a> as a source of energy.<sup id="cite_ref-87" class="reference"><a href="#cite_note-87"><span class="cite-bracket">[</span>84<span class="cite-bracket">]</span></a></sup> The oxidation pathway starts with the removal of the amino group by a <a href="/wiki/Transaminase" title="Transaminase">transaminase</a>; the amino group is then fed into the <a href="/wiki/Urea_cycle" title="Urea cycle">urea cycle</a>. The other product of transamidation is a <a href="/wiki/Keto_acid" title="Keto acid">keto acid</a> that enters the <a href="/wiki/Citric_acid_cycle" title="Citric acid cycle">citric acid cycle</a>.<sup id="cite_ref-88" class="reference"><a href="#cite_note-88"><span class="cite-bracket">[</span>85<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Glucogenic_amino_acid" title="Glucogenic amino acid">Glucogenic amino acids</a> can also be converted into glucose, through <a href="/wiki/Gluconeogenesis" title="Gluconeogenesis">gluconeogenesis</a>.<sup id="cite_ref-89" class="reference"><a href="#cite_note-89"><span class="cite-bracket">[</span>86<span class="cite-bracket">]</span></a></sup> </p><p>Of the 20 standard amino acids, nine (<a href="/wiki/Histidine" title="Histidine">His</a>, <a href="/wiki/Isoleucine" title="Isoleucine">Ile</a>, <a href="/wiki/Leucine" title="Leucine">Leu</a>, <a href="/wiki/Lysine" title="Lysine">Lys</a>, <a href="/wiki/Methionine" title="Methionine">Met</a>, <a href="/wiki/Phenylalanine" title="Phenylalanine">Phe</a>, <a href="/wiki/Threonine" title="Threonine">Thr</a>, <a href="/wiki/Tryptophan" title="Tryptophan">Trp</a> and <a href="/wiki/Valine" title="Valine">Val</a>) are called <a href="/wiki/Essential_amino_acid" title="Essential amino acid">essential amino acids</a> because the <a href="/wiki/Human_body" title="Human body">human body</a> cannot <a href="/wiki/Biosynthesis" title="Biosynthesis">synthesize</a> them from other compounds at the level needed for normal growth, so they must be obtained from food.<sup id="cite_ref-90" class="reference"><a href="#cite_note-90"><span class="cite-bracket">[</span>87<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-91" class="reference"><a href="#cite_note-91"><span class="cite-bracket">[</span>88<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-92" class="reference"><a href="#cite_note-92"><span class="cite-bracket">[</span>89<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading4"><h4 id="Semi-essential_and_conditionally_essential_amino_acids,_and_juvenile_requirements"><span id="Semi-essential_and_conditionally_essential_amino_acids.2C_and_juvenile_requirements"></span>Semi-essential and conditionally essential amino acids, and juvenile requirements</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=19" title="Edit section: Semi-essential and conditionally essential amino acids, and juvenile requirements"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>In addition, cysteine, <a href="/wiki/Tyrosine" title="Tyrosine">tyrosine</a>, and <a href="/wiki/Arginine" title="Arginine">arginine</a> are considered semiessential amino acids, and taurine a semi-essential aminosulfonic acid in children. Some amino acids are <a href="/wiki/Essential_amino_acid#Essentiality_in_humans" title="Essential amino acid">conditionally essential</a> for certain ages or medical conditions. Essential amino acids may also vary from <a href="/wiki/Species" title="Species">species</a> to species.<sup id="cite_ref-93" class="reference"><a href="#cite_note-93"><span class="cite-bracket">[</span>d<span class="cite-bracket">]</span></a></sup> The metabolic pathways that synthesize these monomers are not fully developed.<sup id="cite_ref-94" class="reference"><a href="#cite_note-94"><span class="cite-bracket">[</span>90<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-95" class="reference"><a href="#cite_note-95"><span class="cite-bracket">[</span>91<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Non-protein_functions">Non-protein functions</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=20" title="Edit section: Non-protein functions"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="skin-invert-image"> <table role="presentation" cellpadding="0" style="border-spacing:0; clear:right; float:right;"> <tbody><tr> <td><div class="thumb tright"> <div class="thumbinner" style="width:592px;"> <div style="clear: both; font-weight: bold; font-size: 106.4%; text-align: center; background-color: #F0F8FF;margin-bottom:3px;">Biosynthetic pathways for <a href="/wiki/Catecholamine" title="Catecholamine">catecholamines</a> and <a href="/wiki/Trace_amine" title="Trace amine">trace amines</a> in the <a href="/wiki/Human_brain" title="Human brain">human brain</a><sup id="cite_ref-Trace_amine_template_1_96-0" class="reference"><a href="#cite_note-Trace_amine_template_1-96"><span class="cite-bracket">[</span>92<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Trace_amine_template_2_97-0" class="reference"><a href="#cite_note-Trace_amine_template_2-97"><span class="cite-bracket">[</span>93<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-CYP2D6_tyramine-dopamine_metabolism_98-0" class="reference"><a href="#cite_note-CYP2D6_tyramine-dopamine_metabolism-98"><span class="cite-bracket">[</span>94<span class="cite-bracket">]</span></a></sup></div> <div style="position:relative; width:590px; height:465px; overflow:hidden; border:solid #ccc 1px; background-color:white;"> <div style="left:5px; top:0px; width:580px; position:absolute"> <span typeof="mw:File"><a href="https://commons.wikimedia.org/wiki/File:Catecholamine_and_trace_amine_biosynthesis.svg" title="commons:File:Catecholamine and trace amine biosynthesis.svg"><img alt="Graphic of catecholamine and trace amine biosynthesis" src="//upload.wikimedia.org/wikipedia/commons/thumb/4/46/Catecholamine_and_trace_amine_biosynthesis.svg/580px-Catecholamine_and_trace_amine_biosynthesis.svg.png" decoding="async" width="580" height="458" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/4/46/Catecholamine_and_trace_amine_biosynthesis.svg/870px-Catecholamine_and_trace_amine_biosynthesis.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/4/46/Catecholamine_and_trace_amine_biosynthesis.svg/1160px-Catecholamine_and_trace_amine_biosynthesis.svg.png 2x" data-file-width="512" data-file-height="404" /></a></span> </div> <div style="text-align:center; font-size:14px; line-height:110%"> <div style="background-color:transparent; color:black"><div id="annotation_40x60" style="position:absolute; left:40px; top:60px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Phenylalanine" title="Phenylalanine"><small>L</small>-Phenylalanine</a></span></div> <div id="annotation_50x185" style="position:absolute; left:50px; top:185px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Tyrosine" title="Tyrosine"><small>L</small>-Tyrosine</a></span></div> <div id="annotation_60x315" style="position:absolute; left:60px; top:315px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/L-DOPA" title="L-DOPA"><small>L</small>-DOPA</a></span></div> <div id="annotation_50x445" style="position:absolute; left:50px; top:445px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Adrenaline" title="Adrenaline">Epinephrine</a></span></div> <div id="annotation_245x60" style="position:absolute; left:245px; top:60px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Phenethylamine" title="Phenethylamine">Phenethylamine</a></span></div> <div id="annotation_245x185" style="position:absolute; left:245px; top:185px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Tyramine" title="Tyramine"><i>p</i>-Tyramine</a></span></div> <div id="annotation_245x315" style="position:absolute; left:245px; top:315px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Dopamine" title="Dopamine">Dopamine</a></span></div> <div id="annotation_245x445" style="position:absolute; left:245px; top:445px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Norepinephrine" title="Norepinephrine">Norepinephrine</a></span></div> <div id="annotation_415x60" style="position:absolute; left:415px; top:60px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/N-Methylphenethylamine" title="N-Methylphenethylamine"><i>N</i>-Methylphenethylamine</a></span></div> <div id="annotation_440x138" style="position:absolute; left:440px; top:138px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/N-Methyltyramine" title="N-Methyltyramine"><i>N</i>-Methyltyramine</a></span></div> <div id="annotation_440x228" style="position:absolute; left:440px; top:228px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Octopamine" title="Octopamine"><i>p</i>-Octopamine</a></span></div> <div id="annotation_455x350" style="position:absolute; left:455px; top:350px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Synephrine" title="Synephrine">Synephrine</a></span></div> <div id="annotation_445x445" style="position:absolute; left:445px; top:445px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/3-Methoxytyramine" title="3-Methoxytyramine">3-Methoxytyramine</a></span></div> <div id="annotation_167x16" style="position:absolute; left:167px; top:16px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Aromatic_L-amino_acid_decarboxylase" title="Aromatic L-amino acid decarboxylase">AADC</a></span></div> <div id="annotation_167x145" style="position:absolute; left:167px; top:145px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Aromatic_L-amino_acid_decarboxylase" title="Aromatic L-amino acid decarboxylase">AADC</a></span></div> <div id="annotation_167x275" style="position:absolute; left:167px; top:275px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Aromatic_L-amino_acid_decarboxylase" title="Aromatic L-amino acid decarboxylase">AADC</a></span></div> <div id="annotation_164x295" style="position:absolute; left:164px; top:295px; font-size:12px; font-size:12; line-height:14px;"><span style="background-color:transparent; color:inherit;">primary<br />pathway</span></div> <div id="annotation_370x17" style="position:absolute; left:370px; top:17px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Phenylethanolamine_N-methyltransferase" title="Phenylethanolamine N-methyltransferase">PNMT</a></span></div> <div id="annotation_360x120" style="position:absolute; left:360px; top:120px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Phenylethanolamine_N-methyltransferase" title="Phenylethanolamine N-methyltransferase">PNMT</a></span></div> <div id="annotation_445x255" style="position:absolute; left:445px; top:255px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Phenylethanolamine_N-methyltransferase" title="Phenylethanolamine N-methyltransferase">PNMT</a></span></div> <div id="annotation_176x407" style="position:absolute; left:176px; top:407px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Phenylethanolamine_N-methyltransferase" title="Phenylethanolamine N-methyltransferase">PNMT</a></span></div> <div id="annotation_40x90" style="position:absolute; left:40px; top:90px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Biopterin-dependent_aromatic_amino_acid_hydroxylase" title="Biopterin-dependent aromatic amino acid hydroxylase">AAAH</a></span></div> <div id="annotation_40x220" style="position:absolute; left:40px; top:220px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Biopterin-dependent_aromatic_amino_acid_hydroxylase" title="Biopterin-dependent aromatic amino acid hydroxylase">AAAH</a></span></div> <div id="annotation_225x215" style="position:absolute; left:225px; top:215px; line-height:110%;"><span style="background-color:transparent; color:inherit;">brain<br /><a href="/wiki/CYP2D6" title="CYP2D6">CYP2D6</a></span></div> <div id="annotation_291x217" style="position:absolute; left:291px; top:217px; font-size:12px; font-size:12; line-height:14px; text-align:left;"><span style="background-color:transparent; color:inherit;">minor<br />pathway</span></div> <div id="annotation_325x350" style="position:absolute; left:325px; top:350px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Catechol-O-methyltransferase" title="Catechol-O-methyltransferase">COMT</a></span></div> <div id="annotation_250x350" style="position:absolute; left:250px; top:350px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Dopamine_beta-hydroxylase" title="Dopamine beta-hydroxylase">DBH</a></span></div> <div id="annotation_360x185" style="position:absolute; left:360px; top:185px; line-height:110%;"><span style="background-color:transparent; color:inherit;"><a href="/wiki/Dopamine_beta-hydroxylase" title="Dopamine beta-hydroxylase">DBH</a></span></div></div> </div> </div> <div class="thumbcaption" style="clear:left"><div style="float:left;margin-right:0.5em"><span typeof="mw:File"><span title="The image above contains clickable links"><img alt="The image above contains clickable links" src="//upload.wikimedia.org/wikipedia/commons/thumb/e/e6/Interactive_icon.svg/18px-Interactive_icon.svg.png" decoding="async" width="18" height="27" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/e/e6/Interactive_icon.svg/27px-Interactive_icon.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/e/e6/Interactive_icon.svg/36px-Interactive_icon.svg.png 2x" data-file-width="133" data-file-height="200" /></span></span></div><a href="/wiki/Catecholamine" title="Catecholamine">Catecholamines</a> and <a href="/wiki/Trace_amine" title="Trace amine">trace amines</a> are synthesized from phenylalanine and tyrosine in humans.</div> </div> </div> </td></tr></tbody></table> </div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Further information: <a href="/wiki/Amino_acid_neurotransmitter" title="Amino acid neurotransmitter">Amino acid neurotransmitter</a></div> <p>Many proteinogenic and non-proteinogenic amino acids have biological functions beyond being precursors to proteins and peptides.In humans, amino acids also have important roles in diverse biosynthetic pathways. <a href="/wiki/Plant_defense_against_herbivory" title="Plant defense against herbivory">Defenses against herbivores</a> in plants sometimes employ amino acids.<sup id="cite_ref-Hylin1969_99-0" class="reference"><a href="#cite_note-Hylin1969-99"><span class="cite-bracket">[</span>95<span class="cite-bracket">]</span></a></sup> Examples: </p> <div class="mw-heading mw-heading4"><h4 id="Standard_amino_acids">Standard amino acids</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=21" title="Edit section: Standard amino acids"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a href="/wiki/Tryptophan" title="Tryptophan">Tryptophan</a> is a precursor of the neurotransmitter <a href="/wiki/Serotonin" title="Serotonin">serotonin</a>.<sup id="cite_ref-100" class="reference"><a href="#cite_note-100"><span class="cite-bracket">[</span>96<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Tyrosine" title="Tyrosine">Tyrosine</a> (and its precursor phenylalanine) are precursors of the <a href="/wiki/Catecholamine" title="Catecholamine">catecholamine</a> <a href="/wiki/Neurotransmitter" title="Neurotransmitter">neurotransmitters</a> <a href="/wiki/Dopamine" title="Dopamine">dopamine</a>, <a href="/wiki/Epinephrine" class="mw-redirect" title="Epinephrine">epinephrine</a> and <a href="/wiki/Norepinephrine" title="Norepinephrine">norepinephrine</a> and various <a href="/wiki/Trace_amine" title="Trace amine">trace amines</a>.</li> <li><a href="/wiki/Phenylalanine" title="Phenylalanine">Phenylalanine</a> is a precursor of <a href="/wiki/Phenethylamine" title="Phenethylamine">phenethylamine</a> and tyrosine in humans. In plants, it is a precursor of various <a href="/wiki/Phenylpropanoid" title="Phenylpropanoid">phenylpropanoids</a>, which are important in plant metabolism.</li> <li><a href="/wiki/Glycine" title="Glycine">Glycine</a> is a precursor of <a href="/wiki/Porphyrin" title="Porphyrin">porphyrins</a> such as <a href="/wiki/Heme" title="Heme">heme</a>.<sup id="cite_ref-101" class="reference"><a href="#cite_note-101"><span class="cite-bracket">[</span>97<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Arginine" title="Arginine">Arginine</a> is a precursor of <a href="/wiki/Nitric_oxide" title="Nitric oxide">nitric oxide</a>.<sup id="cite_ref-102" class="reference"><a href="#cite_note-102"><span class="cite-bracket">[</span>98<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Ornithine" title="Ornithine">Ornithine</a> and <a href="/wiki/S-Adenosyl_methionine" title="S-Adenosyl methionine"><i>S</i>-adenosylmethionine</a> are precursors of <a href="/wiki/Polyamine" title="Polyamine">polyamines</a>.<sup id="cite_ref-103" class="reference"><a href="#cite_note-103"><span class="cite-bracket">[</span>99<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Aspartate" class="mw-redirect" title="Aspartate">Aspartate</a>, <a href="/wiki/Glycine" title="Glycine">glycine</a>, and <a href="/wiki/Glutamine" title="Glutamine">glutamine</a> are precursors of <a href="/wiki/Nucleotide" title="Nucleotide">nucleotides</a>.<sup id="cite_ref-Stryer_2002_104-0" class="reference"><a href="#cite_note-Stryer_2002-104"><span class="cite-bracket">[</span>100<span class="cite-bracket">]</span></a></sup> However, not all of the functions of other abundant nonstandard amino acids are known.</li></ul> <div class="mw-heading mw-heading4"><h4 id="Roles_for_nonstandard_amino_acids">Roles for nonstandard amino acids</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=22" title="Edit section: Roles for nonstandard amino acids"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a href="/wiki/Carnitine" title="Carnitine">Carnitine</a> is used in <a href="/wiki/Lipid" title="Lipid">lipid transport</a>.</li> <li><a href="/wiki/Gamma-aminobutyric_acid" class="mw-redirect" title="Gamma-aminobutyric acid">gamma-aminobutyric acid</a> is a neurotransmitter.<sup id="cite_ref-pmid12467378_105-0" class="reference"><a href="#cite_note-pmid12467378-105"><span class="cite-bracket">[</span>101<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/5-HTP" class="mw-redirect" title="5-HTP">5-HTP</a> (5-hydroxytryptophan) is used for experimental treatment of depression.<sup id="cite_ref-106" class="reference"><a href="#cite_note-106"><span class="cite-bracket">[</span>102<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/L-DOPA" title="L-DOPA"><small>L</small>-DOPA</a> (<small>L</small>-dihydroxyphenylalanine) for <a href="/wiki/Parkinson%27s" class="mw-redirect" title="Parkinson's">Parkinson's</a> treatment,<sup id="cite_ref-107" class="reference"><a href="#cite_note-107"><span class="cite-bracket">[</span>103<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Eflornithine" title="Eflornithine">Eflornithine</a> inhibits <a href="/wiki/Ornithine_decarboxylase" title="Ornithine decarboxylase">ornithine decarboxylase</a> and used in the treatment of <a href="/wiki/African_trypanosomiasis" title="African trypanosomiasis">sleeping sickness</a>.<sup id="cite_ref-108" class="reference"><a href="#cite_note-108"><span class="cite-bracket">[</span>104<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Canavanine" title="Canavanine">Canavanine</a>, an analogue of <a href="/wiki/Arginine" title="Arginine">arginine</a> found in many <a href="/wiki/Legume" title="Legume">legumes</a> is an <a href="/wiki/Antifeedant" title="Antifeedant">antifeedant</a>, protecting the plant from predators.<sup id="cite_ref-109" class="reference"><a href="#cite_note-109"><span class="cite-bracket">[</span>105<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Mimosine" title="Mimosine">Mimosine</a> found in some legumes, is another possible <a href="/wiki/Antifeedant" title="Antifeedant">antifeedant</a>.<sup id="cite_ref-110" class="reference"><a href="#cite_note-110"><span class="cite-bracket">[</span>106<span class="cite-bracket">]</span></a></sup> This compound is an analogue of <a href="/wiki/Tyrosine" title="Tyrosine">tyrosine</a> and can poison animals that graze on these plants.</li></ul> <div class="mw-heading mw-heading2"><h2 id="Uses_in_industry">Uses in industry</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=23" title="Edit section: Uses in industry"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="Animal_feed">Animal feed</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=24" title="Edit section: Animal feed"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Amino acids are sometimes added to <a href="/wiki/Compound_feed" class="mw-redirect" title="Compound feed">animal feed</a> because some of the components of these feeds, such as <a href="/wiki/Soybean" title="Soybean">soybeans</a>, have low levels of some of the <a href="/wiki/Essential_amino_acid" title="Essential amino acid">essential amino acids</a>, especially of lysine, methionine, threonine, and tryptophan.<sup id="cite_ref-Leuchtenberger2005_111-0" class="reference"><a href="#cite_note-Leuchtenberger2005-111"><span class="cite-bracket">[</span>107<span class="cite-bracket">]</span></a></sup> Likewise amino acids are used to chelate metal cations in order to improve the absorption of minerals from feed supplements.<sup id="cite_ref-112" class="reference"><a href="#cite_note-112"><span class="cite-bracket">[</span>108<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Food">Food</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=25" title="Edit section: Food"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/wiki/Food_industry" title="Food industry">food industry</a> is a major consumer of amino acids, especially <a href="/wiki/Glutamic_acid" title="Glutamic acid">glutamic acid</a>, which is used as a <a href="/wiki/Flavor_enhancer" class="mw-redirect" title="Flavor enhancer">flavor enhancer</a>,<sup id="cite_ref-Garattini_113-0" class="reference"><a href="#cite_note-Garattini-113"><span class="cite-bracket">[</span>109<span class="cite-bracket">]</span></a></sup> and <a href="/wiki/Aspartame" title="Aspartame">aspartame</a> (aspartylphenylalanine 1-methyl ester), which is used as an <a href="/wiki/Artificial_sweetener" class="mw-redirect" title="Artificial sweetener">artificial sweetener</a>.<sup id="cite_ref-114" class="reference"><a href="#cite_note-114"><span class="cite-bracket">[</span>110<span class="cite-bracket">]</span></a></sup> Amino acids are sometimes added to food by manufacturers to alleviate symptoms of mineral deficiencies, such as anemia, by improving mineral absorption and reducing negative side effects from inorganic mineral supplementation.<sup id="cite_ref-Ullmann_115-0" class="reference"><a href="#cite_note-Ullmann-115"><span class="cite-bracket">[</span>111<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Chemical_building_blocks">Chemical building blocks</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=26" title="Edit section: Chemical building blocks"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Further information: <a href="/wiki/Asymmetric_synthesis" class="mw-redirect" title="Asymmetric synthesis">Asymmetric synthesis</a></div> <p>Amino acids are low-cost <a href="/wiki/Feedstock" class="mw-redirect" title="Feedstock">feedstocks</a> used in <a href="/wiki/Chiral_pool_synthesis" class="mw-redirect" title="Chiral pool synthesis">chiral pool synthesis</a> as <a href="/wiki/Enantiomer" title="Enantiomer">enantiomerically pure</a> building blocks.<sup id="cite_ref-Hanessian1993_116-0" class="reference"><a href="#cite_note-Hanessian1993-116"><span class="cite-bracket">[</span>112<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Blaser1992_117-0" class="reference"><a href="#cite_note-Blaser1992-117"><span class="cite-bracket">[</span>113<span class="cite-bracket">]</span></a></sup> </p><p>Amino acids are used in the synthesis of some <a href="/wiki/Cosmetics" title="Cosmetics">cosmetics</a>.<sup id="cite_ref-Leuchtenberger2005_111-1" class="reference"><a href="#cite_note-Leuchtenberger2005-111"><span class="cite-bracket">[</span>107<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Aspirational_uses">Aspirational uses</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=27" title="Edit section: Aspirational uses"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="Fertilizer">Fertilizer</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=28" title="Edit section: Fertilizer"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/wiki/Chelation" title="Chelation">chelating</a> ability of amino acids is sometimes used in fertilizers to facilitate the delivery of minerals to plants in order to correct mineral deficiencies, such as iron chlorosis. These fertilizers are also used to prevent deficiencies from occurring and to improve the overall health of the plants.<sup id="cite_ref-118" class="reference"><a href="#cite_note-118"><span class="cite-bracket">[</span>114<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Biodegradable_plastics">Biodegradable plastics</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=29" title="Edit section: Biodegradable plastics"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Further information: <a href="/wiki/Biodegradable_plastic" title="Biodegradable plastic">Biodegradable plastic</a> and <a href="/wiki/Biopolymer" title="Biopolymer">Biopolymer</a></div> <p>Amino acids have been considered as components of biodegradable polymers, which have applications as <a href="/wiki/Environmentally_friendly" title="Environmentally friendly">environmentally friendly</a> packaging and in medicine in <a href="/wiki/Drug_delivery" title="Drug delivery">drug delivery</a> and the construction of <a href="/wiki/Prosthetic_implant" class="mw-redirect" title="Prosthetic implant">prosthetic implants</a>.<sup id="cite_ref-Sanda1999_119-0" class="reference"><a href="#cite_note-Sanda1999-119"><span class="cite-bracket">[</span>115<span class="cite-bracket">]</span></a></sup> An interesting example of such materials is <a href="/wiki/Polyaspartate" class="mw-redirect" title="Polyaspartate">polyaspartate</a>, a water-soluble biodegradable polymer that may have applications in disposable <a href="/wiki/Diaper" title="Diaper">diapers</a> and agriculture.<sup id="cite_ref-Gross2002_120-0" class="reference"><a href="#cite_note-Gross2002-120"><span class="cite-bracket">[</span>116<span class="cite-bracket">]</span></a></sup> Due to its solubility and ability to <a href="/wiki/Chelate" class="mw-redirect" title="Chelate">chelate</a> metal ions, polyaspartate is also being used as a biodegradable anti<a href="/wiki/Fouling" title="Fouling">scaling</a> agent and a <a href="/wiki/Corrosion_inhibitor" title="Corrosion inhibitor">corrosion inhibitor</a>.<sup id="cite_ref-121" class="reference"><a href="#cite_note-121"><span class="cite-bracket">[</span>117<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Thombre2005_122-0" class="reference"><a href="#cite_note-Thombre2005-122"><span class="cite-bracket">[</span>118<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Synthesis">Synthesis</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=30" title="Edit section: Synthesis"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">Main article: <a href="/wiki/Amino_acid_synthesis" title="Amino acid synthesis">Amino acid synthesis</a></div> <figure class="mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:Strecker_amino_acid_synthesis_scheme.svg" class="mw-file-description"><img alt="For the steps in the reaction, see the text." src="//upload.wikimedia.org/wikipedia/commons/thumb/a/a9/Strecker_amino_acid_synthesis_scheme.svg/400px-Strecker_amino_acid_synthesis_scheme.svg.png" decoding="async" width="400" height="89" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/a/a9/Strecker_amino_acid_synthesis_scheme.svg/600px-Strecker_amino_acid_synthesis_scheme.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/a/a9/Strecker_amino_acid_synthesis_scheme.svg/800px-Strecker_amino_acid_synthesis_scheme.svg.png 2x" data-file-width="469" data-file-height="104" /></a><figcaption>The Strecker amino acid synthesis</figcaption></figure> <div class="mw-heading mw-heading3"><h3 id="Chemical_synthesis">Chemical synthesis</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=31" title="Edit section: Chemical synthesis"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The commercial production of amino acids usually relies on mutant bacteria that overproduce individual amino acids using glucose as a carbon source. Some amino acids are produced by enzymatic conversions of synthetic intermediates. <a href="/wiki/2-Aminothiazoline-4-carboxylic_acid" title="2-Aminothiazoline-4-carboxylic acid">2-Aminothiazoline-4-carboxylic acid</a> is an intermediate in one industrial synthesis of <a href="/wiki/Cysteine" title="Cysteine"><small>L</small>-cysteine</a> for example. <a href="/wiki/Aspartic_acid" title="Aspartic acid">Aspartic acid</a> is produced by the addition of ammonia to <a href="/wiki/Fumarate" class="mw-redirect" title="Fumarate">fumarate</a> using a lyase.<sup id="cite_ref-Ullmann_115-1" class="reference"><a href="#cite_note-Ullmann-115"><span class="cite-bracket">[</span>111<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Biosynthesis">Biosynthesis</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=32" title="Edit section: Biosynthesis"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>In plants, nitrogen is first assimilated into organic compounds in the form of <a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a>, formed from alpha-ketoglutarate and ammonia in the mitochondrion. For other amino acids, plants use <a href="/wiki/Transaminase" title="Transaminase">transaminases</a> to move the amino group from glutamate to another alpha-keto acid. For example, aspartate aminotransferase converts glutamate and oxaloacetate to alpha-ketoglutarate and aspartate.<sup id="cite_ref-123" class="reference"><a href="#cite_note-123"><span class="cite-bracket">[</span>119<span class="cite-bracket">]</span></a></sup> Other organisms use transaminases for amino acid synthesis, too. </p><p>Nonstandard amino acids are usually formed through modifications to standard amino acids. For example, <a href="/wiki/Homocysteine" title="Homocysteine">homocysteine</a> is formed through the <a href="/wiki/Transsulfuration_pathway" title="Transsulfuration pathway">transsulfuration pathway</a> or by the demethylation of methionine via the intermediate metabolite <a href="/wiki/S-adenosylmethionine" class="mw-redirect" title="S-adenosylmethionine"><i>S</i>-adenosylmethionine</a>,<sup id="cite_ref-Brosnan_124-0" class="reference"><a href="#cite_note-Brosnan-124"><span class="cite-bracket">[</span>120<span class="cite-bracket">]</span></a></sup> while <a href="/wiki/Hydroxyproline" title="Hydroxyproline">hydroxyproline</a> is made by a <a href="/wiki/Post_translational_modification" class="mw-redirect" title="Post translational modification">post translational modification</a> of <a href="/wiki/Proline" title="Proline">proline</a>.<sup id="cite_ref-125" class="reference"><a href="#cite_note-125"><span class="cite-bracket">[</span>121<span class="cite-bracket">]</span></a></sup> </p><p><a href="/wiki/Microorganism" title="Microorganism">Microorganisms</a> and plants synthesize many uncommon amino acids. For example, some microbes make <a href="/wiki/2-aminoisobutyric_acid" class="mw-redirect" title="2-aminoisobutyric acid">2-aminoisobutyric acid</a> and <a href="/wiki/Lanthionine" title="Lanthionine">lanthionine</a>, which is a sulfide-bridged derivative of alanine. Both of these amino acids are found in peptidic <a href="/wiki/Lantibiotics" title="Lantibiotics">lantibiotics</a> such as <a href="/wiki/Alamethicin" title="Alamethicin">alamethicin</a>.<sup id="cite_ref-126" class="reference"><a href="#cite_note-126"><span class="cite-bracket">[</span>122<span class="cite-bracket">]</span></a></sup> However, in plants, <a href="/wiki/1-aminocyclopropane-1-carboxylic_acid" class="mw-redirect" title="1-aminocyclopropane-1-carboxylic acid">1-aminocyclopropane-1-carboxylic acid</a> is a small disubstituted cyclic amino acid that is an intermediate in the production of the plant hormone <a href="/wiki/Ethylene#Ethylene_as_a_plant_hormone" title="Ethylene">ethylene</a>.<sup id="cite_ref-127" class="reference"><a href="#cite_note-127"><span class="cite-bracket">[</span>123<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Primordial_synthesis">Primordial synthesis</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=33" title="Edit section: Primordial synthesis"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The formation of amino acids and peptides are assumed to precede and perhaps induce the <a href="/wiki/Abiogenesis" title="Abiogenesis">emergence of life on earth</a>. Amino acids can form from simple precursors under various conditions.<sup id="cite_ref-10.1016/j.gsf.2017.07.007_128-0" class="reference"><a href="#cite_note-10.1016/j.gsf.2017.07.007-128"><span class="cite-bracket">[</span>124<span class="cite-bracket">]</span></a></sup> Surface-based chemical metabolism of amino acids and very small compounds may have led to the build-up of amino acids, coenzymes and phosphate-based small carbon molecules.<sup id="cite_ref-129" class="reference"><a href="#cite_note-129"><span class="cite-bracket">[</span>125<span class="cite-bracket">]</span></a></sup><sup class="noprint Inline-Template Template-Fact" style="white-space:nowrap;">[<i><a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed"><span title="This claim needs additional references to reliable sources. (September 2022)">additional citation(s) needed</span></a></i>]</sup> Amino acids and similar building blocks could have been elaborated into proto-<a href="/wiki/Peptide" title="Peptide">peptides</a>, with peptides being considered key players in the origin of life.<sup id="cite_ref-10.1021/acs.chemrev.9b00664_130-0" class="reference"><a href="#cite_note-10.1021/acs.chemrev.9b00664-130"><span class="cite-bracket">[</span>126<span class="cite-bracket">]</span></a></sup> </p><p>In the famous <a href="/wiki/Urey-Miller_experiment" class="mw-redirect" title="Urey-Miller experiment">Urey-Miller experiment</a>, the passage of an electric arc through a mixture of methane, hydrogen, and ammonia produces a large number of amino acids. Since then, scientists have discovered a range of ways and components by which the potentially prebiotic formation and chemical evolution of peptides may have occurred, such as condensing agents, the design of self-replicating peptides and a number of non-enzymatic mechanisms by which amino acids could have emerged and elaborated into peptides.<sup id="cite_ref-10.1021/acs.chemrev.9b00664_130-1" class="reference"><a href="#cite_note-10.1021/acs.chemrev.9b00664-130"><span class="cite-bracket">[</span>126<span class="cite-bracket">]</span></a></sup> Several hypotheses invoke the <a href="/wiki/Strecker_synthesis" class="mw-redirect" title="Strecker synthesis">Strecker synthesis</a> whereby hydrogen cyanide, simple aldehydes, ammonia, and water produce amino acids.<sup id="cite_ref-10.1016/j.gsf.2017.07.007_128-1" class="reference"><a href="#cite_note-10.1016/j.gsf.2017.07.007-128"><span class="cite-bracket">[</span>124<span class="cite-bracket">]</span></a></sup> </p><p>According to a review, amino acids, and even peptides, "turn up fairly regularly in the <a href="/wiki/Primordial_soup" title="Primordial soup">various experimental broths</a> that have been allowed to be cooked from simple chemicals. This is because <a href="/wiki/Nucleotide" title="Nucleotide">nucleotides</a> are far more difficult to synthesize chemically than amino acids." For a chronological order, it suggests that there must have been a 'protein world' or at least a 'polypeptide world', possibly later followed by the '<a href="/wiki/RNA_world" title="RNA world">RNA world</a>' and the '<a href="/wiki/DNA_world" class="mw-redirect" title="DNA world">DNA world</a>'.<sup id="cite_ref-131" class="reference"><a href="#cite_note-131"><span class="cite-bracket">[</span>127<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Codon" class="mw-redirect" title="Codon">Codon</a>–amino acids mappings may be the <a href="/wiki/Biology" title="Biology">biological</a> information system at the primordial origin of life on Earth.<sup id="cite_ref-132" class="reference"><a href="#cite_note-132"><span class="cite-bracket">[</span>128<span class="cite-bracket">]</span></a></sup> While amino acids and consequently simple peptides must have formed under different experimentally probed geochemical scenarios, the transition from an abiotic world to the first life forms is to a large extent still unresolved.<sup id="cite_ref-133" class="reference"><a href="#cite_note-133"><span class="cite-bracket">[</span>129<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Reactions">Reactions</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=34" title="Edit section: Reactions"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Amino acids undergo the reactions expected of the constituent functional groups.<sup id="cite_ref-134" class="reference"><a href="#cite_note-134"><span class="cite-bracket">[</span>130<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-135" class="reference"><a href="#cite_note-135"><span class="cite-bracket">[</span>131<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Peptide_bond_formation">Peptide bond formation</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=35" title="Edit section: Peptide bond formation"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236090951"><div role="note" class="hatnote navigation-not-searchable">See also: <a href="/wiki/Peptide_synthesis" title="Peptide synthesis">Peptide synthesis</a> and <a href="/wiki/Peptide_bond" title="Peptide bond">Peptide bond</a></div> <figure class="mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:Peptidformationball.svg" class="mw-file-description"><img alt="Two amino acids are shown next to each other. One loses a hydrogen and oxygen from its carboxyl group (COOH) and the other loses a hydrogen from its amino group (NH2). This reaction produces a molecule of water (H2O) and two amino acids joined by a peptide bond (–CO–NH–). The two joined amino acids are called a dipeptide." src="//upload.wikimedia.org/wikipedia/commons/thumb/6/6d/Peptidformationball.svg/400px-Peptidformationball.svg.png" decoding="async" width="400" height="331" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/6/6d/Peptidformationball.svg/600px-Peptidformationball.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/6/6d/Peptidformationball.svg/800px-Peptidformationball.svg.png 2x" data-file-width="990" data-file-height="820" /></a><figcaption>The condensation of two amino acids to form a <a href="/wiki/Dipeptide" title="Dipeptide">dipeptide</a>. The two amino acid <i>residues</i> are linked through a <i><a href="/wiki/Peptide_bond" title="Peptide bond">peptide bond</a></i>.</figcaption></figure> <p>As both the amine and carboxylic acid groups of amino acids can react to form amide bonds, one amino acid molecule can react with another and become joined through an amide linkage. This <a href="/wiki/Polymerization" title="Polymerization">polymerization</a> of amino acids is what creates proteins. This <a href="/wiki/Condensation_reaction" title="Condensation reaction">condensation reaction</a> yields the newly formed peptide bond and a molecule of water. In cells, this reaction does not occur directly; instead, the amino acid is first activated by attachment to a <a href="/wiki/Transfer_RNA" title="Transfer RNA">transfer RNA</a> molecule through an <a href="/wiki/Ester" title="Ester">ester</a> bond. This aminoacyl-tRNA is produced in an <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a>-dependent reaction carried out by an <a href="/wiki/Aminoacyl_tRNA_synthetase" title="Aminoacyl tRNA synthetase">aminoacyl tRNA synthetase</a>.<sup id="cite_ref-136" class="reference"><a href="#cite_note-136"><span class="cite-bracket">[</span>132<span class="cite-bracket">]</span></a></sup> This aminoacyl-tRNA is then a substrate for the ribosome, which catalyzes the attack of the amino group of the elongating protein chain on the ester bond.<sup id="cite_ref-137" class="reference"><a href="#cite_note-137"><span class="cite-bracket">[</span>133<span class="cite-bracket">]</span></a></sup> As a result of this mechanism, all proteins made by ribosomes are synthesized starting at their <i>N</i>-terminus and moving toward their <i>C</i>-terminus. </p><p>However, not all peptide bonds are formed in this way. In a few cases, peptides are synthesized by specific enzymes. For example, the tripeptide <a href="/wiki/Glutathione" title="Glutathione">glutathione</a> is an essential part of the defenses of cells against oxidative stress. This peptide is synthesized in two steps from free amino acids.<sup id="cite_ref-138" class="reference"><a href="#cite_note-138"><span class="cite-bracket">[</span>134<span class="cite-bracket">]</span></a></sup> In the first step, <a href="/wiki/Gamma-glutamylcysteine_synthetase" class="mw-redirect" title="Gamma-glutamylcysteine synthetase">gamma-glutamylcysteine synthetase</a> condenses cysteine and <a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a> through a peptide bond formed between the side chain carboxyl of the glutamate (the gamma carbon of this side chain) and the amino group of the cysteine. This dipeptide is then condensed with glycine by <a href="/wiki/Glutathione_synthetase" title="Glutathione synthetase">glutathione synthetase</a> to form glutathione.<sup id="cite_ref-139" class="reference"><a href="#cite_note-139"><span class="cite-bracket">[</span>135<span class="cite-bracket">]</span></a></sup> </p><p>In chemistry, peptides are synthesized by a variety of reactions. One of the most-used in <a href="/wiki/Peptide_synthesis" title="Peptide synthesis">solid-phase peptide synthesis</a> uses the aromatic oxime derivatives of amino acids as activated units. These are added in sequence onto the growing peptide chain, which is attached to a solid resin support.<sup id="cite_ref-140" class="reference"><a href="#cite_note-140"><span class="cite-bracket">[</span>136<span class="cite-bracket">]</span></a></sup> Libraries of peptides are used in drug discovery through <a href="/wiki/High-throughput_screening" title="High-throughput screening">high-throughput screening</a>.<sup id="cite_ref-141" class="reference"><a href="#cite_note-141"><span class="cite-bracket">[</span>137<span class="cite-bracket">]</span></a></sup> </p><p>The combination of functional groups allow amino acids to be effective polydentate ligands for metal–amino acid chelates.<sup id="cite_ref-142" class="reference"><a href="#cite_note-142"><span class="cite-bracket">[</span>138<span class="cite-bracket">]</span></a></sup> The multiple side chains of amino acids can also undergo chemical reactions. </p> <div class="mw-heading mw-heading3"><h3 id="Catabolism">Catabolism</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=36" title="Edit section: Catabolism"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure typeof="mw:File/Thumb"><a href="/wiki/File:Amino_acid_catabolism_revised.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/1/16/Amino_acid_catabolism_revised.png/300px-Amino_acid_catabolism_revised.png" decoding="async" width="300" height="211" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/1/16/Amino_acid_catabolism_revised.png/450px-Amino_acid_catabolism_revised.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/1/16/Amino_acid_catabolism_revised.png/600px-Amino_acid_catabolism_revised.png 2x" data-file-width="906" data-file-height="636" /></a><figcaption>Catabolism of proteinogenic amino acids. Amino acids can be classified according to the properties of their main degradation products:<sup id="cite_ref-143" class="reference"><a href="#cite_note-143"><span class="cite-bracket">[</span>139<span class="cite-bracket">]</span></a></sup> <br />* <i>Glucogenic</i>, with the products having the ability to form <a href="/wiki/Glucose" title="Glucose">glucose</a> by <a href="/wiki/Gluconeogenesis" title="Gluconeogenesis">gluconeogenesis</a> <br />* <i>Ketogenic</i>, with the products not having the ability to form glucose. These products may still be used for <a href="/wiki/Ketogenesis" title="Ketogenesis">ketogenesis</a> or <a href="/wiki/Lipid_synthesis" class="mw-redirect" title="Lipid synthesis">lipid synthesis</a>. <br />* Amino acids catabolized into both glucogenic and ketogenic products.</figcaption></figure> <p>Degradation of an amino acid often involves <a href="/wiki/Deamination" title="Deamination">deamination</a> by moving its amino group to α-ketoglutarate, forming <a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a>. This process involves transaminases, often the same as those used in amination during synthesis. In many vertebrates, the amino group is then removed through the <a href="/wiki/Urea_cycle" title="Urea cycle">urea cycle</a> and is excreted in the form of <a href="/wiki/Urea" title="Urea">urea</a>. However, amino acid degradation can produce <a href="/wiki/Uric_acid" title="Uric acid">uric acid</a> or ammonia instead. For example, <a href="/wiki/Serine_dehydratase" title="Serine dehydratase">serine dehydratase</a> converts serine to pyruvate and ammonia.<sup id="cite_ref-Stryer_2002_104-1" class="reference"><a href="#cite_note-Stryer_2002-104"><span class="cite-bracket">[</span>100<span class="cite-bracket">]</span></a></sup> After removal of one or more amino groups, the remainder of the molecule can sometimes be used to synthesize new amino acids, or it can be used for energy by entering <a href="/wiki/Glycolysis" title="Glycolysis">glycolysis</a> or the <a href="/wiki/Citric_acid_cycle" title="Citric acid cycle">citric acid cycle</a>, as detailed in image at right. </p> <div class="mw-heading mw-heading3"><h3 id="Complexation">Complexation</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=37" title="Edit section: Complexation"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Amino acids are bidentate ligands, forming <a href="/wiki/Transition_metal_amino_acid_complexes" title="Transition metal amino acid complexes">transition metal amino acid complexes</a>.<sup id="cite_ref-144" class="reference"><a href="#cite_note-144"><span class="cite-bracket">[</span>140<span class="cite-bracket">]</span></a></sup> </p><p><span typeof="mw:File"><a href="/wiki/File:AAcomplexation.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/e/e2/AAcomplexation.png/420px-AAcomplexation.png" decoding="async" width="420" height="95" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/e/e2/AAcomplexation.png/630px-AAcomplexation.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/e/e2/AAcomplexation.png/840px-AAcomplexation.png 2x" data-file-width="1733" data-file-height="390" /></a></span> </p> <div class="mw-heading mw-heading2"><h2 id="Chemical_analysis">Chemical analysis</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=38" title="Edit section: Chemical analysis"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The total nitrogen content of organic matter is mainly formed by the amino groups in proteins. The Total Kjeldahl Nitrogen (<a href="/wiki/TKN" class="mw-redirect" title="TKN">TKN</a>) is a measure of nitrogen widely used in the analysis of (waste) water, soil, food, feed and organic matter in general. As the name suggests, the <a href="/wiki/Kjeldahl_method" title="Kjeldahl method">Kjeldahl method</a> is applied. More sensitive methods are available.<sup id="cite_ref-pmid23959242_145-0" class="reference"><a href="#cite_note-pmid23959242-145"><span class="cite-bracket">[</span>141<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-146" class="reference"><a href="#cite_note-146"><span class="cite-bracket">[</span>142<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=39" title="Edit section: See also"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239009302">.mw-parser-output .portalbox{padding:0;margin:0.5em 0;display:table;box-sizing:border-box;max-width:175px;list-style:none}.mw-parser-output .portalborder{border:1px solid 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href="/wiki/Degron" title="Degron">Degron</a></li> <li><a href="/wiki/Erepsin" title="Erepsin">Erepsin</a></li> <li><a href="/wiki/Homochirality" title="Homochirality">Homochirality</a></li> <li><a href="/wiki/Hyperaminoacidemia" title="Hyperaminoacidemia">Hyperaminoacidemia</a></li> <li><a href="/wiki/Leucines" title="Leucines">Leucines</a></li> <li><a href="/wiki/Miller%E2%80%93Urey_experiment" title="Miller–Urey experiment">Miller–Urey experiment</a></li> <li><a href="/wiki/Nucleic_acid_sequence" title="Nucleic acid sequence">Nucleic acid sequence</a></li> <li><a href="/wiki/RNA_codon_table" class="mw-redirect" title="RNA codon table">RNA codon table</a></li></ul> </div> <div class="mw-heading mw-heading2"><h2 id="Notes">Notes</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=40" title="Edit section: Notes"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style 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class="references"> <li id="cite_note-14"><span class="mw-cite-backlink"><b><a href="#cite_ref-14">^</a></b></span> <span class="reference-text">The late discovery is explained by the fact that cysteine becomes oxidized to cystine in air.</span> </li> <li id="cite_note-23"><span class="mw-cite-backlink"><b><a href="#cite_ref-23">^</a></b></span> <span class="reference-text"><a href="/wiki/Proline" title="Proline">Proline</a> and other cyclic amino acids are an exception to this general formula. Cyclization of the α-amino acid creates the corresponding secondary amine. These are occasionally referred to as <a href="/wiki/Imino_acid" title="Imino acid">imino acids</a>.</span> </li> <li id="cite_note-34"><span class="mw-cite-backlink"><b><a href="#cite_ref-34">^</a></b></span> <span class="reference-text">The <small>L</small> and <small>D</small> convention for amino acid configuration refers not to the optical activity of the amino acid itself but rather to the optical activity of the isomer of <a href="/wiki/Glyceraldehyde" title="Glyceraldehyde">glyceraldehyde</a> from which that amino acid can, in theory, be synthesized (<small>D</small>-glyceraldehyde is dextrorotatory; <small>L</small>-glyceraldehyde is levorotatory). An alternative convention is to use the <a href="/wiki/Cahn%E2%80%93Ingold%E2%80%93Prelog_priority_rules" title="Cahn–Ingold–Prelog priority rules">(<i>S</i>) and (<i>R</i>) designators</a> to specify the <i>absolute configuration</i>.<sup id="cite_ref-Cahn_32-0" class="reference"><a href="#cite_note-Cahn-32"><span class="cite-bracket">[</span>30<span class="cite-bracket">]</span></a></sup> Almost all of the amino acids in proteins are (<i>S</i>) at the α carbon, with <a href="/wiki/Cysteine" title="Cysteine">cysteine</a> being (<i>R</i>) and glycine non-<a href="/wiki/Chirality_(chemistry)" title="Chirality (chemistry)">chiral</a>.<sup id="cite_ref-33" class="reference"><a href="#cite_note-33"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup> Cysteine has its side chain in the same geometric location as the other amino acids, but the <i>R</i>/<i>S</i> terminology is reversed because <a href="/wiki/Sulfur" title="Sulfur">sulfur</a> has higher atomic number compared to the carboxyl oxygen which gives the side chain a higher priority by the <a href="/wiki/Cahn%E2%80%93Ingold%E2%80%93Prelog_priority_rules" title="Cahn–Ingold–Prelog priority rules">Cahn-Ingold-Prelog sequence rules</a>.</span> </li> <li id="cite_note-93"><span class="mw-cite-backlink"><b><a href="#cite_ref-93">^</a></b></span> <span class="reference-text">For example, <a href="/wiki/Ruminant" title="Ruminant">ruminants</a> such as cows obtain a number of amino acids via <a href="/wiki/Microbe" class="mw-redirect" title="Microbe">microbes</a> in the <a href="/wiki/Reticulorumen" title="Reticulorumen">first two stomach chambers</a>.</span> </li> </ol></div></div> <div class="mw-heading mw-heading2"><h2 id="References">References</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=41" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239543626"><div class="reflist"> <div class="mw-references-wrap mw-references-columns"><ol class="references"> <li id="cite_note-1"><span class="mw-cite-backlink"><b><a href="#cite_ref-1">^</a></b></span> <span class="reference-text"><style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#d33)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}</style><cite id="CITEREFNelsonCox2005" class="citation book cs1">Nelson DL, Cox MM (2005). <i>Principles of Biochemistry</i> (4th ed.). 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Freeman. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/0-7167-4339-6" title="Special:BookSources/0-7167-4339-6"><bdi>0-7167-4339-6</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Principles+of+Biochemistry&rft.place=New+York&rft.edition=4th&rft.pub=W.+H.+Freeman&rft.date=2005&rft.isbn=0-7167-4339-6&rft.aulast=Nelson&rft.aufirst=David+L.&rft.au=Cox%2C+Michael+M.&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> <li id="cite_note-2"><span class="mw-cite-backlink"><b><a href="#cite_ref-2">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFFlissiRicartCampartChevalier2020" class="citation journal cs1">Flissi, Areski; Ricart, Emma; Campart, Clémentine; Chevalier, Mickael; Dufresne, Yoann; Michalik, Juraj; Jacques, Philippe; Flahaut, Christophe; Lisacek, Frédérique; Leclère, Valérie; Pupin, Maude (2020). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7145658">"Norine: update of the nonribosomal peptide resource"</a>. <i>Nucleic Acids Research</i>. <b>48</b> (D1): D465–D469. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1093%2Fnar%2Fgkz1000">10.1093/nar/gkz1000</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7145658">7145658</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/31691799">31691799</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nucleic+Acids+Research&rft.atitle=Norine%3A+update+of+the+nonribosomal+peptide+resource&rft.volume=48&rft.issue=D1&rft.pages=D465-D469&rft.date=2020&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC7145658%23id-name%3DPMC&rft_id=info%3Apmid%2F31691799&rft_id=info%3Adoi%2F10.1093%2Fnar%2Fgkz1000&rft.aulast=Flissi&rft.aufirst=Areski&rft.au=Ricart%2C+Emma&rft.au=Campart%2C+Cl%C3%A9mentine&rft.au=Chevalier%2C+Mickael&rft.au=Dufresne%2C+Yoann&rft.au=Michalik%2C+Juraj&rft.au=Jacques%2C+Philippe&rft.au=Flahaut%2C+Christophe&rft.au=Lisacek%2C+Fr%C3%A9d%C3%A9rique&rft.au=Lecl%C3%A8re%2C+Val%C3%A9rie&rft.au=Pupin%2C+Maude&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC7145658&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> <li id="cite_note-3"><span class="mw-cite-backlink"><b><a href="#cite_ref-3">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFRichard_Cammack2009" class="citation web cs1">Richard Cammack, ed. (2009). <a rel="nofollow" class="external text" href="https://web.archive.org/web/20170912194130/http://www.chem.qmul.ac.uk/iubmb/newsletter/2009.html#item35">"Newsletter 2009"</a>. Biochemical Nomenclature Committee of IUPAC and NC-IUBMB. Pyrrolysine. Archived from <a rel="nofollow" class="external text" href="http://www.chem.qmul.ac.uk/iubmb/newsletter/2009.html#item35">the original</a> on 12 September 2017<span class="reference-accessdate">. Retrieved <span class="nowrap">16 April</span> 2012</span>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=unknown&rft.btitle=Newsletter+2009&rft.pages=Pyrrolysine&rft.pub=Biochemical+Nomenclature+Committee+of+IUPAC+and+NC-IUBMB&rft.date=2009&rft_id=http%3A%2F%2Fwww.chem.qmul.ac.uk%2Fiubmb%2Fnewsletter%2F2009.html%23item35&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> <li id="cite_note-pmid20847933-4"><span class="mw-cite-backlink"><b><a href="#cite_ref-pmid20847933_4-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFRotherKrzycki2010" class="citation journal cs1">Rother, Michael; Krzycki, Joseph A. (1 January 2010). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2933860">"Selenocysteine, Pyrrolysine, and the Unique Energy Metabolism of Methanogenic Archaea"</a>. <i>Archaea</i>. <b>2010</b>: 1–14. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1155%2F2010%2F453642">10.1155/2010/453642</a></span>. <a href="/wiki/ISSN_(identifier)" class="mw-redirect" title="ISSN (identifier)">ISSN</a> <a rel="nofollow" class="external text" href="https://search.worldcat.org/issn/1472-3646">1472-3646</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2933860">2933860</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/20847933">20847933</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Archaea&rft.atitle=Selenocysteine%2C+Pyrrolysine%2C+and+the+Unique+Energy+Metabolism+of+Methanogenic+Archaea&rft.volume=2010&rft.pages=1-14&rft.date=2010-01-01&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2933860%23id-name%3DPMC&rft.issn=1472-3646&rft_id=info%3Apmid%2F20847933&rft_id=info%3Adoi%2F10.1155%2F2010%2F453642&rft.aulast=Rother&rft.aufirst=Michael&rft.au=Krzycki%2C+Joseph+A.&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2933860&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> <li id="cite_note-5"><span class="mw-cite-backlink"><b><a href="#cite_ref-5">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFLatham1997" class="citation book cs1">Latham MC (1997). <a rel="nofollow" class="external text" href="https://web.archive.org/web/20121008212843/http://www.fao.org/docrep/W0073e/w0073e04.htm#P1625_217364">"Chapter 8. Body composition, the functions of food, metabolism and energy"</a>. <i>Human nutrition in the developing world</i>. Food and Nutrition Series – No. 29. Rome: Food and Agriculture Organization of the United Nations. Archived from <a rel="nofollow" class="external text" href="http://www.fao.org/docrep/W0073E/w0073e04.htm#P1625_217364">the original</a> on 8 October 2012<span class="reference-accessdate">. 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(September 2010)">page needed</span></a></i>]</sup></span> </li> <li id="cite_note-55"><span class="mw-cite-backlink"><b><a href="#cite_ref-55">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFKozlowski2017" class="citation journal cs1">Kozlowski LP (January 2017). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5210655">"Proteome-p<i>I</i>: proteome isoelectric point database"</a>. <i>Nucleic Acids Research</i>. <b>45</b> (D1): D1112–D1116. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1093%2Fnar%2Fgkw978">10.1093/nar/gkw978</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5210655">5210655</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/27789699">27789699</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nucleic+Acids+Research&rft.atitle=Proteome-pI%3A+proteome+isoelectric+point+database&rft.volume=45&rft.issue=D1&rft.pages=D1112-D1116&rft.date=2017-01&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5210655%23id-name%3DPMC&rft_id=info%3Apmid%2F27789699&rft_id=info%3Adoi%2F10.1093%2Fnar%2Fgkw978&rft.aulast=Kozlowski&rft.aufirst=LP&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5210655&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> <li id="cite_note-Hausman-56"><span class="mw-cite-backlink">^ <a href="#cite_ref-Hausman_56-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Hausman_56-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFHausmanCooper2004" class="citation book cs1">Hausman RE, Cooper GM (2004). <i>The cell: a molecular approach</i>. Washington, D.C.: ASM Press. p. 51. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-87893-214-6" title="Special:BookSources/978-0-87893-214-6"><bdi>978-0-87893-214-6</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=The+cell%3A+a+molecular+approach&rft.place=Washington%2C+D.C.&rft.pages=51&rft.pub=ASM+Press&rft.date=2004&rft.isbn=978-0-87893-214-6&rft.aulast=Hausman&rft.aufirst=Robert+E.&rft.au=Cooper%2C+Geoffrey+M.&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> <li id="cite_note-57"><span class="mw-cite-backlink"><b><a href="#cite_ref-57">^</a></b></span> <span class="reference-text">Codons can also be expressed by: CGN, AGR</span> </li> <li id="cite_note-58"><span class="mw-cite-backlink"><b><a href="#cite_ref-58">^</a></b></span> <span class="reference-text">codons can also be expressed by: CUN, UUR</span> </li> <li id="cite_note-59"><span class="mw-cite-backlink"><b><a href="#cite_ref-59">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFAaslandAbramsAmpeBall2002" class="citation journal cs1">Aasland R, Abrams C, Ampe C, Ball LJ, Bedford MT, Cesareni G, Gimona M, Hurley JH, Jarchau T, Lehto VP, Lemmon MA, Linding R, Mayer BJ, Nagai M, Sudol M, Walter U, Winder SJ (February 2002). "Normalization of nomenclature for peptide motifs as ligands of modular protein domains". <i>FEBS Letters</i>. <b>513</b> (1): 141–144. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1111%2Fj.1432-1033.1968.tb00350.x">10.1111/j.1432-1033.1968.tb00350.x</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11911894">11911894</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=FEBS+Letters&rft.atitle=Normalization+of+nomenclature+for+peptide+motifs+as+ligands+of+modular+protein+domains&rft.volume=513&rft.issue=1&rft.pages=141-144&rft.date=2002-02&rft_id=info%3Adoi%2F10.1111%2Fj.1432-1033.1968.tb00350.x&rft_id=info%3Apmid%2F11911894&rft.aulast=Aasland&rft.aufirst=R&rft.au=Abrams%2C+C&rft.au=Ampe%2C+C&rft.au=Ball%2C+LJ&rft.au=Bedford%2C+MT&rft.au=Cesareni%2C+G&rft.au=Gimona%2C+M&rft.au=Hurley%2C+JH&rft.au=Jarchau%2C+T&rft.au=Lehto%2C+VP&rft.au=Lemmon%2C+MA&rft.au=Linding%2C+R&rft.au=Mayer%2C+BJ&rft.au=Nagai%2C+M&rft.au=Sudol%2C+M&rft.au=Walter%2C+U&rft.au=Winder%2C+SJ&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> <li id="cite_note-60"><span class="mw-cite-backlink"><b><a href="#cite_ref-60">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFIUPAC–IUB_Commission_on_Biochemical_Nomenclature1972" class="citation journal cs1">IUPAC–IUB Commission on Biochemical Nomenclature (1972). <a rel="nofollow" class="external text" href="https://doi.org/10.1351%2Fpac197231040639">"A one-letter notation for amino acid sequences"</a>. <i>Pure and Applied Chemistry</i>. <b>31</b> (4): 641–645. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1351%2Fpac197231040639">10.1351/pac197231040639</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/5080161">5080161</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Pure+and+Applied+Chemistry&rft.atitle=A+one-letter+notation+for+amino+acid+sequences&rft.volume=31&rft.issue=4&rft.pages=641-645&rft.date=1972&rft_id=info%3Adoi%2F10.1351%2Fpac197231040639&rft_id=info%3Apmid%2F5080161&rft.au=IUPAC%E2%80%93IUB+Commission+on+Biochemical+Nomenclature&rft_id=https%3A%2F%2Fdoi.org%2F10.1351%252Fpac197231040639&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> <li id="cite_note-61"><span class="mw-cite-backlink"><b><a href="#cite_ref-61">^</a></b></span> <span class="reference-text">Codons can also be expressed by: CTN, ATH, TTR; MTY, YTR, ATA; MTY, HTA, YTG</span> </li> <li id="cite_note-62"><span class="mw-cite-backlink"><b><a href="#cite_ref-62">^</a></b></span> <span class="reference-text">Codons can also be expressed by: TWY, CAY, TGG</span> </li> <li id="cite_note-63"><span class="mw-cite-backlink"><b><a href="#cite_ref-63">^</a></b></span> <span class="reference-text">Codons can also be expressed by: NTR, VTY</span> </li> <li id="cite_note-64"><span class="mw-cite-backlink"><b><a href="#cite_ref-64">^</a></b></span> <span class="reference-text">Codons can also be expressed by: VAN, WCN, MGY, CGP</span> </li> <li id="cite_note-HGSV_recommendations-65"><span class="mw-cite-backlink"><b><a href="#cite_ref-HGSV_recommendations_65-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite class="citation web cs1"><a rel="nofollow" class="external text" href="http://varnomen.hgvs.org/recommendations/protein/variant/substitution/">"HGVS: Sequence Variant Nomenclature, Protein Recommendations"</a>. <a rel="nofollow" class="external text" href="https://web.archive.org/web/20210924091505/http://varnomen.hgvs.org/recommendations/protein/variant/substitution/">Archived</a> from the original on 24 September 2021<span class="reference-accessdate">. Retrieved <span class="nowrap">23 September</span> 2021</span>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=unknown&rft.btitle=HGVS%3A+Sequence+Variant+Nomenclature%2C+Protein+Recommendations&rft_id=http%3A%2F%2Fvarnomen.hgvs.org%2Frecommendations%2Fprotein%2Fvariant%2Fsubstitution%2F&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> <li id="cite_note-66"><span class="mw-cite-backlink"><b><a href="#cite_ref-66">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFSuchanekRadzikowskaThiele2005" class="citation journal cs1">Suchanek M, Radzikowska A, Thiele C (April 2005). <a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnmeth752">"Photo-leucine and photo-methionine allow identification of protein–protein interactions in living cells"</a>. <i>Nature Methods</i>. <b>2</b> (4): 261–267. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnmeth752">10.1038/nmeth752</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15782218">15782218</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature+Methods&rft.atitle=Photo-leucine+and+photo-methionine+allow+identification+of+protein%E2%80%93protein+interactions+in+living+cells&rft.volume=2&rft.issue=4&rft.pages=261-267&rft.date=2005-04&rft_id=info%3Adoi%2F10.1038%2Fnmeth752&rft_id=info%3Apmid%2F15782218&rft.aulast=Suchanek&rft.aufirst=M&rft.au=Radzikowska%2C+A&rft.au=Thiele%2C+C&rft_id=https%3A%2F%2Fdoi.org%2F10.1038%252Fnmeth752&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> <li id="cite_note-67"><span class="mw-cite-backlink"><b><a href="#cite_ref-67">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFRodninaBeringerWintermeyer2007" class="citation journal cs1">Rodnina MV, Beringer M, Wintermeyer W (January 2007). 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"Past and future perspectives of synthetic peptide libraries". <i>Current Protein & Peptide Science</i>. <b>9</b> (5): 447–467. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.2174%2F138920308785915209">10.2174/138920308785915209</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/18855697">18855697</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Protein+%26+Peptide+Science&rft.atitle=Past+and+future+perspectives+of+synthetic+peptide+libraries&rft.volume=9&rft.issue=5&rft.pages=447-467&rft.date=2008-10&rft_id=info%3Adoi%2F10.2174%2F138920308785915209&rft_id=info%3Apmid%2F18855697&rft.aulast=Marasco&rft.aufirst=D&rft.au=Perretta%2C+G&rft.au=Sabatella%2C+M&rft.au=Ruvo%2C+M&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> <li id="cite_note-142"><span class="mw-cite-backlink"><b><a href="#cite_ref-142">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFKonaraGagnonaClearfieldThompson2010" class="citation journal cs1">Konara S, Gagnona K, Clearfield A, Thompson C, Hartle J, Ericson C, Nelson C (2010). 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Saunders Elsevier.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Biochemical%2C+physiological%2C+%26+molecular+aspects+of+human+nutrition&rft.edition=2nd&rft.pub=Saunders+Elsevier&rft.date=2006&rft.aulast=Stipanuk&rft.aufirst=MH&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> <li id="cite_note-144"><span class="mw-cite-backlink"><b><a href="#cite_ref-144">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFDghaymDhawanArndtsen2001" class="citation journal cs1">Dghaym RD, Dhawan R, Arndtsen BA (September 2001). "The Use of Carbon Monoxide and Imines as Peptide Derivative Synthons: A Facile Palladium-Catalyzed Synthesis of α-Amino Acid Derived Imidazolines". <i>Angewandte Chemie</i>. <b>40</b> (17): 3228–3230. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2F%28SICI%291521-3773%2819980703%2937%3A12%3C1634%3A%3AAID-ANIE1634%3E3.0.CO%3B2-C">10.1002/(SICI)1521-3773(19980703)37:12<1634::AID-ANIE1634>3.0.CO;2-C</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/29712039">29712039</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Angewandte+Chemie&rft.atitle=The+Use+of+Carbon+Monoxide+and+Imines+as+Peptide+Derivative+Synthons%3A+A+Facile+Palladium-Catalyzed+Synthesis+of+%CE%B1-Amino+Acid+Derived+Imidazolines&rft.volume=40&rft.issue=17&rft.pages=3228-3230&rft.date=2001-09&rft_id=info%3Adoi%2F10.1002%2F%28SICI%291521-3773%2819980703%2937%3A12%3C1634%3A%3AAID-ANIE1634%3E3.0.CO%3B2-C&rft_id=info%3Apmid%2F29712039&rft.aulast=Dghaym&rft.aufirst=RD&rft.au=Dhawan%2C+R&rft.au=Arndtsen%2C+BA&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> <li id="cite_note-pmid23959242-145"><span class="mw-cite-backlink"><b><a href="#cite_ref-pmid23959242_145-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFMuñoz-HuertaGuevara-GonzalezContreras-MedinaTorres-Pacheco2013" class="citation journal cs1">Muñoz-Huerta RF, Guevara-Gonzalez RG, Contreras-Medina LM, Torres-Pacheco I, Prado-Olivarez J, Ocampo-Velazquez RV (August 2013). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3812630">"A review of methods for sensing the nitrogen status in plants: advantages, disadvantages and recent advances"</a>. <i>Sensors</i>. <b>13</b> (8). Basel, Switzerland: 10823–43. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2013Senso..1310823M">2013Senso..1310823M</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.3390%2Fs130810823">10.3390/s130810823</a></span>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3812630">3812630</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/23959242">23959242</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Sensors&rft.atitle=A+review+of+methods+for+sensing+the+nitrogen+status+in+plants%3A+advantages%2C+disadvantages+and+recent+advances&rft.volume=13&rft.issue=8&rft.pages=10823-43&rft.date=2013-08&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3812630%23id-name%3DPMC&rft_id=info%3Apmid%2F23959242&rft_id=info%3Adoi%2F10.3390%2Fs130810823&rft_id=info%3Abibcode%2F2013Senso..1310823M&rft.aulast=Mu%C3%B1oz-Huerta&rft.aufirst=RF&rft.au=Guevara-Gonzalez%2C+RG&rft.au=Contreras-Medina%2C+LM&rft.au=Torres-Pacheco%2C+I&rft.au=Prado-Olivarez%2C+J&rft.au=Ocampo-Velazquez%2C+RV&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3812630&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> <li id="cite_note-146"><span class="mw-cite-backlink"><b><a href="#cite_ref-146">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFMartinMalleyManningFuller2002" class="citation journal cs1">Martin PD, Malley DF, Manning G, Fuller L (2002). "Determination of soil organic carbon and nitrogen at thefield level using near-infrared spectroscopy". <i>Canadian Journal of Soil Science</i>. <b>82</b> (4): 413–422. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.4141%2FS01-054">10.4141/S01-054</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Canadian+Journal+of+Soil+Science&rft.atitle=Determination+of+soil+organic+carbon+and+nitrogen+at+thefield+level+using+near-infrared+spectroscopy&rft.volume=82&rft.issue=4&rft.pages=413-422&rft.date=2002&rft_id=info%3Adoi%2F10.4141%2FS01-054&rft.aulast=Martin&rft.aufirst=PD&rft.au=Malley%2C+DF&rft.au=Manning%2C+G&rft.au=Fuller%2C+L&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></span> </li> </ol></div></div> <div class="mw-heading mw-heading2"><h2 id="Further_reading">Further reading</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=42" title="Edit section: Further reading"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239549316">.mw-parser-output .refbegin{margin-bottom:0.5em}.mw-parser-output .refbegin-hanging-indents>ul{margin-left:0}.mw-parser-output .refbegin-hanging-indents>ul>li{margin-left:0;padding-left:3.2em;text-indent:-3.2em}.mw-parser-output .refbegin-hanging-indents ul,.mw-parser-output .refbegin-hanging-indents ul li{list-style:none}@media(max-width:720px){.mw-parser-output .refbegin-hanging-indents>ul>li{padding-left:1.6em;text-indent:-1.6em}}.mw-parser-output .refbegin-columns{margin-top:0.3em}.mw-parser-output .refbegin-columns ul{margin-top:0}.mw-parser-output .refbegin-columns li{page-break-inside:avoid;break-inside:avoid-column}@media screen{.mw-parser-output .refbegin{font-size:90%}}</style><div class="refbegin" style=""> <ul><li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFTymoczko2012" class="citation book cs1">Tymoczko JL (2012). <a rel="nofollow" class="external text" href="https://archive.org/details/biochemistryseve00berg/page/n61">"Protein Composition and Structure"</a>. <span class="id-lock-limited" title="Free access subject to limited trial, subscription normally required"><a rel="nofollow" class="external text" href="https://archive.org/details/biochemistryseve00berg"><i>Biochemistry</i></a></span>. New York: W. H. Freeman and company. pp. 28–31. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/9781429229364" title="Special:BookSources/9781429229364"><bdi>9781429229364</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Protein+Composition+and+Structure&rft.btitle=Biochemistry&rft.place=New+York&rft.pages=28-31&rft.pub=W.+H.+Freeman+and+company&rft.date=2012&rft.isbn=9781429229364&rft.aulast=Tymoczko&rft.aufirst=John+L.&rft_id=https%3A%2F%2Farchive.org%2Fdetails%2Fbiochemistryseve00berg%2Fpage%2Fn61&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></li> <li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFDoolittle1989" class="citation book cs1"><a href="/wiki/Russell_Doolittle" title="Russell Doolittle">Doolittle RF</a> (1989). "Redundancies in protein sequences". In Fasman GD (ed.). <i>Predictions of Protein Structure and the Principles of Protein Conformation</i>. New York: <a href="/wiki/Plenum_Press" class="mw-redirect" title="Plenum Press">Plenum Press</a>. pp. 599–623. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-306-43131-9" title="Special:BookSources/978-0-306-43131-9"><bdi>978-0-306-43131-9</bdi></a>. <a href="/wiki/LCCN_(identifier)" class="mw-redirect" title="LCCN (identifier)">LCCN</a> <a rel="nofollow" class="external text" href="https://lccn.loc.gov/89008555">89008555</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Redundancies+in+protein+sequences&rft.btitle=Predictions+of+Protein+Structure+and+the+Principles+of+Protein+Conformation&rft.place=New+York&rft.pages=599-623&rft.pub=Plenum+Press&rft.date=1989&rft_id=info%3Alccn%2F89008555&rft.isbn=978-0-306-43131-9&rft.aulast=Doolittle&rft.aufirst=RF&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></li> <li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFNelsonCox2000" class="citation book cs1">Nelson DL, Cox MM (2000). <span class="id-lock-registration" title="Free registration required"><a rel="nofollow" class="external text" href="https://archive.org/details/lehningerprincip01lehn"><i>Lehninger Principles of Biochemistry</i></a></span> (3rd ed.). <a href="/wiki/Worth_Publishers" class="mw-redirect" title="Worth Publishers">Worth Publishers</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-1-57259-153-0" title="Special:BookSources/978-1-57259-153-0"><bdi>978-1-57259-153-0</bdi></a>. <a href="/wiki/LCCN_(identifier)" class="mw-redirect" title="LCCN (identifier)">LCCN</a> <a rel="nofollow" class="external text" href="https://lccn.loc.gov/99049137">99049137</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Lehninger+Principles+of+Biochemistry&rft.edition=3rd&rft.pub=Worth+Publishers&rft.date=2000&rft_id=info%3Alccn%2F99049137&rft.isbn=978-1-57259-153-0&rft.aulast=Nelson&rft.aufirst=David+L.&rft.au=Cox%2C+Michael+M.&rft_id=https%3A%2F%2Farchive.org%2Fdetails%2Flehningerprincip01lehn&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></li> <li><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFMeierhenrich2008" class="citation book cs1"><a href="/wiki/Uwe_Meierhenrich" title="Uwe Meierhenrich">Meierhenrich U</a> (2008). <a rel="nofollow" class="external text" href="https://web.archive.org/web/20120112005425/http://rogov.zwz.ru/Macroevolution/amino.pdf"><i>Amino acids and the asymmetry of life</i></a> <span class="cs1-format">(PDF)</span>. Berlin: <a href="/wiki/Springer_Verlag" class="mw-redirect" title="Springer Verlag">Springer Verlag</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-3-540-76885-2" title="Special:BookSources/978-3-540-76885-2"><bdi>978-3-540-76885-2</bdi></a>. <a href="/wiki/LCCN_(identifier)" class="mw-redirect" title="LCCN (identifier)">LCCN</a> <a rel="nofollow" class="external text" href="https://lccn.loc.gov/2008930865">2008930865</a>. Archived from <a rel="nofollow" class="external text" href="http://rogov.zwz.ru/Macroevolution/amino.pdf">the original</a> <span class="cs1-format">(PDF)</span> on 12 January 2012.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Amino+acids+and+the+asymmetry+of+life&rft.place=Berlin&rft.pub=Springer+Verlag&rft.date=2008&rft_id=info%3Alccn%2F2008930865&rft.isbn=978-3-540-76885-2&rft.aulast=Meierhenrich&rft.aufirst=Uwe&rft_id=http%3A%2F%2Frogov.zwz.ru%2FMacroevolution%2Famino.pdf&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid" class="Z3988"></span></li></ul> </div> <div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid&action=edit&section=43" title="Edit section: External links"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><span class="noviewer" typeof="mw:File"><a href="/wiki/File:Commons-logo.svg" class="mw-file-description"><img alt="" src="//upload.wikimedia.org/wikipedia/en/thumb/4/4a/Commons-logo.svg/12px-Commons-logo.svg.png" decoding="async" width="12" height="16" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/4/4a/Commons-logo.svg/18px-Commons-logo.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/4/4a/Commons-logo.svg/24px-Commons-logo.svg.png 2x" data-file-width="1024" data-file-height="1376" /></a></span> Media related to <a href="https://commons.wikimedia.org/wiki/Category:Amino_acids" class="extiw" title="commons:Category:Amino acids">Amino acids</a> at Wikimedia Commons</li></ul> <div class="navbox-styles"><style data-mw-deduplicate="TemplateStyles:r1129693374">.mw-parser-output .hlist dl,.mw-parser-output .hlist ol,.mw-parser-output .hlist ul{margin:0;padding:0}.mw-parser-output .hlist dd,.mw-parser-output .hlist dt,.mw-parser-output .hlist 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.navbar{display:none!important}}</style><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Proteinogenic_amino_acids" title="Template:Proteinogenic amino acids"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Proteinogenic_amino_acids" title="Template talk:Proteinogenic amino acids"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Proteinogenic_amino_acids" title="Special:EditPage/Template:Proteinogenic amino acids"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Encoded_(proteinogenic)_amino_acids" style="font-size:114%;margin:0 4em"><a href="/wiki/Proteinogenic_amino_acid" title="Proteinogenic amino acid">Encoded (proteinogenic) amino acids</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">General topics</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Protein" title="Protein">Protein</a></li> <li><a href="/wiki/Peptide" title="Peptide">Peptide</a></li> <li><a href="/wiki/Genetic_code" title="Genetic code">Genetic code</a></li></ul> </div></td><td class="noviewer navbox-image" rowspan="2" style="width:1px;padding:0 0 0 2px"><div><span typeof="mw:File"><a href="/wiki/File:L-amino_acid_any.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/0/0e/L-amino_acid_any.png/182px-L-amino_acid_any.png" decoding="async" width="182" height="160" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/0/0e/L-amino_acid_any.png/273px-L-amino_acid_any.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/0/0e/L-amino_acid_any.png/364px-L-amino_acid_any.png 2x" data-file-width="728" data-file-height="640" /></a></span></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">By properties</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Aliphatic_compound" title="Aliphatic compound">Aliphatic</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Branched-chain_amino_acid" title="Branched-chain amino acid">Branched-chain amino acids</a> (<a href="/wiki/Valine" title="Valine">Valine</a></li> <li><a href="/wiki/Isoleucine" title="Isoleucine">Isoleucine</a></li> <li><a href="/wiki/Leucine" title="Leucine">Leucine</a>)</li> <li><a href="/wiki/Methionine" title="Methionine">Methionine</a></li> <li><a href="/wiki/Alanine" title="Alanine">Alanine</a></li> <li><a href="/wiki/Proline" title="Proline">Proline</a></li> <li><a href="/wiki/Glycine" title="Glycine">Glycine</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Aromatic_amino_acid" title="Aromatic amino acid">Aromatic</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Histidine" title="Histidine">Histidine</a></li> <li><a href="/wiki/Tyrosine" title="Tyrosine">Tyrosine</a></li> <li><a href="/wiki/Tryptophan" title="Tryptophan">Tryptophan</a></li> <li><a href="/wiki/Phenylalanine" title="Phenylalanine">Phenylalanine</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Chemical_polarity" title="Chemical polarity">Polar</a>, uncharged</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Asparagine" title="Asparagine">Asparagine</a></li> <li><a href="/wiki/Glutamine" title="Glutamine">Glutamine</a></li> <li><a href="/wiki/Serine" title="Serine">Serine</a></li> <li><a href="/wiki/Threonine" title="Threonine">Threonine</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Positive charge (p<i>K</i><sub>a</sub>)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Lysine" title="Lysine">Lysine</a> (≈10.8)</li> <li><a href="/wiki/Arginine" title="Arginine">Arginine</a> (≈12.5)</li> <li><a href="/wiki/Histidine" title="Histidine">Histidine</a> (≈6.1)</li> <li><a href="/wiki/Pyrrolysine" title="Pyrrolysine">Pyrrolysine</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Negative charge (p<i>K</i><sub>a</sub>)</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Aspartic_acid" title="Aspartic acid">Aspartic acid</a> (≈3.9)</li> <li><a href="/wiki/Glutamic_acid" title="Glutamic acid">Glutamic acid</a> (≈4.1)</li> <li><a href="/wiki/Selenocysteine" title="Selenocysteine">Selenocysteine</a> (≈5.4)</li> <li><a href="/wiki/Cysteine" title="Cysteine">Cysteine</a> (≈8.3)</li> <li><a href="/wiki/Tyrosine" title="Tyrosine">Tyrosine</a> (≈10.1)</li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><td class="navbox-abovebelow" colspan="3"><div><div class="hlist" style="font-size:88%;"> <ul><li><b><a href="/wiki/Amino_acids" class="mw-redirect" title="Amino acids">Amino acids</a> types</b>: <a href="/wiki/Template:Encoded_amino_acids" class="mw-redirect" title="Template:Encoded amino acids">Encoded (proteins)</a></li> <li><a href="/wiki/Essential_amino_acids" class="mw-redirect" title="Essential amino acids">Essential</a></li> <li><a href="/wiki/Template:Non-proteinogenic_amino_acids" title="Template:Non-proteinogenic amino acids">Non-proteinogenic</a></li> <li><a href="/wiki/Ketogenic_amino_acids" class="mw-redirect" title="Ketogenic amino acids">Ketogenic</a></li> <li><a href="/wiki/Glucogenic_amino_acids" class="mw-redirect" title="Glucogenic amino acids">Glucogenic</a></li> <li><a href="/wiki/Secondary_amino_acid" title="Secondary amino acid">Secondary amino</a></li> <li><a href="/wiki/Imino_acid" title="Imino acid">Imino acids</a></li> <li><a href="/wiki/D-amino_acids" class="mw-redirect" title="D-amino acids">D-amino acids</a></li> <li><a href="/wiki/Dehydroamino_acid" title="Dehydroamino acid">Dehydroamino acids</a></li></ul> </div></div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235"></div><div role="navigation" class="navbox" aria-labelledby="Chemical_bonds" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="3"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239400231"><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Chemical_bonds" title="Template:Chemical bonds"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Chemical_bonds" title="Template talk:Chemical bonds"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Chemical_bonds" title="Special:EditPage/Template:Chemical bonds"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Chemical_bonds" style="font-size:114%;margin:0 4em"><a href="/wiki/Chemical_bond" title="Chemical bond">Chemical bonds</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Intramolecular_force" title="Intramolecular force">Intramolecular</a><br />(strong)</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Covalent_bond" title="Covalent bond">Covalent</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Electron_deficiency" title="Electron deficiency">Electron deficiency</a> <ul><li><a href="/wiki/Three-center_two-electron_bond" title="Three-center two-electron bond">3c–2e</a></li> <li><a href="/wiki/Four-center_two-electron_bond" title="Four-center two-electron bond">4c–2e</a></li> <li><a href="/wiki/Eight-center_two-electron_bond" class="mw-redirect" title="Eight-center two-electron bond">8c–2e</a></li></ul></li> <li><a href="/wiki/Hypervalent_molecule" title="Hypervalent molecule">Hypervalence</a> <ul><li><a href="/wiki/Three-center_four-electron_bond" title="Three-center four-electron bond">3c–4e</a></li></ul></li> <li><a href="/wiki/Agostic_interaction" title="Agostic interaction">Agostic</a></li> <li><a href="/wiki/Bent_bond" title="Bent bond">Bent</a></li> <li><a href="/wiki/Coordinate_covalent_bond" title="Coordinate covalent bond">Coordinate (dipolar)</a></li> <li><a href="/wiki/Pi_backbonding" title="Pi backbonding">Pi backbond</a></li> <li><a href="/wiki/Metal%E2%80%93ligand_multiple_bond" title="Metal–ligand multiple bond">Metal–ligand multiple bond</a></li> <li><a href="/wiki/Charge-shift_bond" title="Charge-shift bond">Charge-shift</a></li> <li><a href="/wiki/Hapticity" title="Hapticity">Hapticity</a></li> <li><a href="/wiki/Conjugated_system" title="Conjugated system">Conjugation</a></li> <li><a href="/wiki/Hyperconjugation" title="Hyperconjugation">Hyperconjugation</a></li> <li><a href="/wiki/Aromaticity" title="Aromaticity">Aromaticity</a> <ul><li><a href="/wiki/Homoaromaticity" title="Homoaromaticity">homo</a></li> <li><a href="/wiki/Bicycloaromaticity" title="Bicycloaromaticity">bicyclo</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Metallic_bonding" title="Metallic bonding">Metallic</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Metal_aromaticity" title="Metal aromaticity">Metal aromaticity</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Ionic_bonding" title="Ionic bonding">Ionic</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li class="mw-empty-elt"></li></ul> </div></td></tr></tbody></table><div></div></td><td class="noviewer navbox-image" rowspan="4" style="width:1px;padding:0 0 0 2px"><div><span typeof="mw:File"><a href="/wiki/File:Ligatio-covalens.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/2/21/Ligatio-covalens.svg/200px-Ligatio-covalens.svg.png" decoding="async" width="200" height="89" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/2/21/Ligatio-covalens.svg/300px-Ligatio-covalens.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/2/21/Ligatio-covalens.svg/400px-Ligatio-covalens.svg.png 2x" data-file-width="597" data-file-height="265" /></a></span><br /><span typeof="mw:File"><a href="/wiki/File:Chemfm_carbon_monoxide_3_1.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/7/77/Chemfm_carbon_monoxide_3_1.svg/200px-Chemfm_carbon_monoxide_3_1.svg.png" decoding="async" width="200" height="113" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/7/77/Chemfm_carbon_monoxide_3_1.svg/300px-Chemfm_carbon_monoxide_3_1.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/7/77/Chemfm_carbon_monoxide_3_1.svg/400px-Chemfm_carbon_monoxide_3_1.svg.png 2x" data-file-width="99" data-file-height="56" /></a></span><br /><span typeof="mw:File"><a href="/wiki/File:Pi-Bond.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/7/70/Pi-Bond.svg/200px-Pi-Bond.svg.png" decoding="async" width="200" height="113" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/7/70/Pi-Bond.svg/300px-Pi-Bond.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/7/70/Pi-Bond.svg/400px-Pi-Bond.svg.png 2x" data-file-width="1920" data-file-height="1080" /></a></span></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Intermolecular_force" title="Intermolecular force">Intermolecular</a><br />(weak)</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Van_der_Waals_force" title="Van der Waals force">Van der Waals<br />forces</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/London_dispersion_force" title="London dispersion force">London dispersion</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Hydrogen_bond" title="Hydrogen bond">Hydrogen</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Low-barrier_hydrogen_bond" title="Low-barrier hydrogen bond">Low-barrier</a></li> <li><a href="/wiki/Resonance-assisted_hydrogen_bond" class="mw-redirect" title="Resonance-assisted hydrogen bond">Resonance-assisted</a></li> <li><a href="/wiki/Symmetric_hydrogen_bond" title="Symmetric hydrogen bond">Symmetric</a></li> <li><a href="/wiki/Dihydrogen_bond" title="Dihydrogen bond">Dihydrogen bonds</a></li> <li><a href="/wiki/C%E2%80%93H%C2%B7%C2%B7%C2%B7O_interaction" title="C–H···O interaction">C–H···O interaction</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Non-covalent_interactions" class="mw-redirect" title="Non-covalent interactions">Noncovalent</a><br />other</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Mechanically_interlocked_molecular_architectures" title="Mechanically interlocked molecular architectures">Mechanical</a></li> <li><a href="/wiki/Halogen_bond" title="Halogen bond">Halogen</a></li> <li><a href="/wiki/Chalcogen_bond" title="Chalcogen bond">Chalcogen</a></li> <li><a href="/wiki/Metallophilic_interaction" title="Metallophilic interaction">Metallophilic</a> (<a href="/wiki/Aurophilicity" title="Aurophilicity">aurophilic</a>)</li> <li><a href="/wiki/Intercalation_(chemistry)" title="Intercalation (chemistry)">Intercalation</a></li> <li><a href="/wiki/Stacking_(chemistry)" title="Stacking (chemistry)">Stacking</a></li> <li><a href="/wiki/Cation%E2%80%93pi_interaction" class="mw-redirect" title="Cation–pi interaction">Cation–pi</a></li> <li><a href="/wiki/Cation%E2%80%93pi_interaction#Anion–π_interaction" class="mw-redirect" title="Cation–pi interaction">Anion–pi</a></li> <li><a href="/wiki/Salt_bridge_(protein_and_supramolecular)" title="Salt bridge (protein and supramolecular)">Salt bridge</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Bond_cleavage" title="Bond cleavage">Bond cleavage</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Heterolysis_(chemistry)" title="Heterolysis (chemistry)">Heterolysis</a></li> <li><a href="/wiki/Homolysis_(chemistry)" title="Homolysis (chemistry)">Homolysis</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Electron_counting" title="Electron counting">Electron counting</a> rules</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Aromaticity" title="Aromaticity">Aromaticity</a> <ul><li><a href="/wiki/H%C3%BCckel%27s_rule" title="Hückel's rule">Hückel's rule</a></li> <li><a href="/wiki/Baird%27s_rule" title="Baird's rule">Baird's rule</a></li> <li><a href="/wiki/M%C3%B6bius_aromaticity" title="Möbius aromaticity">Möbius</a></li> <li><a href="/wiki/Spherical_aromaticity" title="Spherical aromaticity">spherical</a></li></ul></li> <li><a href="/wiki/Polyhedral_skeletal_electron_pair_theory" title="Polyhedral skeletal electron pair theory">Polyhedral skeletal electron pair theory</a></li> <li><a href="/wiki/Jemmis_mno_rules" title="Jemmis mno rules">Jemmis mno rules</a></li></ul> </div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235"></div><div role="navigation" class="navbox" aria-labelledby="Protein_primary_structure_and_posttranslational_modifications" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239400231"><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Protein_primary_structure" title="Template:Protein primary structure"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Protein_primary_structure" title="Template talk:Protein primary structure"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Protein_primary_structure" title="Special:EditPage/Template:Protein primary structure"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Protein_primary_structure_and_posttranslational_modifications" style="font-size:114%;margin:0 4em"><a href="/wiki/Protein_primary_structure" title="Protein primary structure">Protein primary structure</a> and <a href="/wiki/Posttranslational_modification" class="mw-redirect" title="Posttranslational modification">posttranslational modifications</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">General</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Peptide_bond" title="Peptide bond">Peptide bond</a></li> <li><a href="/wiki/Protein_biosynthesis" title="Protein biosynthesis">Protein biosynthesis</a></li> <li><a href="/wiki/Proteolysis" title="Proteolysis">Proteolysis</a></li> <li><a href="/wiki/Racemization" title="Racemization">Racemization</a></li> <li><a href="/w/index.php?title=N%E2%80%93O_acyl_shift&action=edit&redlink=1" class="new" title="N–O acyl shift (page does not exist)">N–O acyl shift</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/N_terminus" class="mw-redirect" title="N terminus">N terminus</a></th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Acetylation" title="Acetylation">Acetylation</a></li> <li><a href="/wiki/Carbamylation" class="mw-redirect" title="Carbamylation">Carbamylation</a></li> <li><a href="/wiki/Formylation" title="Formylation">Formylation</a></li> <li><a href="/wiki/Glycation" title="Glycation">Glycation</a></li> <li><a href="/wiki/Methylation" title="Methylation">Methylation</a></li> <li><a href="/wiki/Myristoylation" title="Myristoylation">Myristoylation</a> (Gly)</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/C_terminus" class="mw-redirect" title="C terminus">C terminus</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Amide" title="Amide">Amidation</a></li> <li><a href="/wiki/Glycophosphatidylinositol" class="mw-redirect" title="Glycophosphatidylinositol">Glycosyl phosphatidylinositol (GPI)</a></li> <li><a href="/w/index.php?title=O-methylation&action=edit&redlink=1" class="new" title="O-methylation (page does not exist)">O-methylation</a></li> <li><a href="/wiki/Detyrosination" title="Detyrosination">Detyrosination</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Single specific <a class="mw-selflink selflink">AAs</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Serine" title="Serine">Serine</a>/<a href="/wiki/Threonine" title="Threonine">Threonine</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Phosphorylation" title="Phosphorylation">Phosphorylation</a></li> <li><a href="/wiki/Dephosphorylation" title="Dephosphorylation">Dephosphorylation</a></li> <li><a href="/wiki/Glycosylation" title="Glycosylation">Glycosylation</a></li> <li><a href="/wiki/O-GlcNAc" title="O-GlcNAc"><i>O</i>-GlcNAc</a></li> <li><a href="/wiki/ADP-ribosylation" title="ADP-ribosylation">ADP-ribosylation</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Tyrosine" title="Tyrosine">Tyrosine</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Phosphorylation" title="Phosphorylation">Phosphorylation</a></li> <li><a href="/wiki/Dephosphorylation" title="Dephosphorylation">Dephosphorylation</a></li> <li><a href="/wiki/ADP-ribosylation" title="ADP-ribosylation">ADP-ribosylation</a></li> <li><a href="/wiki/Tyrosine_sulfation" title="Tyrosine sulfation">Sulfation</a></li> <li><a href="/wiki/Porphyrin" title="Porphyrin">Porphyrin ring linkage</a></li> <li><a href="/wiki/Adenylylation" title="Adenylylation">Adenylylation</a></li> <li><a href="/wiki/Flavin_group" title="Flavin group">Flavin linkage</a></li> <li><a href="/wiki/Topaquinone" title="Topaquinone">Topaquinone (TPQ) formation</a></li> <li><a href="/wiki/Detyrosination" title="Detyrosination">Detyrosination</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Cysteine" title="Cysteine">Cysteine</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Palmitoylation" title="Palmitoylation">Palmitoylation</a></li> <li><a href="/wiki/Prenylation" title="Prenylation">Prenylation</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Aspartate" class="mw-redirect" title="Aspartate">Aspartate</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Deamidation" title="Deamidation">Succinimide formation</a></li> <li><a href="/wiki/ADP-ribosylation" title="ADP-ribosylation">ADP-ribosylation</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">Glutamate</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Carboxylation" title="Carboxylation">Carboxylation</a></li> <li><a href="/wiki/ADP-ribosylation" title="ADP-ribosylation">ADP-ribosylation</a></li> <li><a href="/wiki/Methylation" title="Methylation">Methylation</a></li> <li><a href="/wiki/Polyglutamylation" title="Polyglutamylation">Polyglutamylation</a></li> <li><a href="/wiki/Polyglycylation" title="Polyglycylation">Polyglycylation</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Asparagine" title="Asparagine">Asparagine</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Deamidation" title="Deamidation">Deamidation</a></li> <li><a href="/wiki/Glycosylation" title="Glycosylation">Glycosylation</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Glutamine" title="Glutamine">Glutamine</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Transglutamination" class="mw-redirect" title="Transglutamination">Transglutamination</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Lysine" title="Lysine">Lysine</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Methylation" title="Methylation">Methylation</a></li> <li><a href="/wiki/Acetylation" title="Acetylation">Acetylation</a></li> <li><a href="/wiki/Acylation" title="Acylation">Acylation</a></li> <li><a href="/wiki/Adenylylation" title="Adenylylation">Adenylylation</a></li> <li><a href="/wiki/Hydroxylation" title="Hydroxylation">Hydroxylation</a></li> <li><a href="/wiki/Ubiquitination" class="mw-redirect" title="Ubiquitination">Ubiquitination</a></li> <li><a href="/wiki/SUMO_protein" title="SUMO protein">Sumoylation</a></li> <li><a href="/wiki/ADP-ribosylation" title="ADP-ribosylation">ADP-ribosylation</a></li> <li><a href="/wiki/Deamination" title="Deamination">Deamination</a></li> <li><a href="/wiki/Allysine" title="Allysine">Oxidative deamination to aldehyde</a></li> <li><a href="/wiki/O-glycosylation" class="mw-redirect" title="O-glycosylation"><i>O</i>-glycosylation</a></li> <li><a href="/wiki/Imine" title="Imine">Imine formation</a></li> <li><a href="/wiki/Glycation" title="Glycation">Glycation</a></li> <li><a href="/wiki/Carbamylation" class="mw-redirect" title="Carbamylation">Carbamylation</a></li> <li><a href="/wiki/Succinylation" title="Succinylation">Succinylation</a></li> <li><a href="/w/index.php?title=Lactylation&action=edit&redlink=1" class="new" title="Lactylation (page does not exist)">Lactylation</a></li> <li><a href="/wiki/Propionylation" title="Propionylation">Propionylation</a></li> <li><a href="/w/index.php?title=Butyrylation&action=edit&redlink=1" class="new" title="Butyrylation (page does not exist)">Butyrylation</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Arginine" title="Arginine">Arginine</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Citrullination" title="Citrullination">Citrullination</a></li> <li><a href="/wiki/Methylation" title="Methylation">Methylation</a></li> <li><a href="/wiki/ADP-ribosylation" title="ADP-ribosylation">ADP-ribosylation</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Proline" title="Proline">Proline</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Hydroxylation" title="Hydroxylation">Hydroxylation</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Histidine" title="Histidine">Histidine</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Diphthamide" title="Diphthamide">Diphthamide</a> formation</li> <li><a href="/wiki/Adenylylation" title="Adenylylation">Adenylylation</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Tryptophan" title="Tryptophan">Tryptophan</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Glycosylation#C-mannosylation" title="Glycosylation">C-mannosylation</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Crosslinks between two <a class="mw-selflink selflink">AAs</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Cysteine" title="Cysteine">Cysteine</a>–<a href="/wiki/Cysteine" title="Cysteine">Cysteine</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Disulfide_bond" class="mw-redirect" title="Disulfide bond">Disulfide bond</a></li> <li><a href="/wiki/ADP-ribosylation" title="ADP-ribosylation">ADP-ribosylation</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Methionine" title="Methionine">Methionine</a>–<a href="/wiki/Hydroxylysine" title="Hydroxylysine">Hydroxylysine</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Sulfilimine_bond" class="mw-redirect" title="Sulfilimine bond">Sulfilimine bond</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Lysine" title="Lysine">Lysine</a>–<a href="/wiki/Tyrosine" title="Tyrosine">Tyrosine</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/w/index.php?title=Lysine_tyrosylquinone&action=edit&redlink=1" class="new" title="Lysine tyrosylquinone (page does not exist)">Lysine tyrosylquinone (LTQ) formation</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Tryptophan" title="Tryptophan">Tryptophan</a>–<a href="/wiki/Tryptophan" title="Tryptophan">Tryptophan</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Tryptophan_tryptophylquinone" title="Tryptophan tryptophylquinone">Tryptophan tryptophylquinone (TTQ) formation</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Crosslinks between three <a class="mw-selflink selflink">AAs</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Serine" title="Serine">Serine</a>–<a href="/wiki/Tyrosine" title="Tyrosine">Tyrosine</a>–<a href="/wiki/Glycine" title="Glycine">Glycine</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Green_Fluorescent_Protein#Autocatalytic_formation_of_the_chromophore_in_wtGFP" class="mw-redirect" title="Green Fluorescent Protein">p-Hydroxybenzylidene-imidazolinone (HBI) formation</a> (chromophore)</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Histidine" title="Histidine">Histidine</a>–<a href="/wiki/Tyrosine" title="Tyrosine">Tyrosine</a>–<a href="/wiki/Glycine" title="Glycine">Glycine</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Kaede_(protein)" title="Kaede (protein)">4-(p-hydroxybenzylidene)-5-imidazolinone (HBI) formation</a> (chromophore)</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Alanine" title="Alanine">Alanine</a>–<a href="/wiki/Serine" title="Serine">Serine</a>–<a href="/wiki/Glycine" title="Glycine">Glycine</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Histidine_ammonia-lyase" title="Histidine ammonia-lyase">Methylidene-imidazolone (MIO) formation</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Crosslinks between four <a class="mw-selflink selflink">AAs</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="Allysine–Allysine–Allysine–Lysine" scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Allysine" title="Allysine">Allysine</a>–<a href="/wiki/Allysine" title="Allysine">Allysine</a>–<a href="/wiki/Allysine" title="Allysine">Allysine</a>–<a href="/wiki/Lysine" title="Lysine">Lysine</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Desmosine" title="Desmosine">Desmosine</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235"></div><div role="navigation" class="navbox" aria-labelledby="Metabolism:_Protein_metabolism,_synthesis_and_catabolism_enzymes" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239400231"><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Amino_acid_metabolism_enzymes" title="Template:Amino acid metabolism enzymes"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Amino_acid_metabolism_enzymes" title="Template talk:Amino acid metabolism enzymes"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Amino_acid_metabolism_enzymes" title="Special:EditPage/Template:Amino acid metabolism enzymes"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Metabolism:_Protein_metabolism,_synthesis_and_catabolism_enzymes" style="font-size:114%;margin:0 4em"><a href="/wiki/Metabolism" title="Metabolism">Metabolism</a>: <a href="/wiki/Protein_metabolism" title="Protein metabolism">Protein metabolism</a>, <a href="/wiki/Amino_acid_synthesis" title="Amino acid synthesis">synthesis</a> and catabolism <a href="/wiki/Enzyme" title="Enzyme">enzymes</a></div></th></tr><tr><td class="navbox-abovebelow" colspan="2"><div><i><a href="/wiki/Essential_amino_acid" title="Essential amino acid">Essential amino acids</a> are in Capitals</i></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Ketogenic_amino_acid" title="Ketogenic amino acid">K</a>→<a href="/wiki/Acetyl-CoA" title="Acetyl-CoA">acetyl-CoA</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Lysine" title="Lysine">LYSINE</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Saccharopine_dehydrogenase" title="Saccharopine dehydrogenase">Saccharopine dehydrogenase</a></li> <li><a href="/wiki/Glutaryl-CoA_dehydrogenase" title="Glutaryl-CoA dehydrogenase">Glutaryl-CoA dehydrogenase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Leucine" title="Leucine">LEUCINE</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/3-Hydroxybutyryl-CoA_dehydrogenase" title="3-Hydroxybutyryl-CoA dehydrogenase">3-Hydroxybutyryl-CoA dehydrogenase</a></li> <li><a href="/wiki/Branched-chain_amino_acid_aminotransferase" title="Branched-chain amino acid aminotransferase">Branched-chain amino acid aminotransferase</a></li> <li><a href="/wiki/Branched-chain_alpha-keto_acid_dehydrogenase_complex" title="Branched-chain alpha-keto acid dehydrogenase complex">Branched-chain alpha-keto acid dehydrogenase complex</a></li> <li><a href="/wiki/Enoyl-CoA_hydratase" title="Enoyl-CoA hydratase">Enoyl-CoA hydratase</a></li> <li><a href="/wiki/3-hydroxy-3-methylglutaryl-CoA_lyase" class="mw-redirect" title="3-hydroxy-3-methylglutaryl-CoA lyase">HMG-CoA lyase</a></li> <li><a href="/wiki/HMG-CoA_reductase" title="HMG-CoA reductase">HMG-CoA reductase</a></li> <li><a href="/wiki/Isovaleryl_coenzyme_A_dehydrogenase" class="mw-redirect" title="Isovaleryl coenzyme A dehydrogenase">Isovaleryl coenzyme A dehydrogenase</a></li> <li><a href="/wiki/%CE%91-ketoisocaproate_dioxygenase" class="mw-redirect" title="Α-ketoisocaproate dioxygenase">α-Ketoisocaproate dioxygenase</a></li> <li><a href="/wiki/Leucine_2,3-aminomutase" title="Leucine 2,3-aminomutase">Leucine 2,3-aminomutase</a></li> <li><a href="/wiki/Methylcrotonyl-CoA_carboxylase" title="Methylcrotonyl-CoA carboxylase">Methylcrotonyl-CoA carboxylase</a></li> <li><a href="/wiki/Methylglutaconyl-CoA_hydratase" title="Methylglutaconyl-CoA hydratase">Methylglutaconyl-CoA hydratase</a></li></ul> <p>(See <a href="/wiki/Template:Leucine_metabolism_in_humans" title="Template:Leucine metabolism in humans">Template:Leucine metabolism in humans</a> – this diagram does not include the pathway for β-leucine synthesis via leucine 2,3-aminomutase) </p> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Tryptophan" title="Tryptophan">TRYPTOPHAN</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Indoleamine_2,3-dioxygenase" title="Indoleamine 2,3-dioxygenase">Indoleamine 2,3-dioxygenase</a>/<a href="/wiki/Tryptophan_2,3-dioxygenase" title="Tryptophan 2,3-dioxygenase">Tryptophan 2,3-dioxygenase</a></li> <li><a href="/wiki/Arylformamidase" title="Arylformamidase">Arylformamidase</a></li> <li><a href="/wiki/Kynureninase" title="Kynureninase">Kynureninase</a></li> <li><a href="/wiki/3-hydroxyanthranilate_oxidase" title="3-hydroxyanthranilate oxidase">3-hydroxyanthranilate oxidase</a></li> <li><a href="/wiki/Aminocarboxymuconate-semialdehyde_decarboxylase" title="Aminocarboxymuconate-semialdehyde decarboxylase">Aminocarboxymuconate-semialdehyde decarboxylase</a></li> <li><a href="/wiki/Aminomuconate-semialdehyde_dehydrogenase" title="Aminomuconate-semialdehyde dehydrogenase">Aminomuconate-semialdehyde dehydrogenase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Phenylalanine" title="Phenylalanine">PHENYLALANINE</a>→<a href="/wiki/Tyrosine" title="Tyrosine">tyrosine</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li>(see below)</li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Glucogenic_amino_acid" title="Glucogenic amino acid">G</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="G→pyruvate→citrate" scope="row" class="navbox-group" style="width:1%">G→<a href="/wiki/Pyruvate" class="mw-redirect" title="Pyruvate">pyruvate</a><br />→<a href="/wiki/Citrate" class="mw-redirect" title="Citrate">citrate</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Glycine" title="Glycine">glycine</a>→<a href="/wiki/Serine" title="Serine">serine</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Serine_hydroxymethyltransferase" title="Serine hydroxymethyltransferase">Serine hydroxymethyltransferase</a></li> <li><a href="/wiki/Serine_dehydratase" title="Serine dehydratase">Serine dehydratase</a></li></ul> <ul><li><a href="/wiki/Glycine" title="Glycine">glycine</a>→<a href="/wiki/Creatine" title="Creatine">creatine</a>: <a href="/wiki/Guanidinoacetate_N-methyltransferase" title="Guanidinoacetate N-methyltransferase">Guanidinoacetate N-methyltransferase</a></li> <li><a href="/wiki/Creatine_kinase" title="Creatine kinase">Creatine kinase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Alanine" title="Alanine">alanine</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Alanine_transaminase" title="Alanine transaminase">Alanine transaminase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Cysteine" title="Cysteine">cysteine</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/D-cysteine_desulfhydrase" title="D-cysteine desulfhydrase">D-cysteine desulfhydrase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Threonine" title="Threonine">threonine</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/L-threonine_dehydrogenase" class="mw-redirect" title="L-threonine dehydrogenase">L-threonine dehydrogenase</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">G→<a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a>→<br /><a href="/wiki/Alpha-Ketoglutaric_acid" class="mw-redirect" title="Alpha-Ketoglutaric acid">α-ketoglutarate</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Histidine" title="Histidine">HISTIDINE</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Histidine_ammonia-lyase" title="Histidine ammonia-lyase">Histidine ammonia-lyase</a></li> <li><a href="/wiki/Urocanase" title="Urocanase">Urocanate hydratase</a></li> <li><a href="/wiki/Formiminotransferase_cyclodeaminase" class="mw-redirect" title="Formiminotransferase cyclodeaminase">Formiminotransferase cyclodeaminase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Proline" title="Proline">proline</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Proline_oxidase" title="Proline oxidase">Proline oxidase</a></li> <li><a href="/wiki/Pyrroline-5-carboxylate_reductase" title="Pyrroline-5-carboxylate reductase">Pyrroline-5-carboxylate reductase</a></li> <li><a href="/wiki/1-Pyrroline-5-carboxylate_dehydrogenase" title="1-Pyrroline-5-carboxylate dehydrogenase">1-Pyrroline-5-carboxylate dehydrogenase</a>/<a href="/wiki/Aldehyde_dehydrogenase_4_family,_member_A1" title="Aldehyde dehydrogenase 4 family, member A1">ALDH4A1</a></li> <li><a href="/wiki/PYCR1" title="PYCR1">PYCR1</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Arginine" title="Arginine">arginine</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Ornithine_aminotransferase" title="Ornithine aminotransferase">Ornithine aminotransferase</a></li> <li><a href="/wiki/Ornithine_decarboxylase" title="Ornithine decarboxylase">Ornithine decarboxylase</a></li> <li><a href="/wiki/Agmatinase" title="Agmatinase">Agmatinase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">→<a href="/wiki/Alpha-ketoglutarate" class="mw-redirect" title="Alpha-ketoglutarate">alpha-ketoglutarate</a>→TCA</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Glutamate_dehydrogenase" title="Glutamate dehydrogenase">Glutamate dehydrogenase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Cysteine" title="Cysteine">cysteine</a>+<a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a>→<a href="/wiki/Glutathione" title="Glutathione">glutathione</a>: <a href="/wiki/Gamma-glutamylcysteine_synthetase" class="mw-redirect" title="Gamma-glutamylcysteine synthetase">Gamma-glutamylcysteine synthetase</a></li> <li><a href="/wiki/Glutathione_synthetase" title="Glutathione synthetase">Glutathione synthetase</a></li> <li><a href="/wiki/Gamma-glutamyl_transpeptidase" class="mw-redirect" title="Gamma-glutamyl transpeptidase">Gamma-glutamyl transpeptidase</a></li></ul> <ul><li><a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a>→<a href="/wiki/Glutamine" title="Glutamine">glutamine</a>: <a href="/wiki/Glutamine_synthetase" title="Glutamine synthetase">Glutamine synthetase</a></li> <li><a href="/wiki/Glutaminase" title="Glutaminase">Glutaminase</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">G→<a href="/wiki/Propionyl-CoA" title="Propionyl-CoA">propionyl-CoA</a>→<br /><a href="/wiki/Succinyl-CoA" title="Succinyl-CoA">succinyl-CoA</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Valine" title="Valine">VALINE</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Branched-chain_amino_acid_aminotransferase" title="Branched-chain amino acid aminotransferase">Branched-chain amino acid aminotransferase</a></li> <li><a href="/wiki/Branched-chain_alpha-keto_acid_dehydrogenase_complex" title="Branched-chain alpha-keto acid dehydrogenase complex">Branched-chain alpha-keto acid dehydrogenase complex</a></li> <li><a href="/wiki/Enoyl-CoA_hydratase" title="Enoyl-CoA hydratase">Enoyl-CoA hydratase</a></li> <li><a href="/wiki/3-hydroxyisobutyryl-CoA_hydrolase" title="3-hydroxyisobutyryl-CoA hydrolase">3-hydroxyisobutyryl-CoA hydrolase</a></li> <li><a href="/wiki/3-hydroxyisobutyrate_dehydrogenase" title="3-hydroxyisobutyrate dehydrogenase">3-hydroxyisobutyrate dehydrogenase</a></li> <li><a href="/wiki/Methylmalonate-semialdehyde_dehydrogenase_(acylating)" title="Methylmalonate-semialdehyde dehydrogenase (acylating)">Methylmalonate semialdehyde dehydrogenase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Isoleucine" title="Isoleucine">ISOLEUCINE</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Branched-chain_amino_acid_aminotransferase" title="Branched-chain amino acid aminotransferase">Branched-chain amino acid aminotransferase</a></li> <li><a href="/wiki/Branched-chain_alpha-keto_acid_dehydrogenase_complex" title="Branched-chain alpha-keto acid dehydrogenase complex">Branched-chain alpha-keto acid dehydrogenase complex</a></li> <li><a href="/wiki/3-hydroxy-2-methylbutyryl-CoA_dehydrogenase" title="3-hydroxy-2-methylbutyryl-CoA dehydrogenase">3-hydroxy-2-methylbutyryl-CoA dehydrogenase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Methionine" title="Methionine">METHIONINE</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><i><a href="/wiki/Methionine#Generation_of_homocysteine" title="Methionine">generation of homocysteine</a>:</i> <a href="/wiki/Methionine_adenosyltransferase" class="mw-redirect" title="Methionine adenosyltransferase">Methionine adenosyltransferase</a></li> <li><a href="/wiki/Adenosylhomocysteinase" title="Adenosylhomocysteinase">Adenosylhomocysteinase</a></li></ul> <ul><li><i><a href="/wiki/Methionine#Regeneration_of_methionine" title="Methionine">regeneration of methionine</a>:</i> <a href="/wiki/Methionine_synthase" title="Methionine synthase">Methionine synthase</a>/<a href="/wiki/Methionine_synthase" title="Methionine synthase">Homocysteine methyltransferase</a></li> <li><a href="/wiki/Betaine-homocysteine_S-methyltransferase" class="mw-redirect" title="Betaine-homocysteine S-methyltransferase">Betaine-homocysteine methyltransferase</a></li></ul> <ul><li><i><a href="/wiki/Methionine#Conversion_to_cysteine" title="Methionine">conversion to cysteine</a>:</i> <a href="/wiki/Cystathionine_beta_synthase" title="Cystathionine beta synthase">Cystathionine beta synthase</a></li> <li><a href="/wiki/Cystathionine_gamma-lyase" title="Cystathionine gamma-lyase">Cystathionine gamma-lyase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Threonine" title="Threonine">THREONINE</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Threonine_aldolase" title="Threonine aldolase">Threonine aldolase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">→<a href="/wiki/Succinyl-CoA" title="Succinyl-CoA">succinyl-CoA</a>→TCA</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Propionyl-CoA_carboxylase" title="Propionyl-CoA carboxylase">Propionyl-CoA carboxylase</a></li> <li><a href="/wiki/Methylmalonyl_CoA_epimerase" title="Methylmalonyl CoA epimerase">Methylmalonyl CoA epimerase</a></li> <li><a href="/wiki/Methylmalonyl-CoA_mutase" title="Methylmalonyl-CoA mutase">Methylmalonyl-CoA mutase</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">G→<a href="/wiki/Fumarate" class="mw-redirect" title="Fumarate">fumarate</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Phenylalanine" title="Phenylalanine">PHENYLALANINE</a>→<a href="/wiki/Tyrosine" title="Tyrosine">tyrosine</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Phenylalanine_hydroxylase" title="Phenylalanine hydroxylase">Phenylalanine hydroxylase</a></li> <li><a href="/wiki/Tyrosine_aminotransferase" title="Tyrosine aminotransferase">Tyrosine aminotransferase</a></li> <li><a href="/wiki/4-Hydroxyphenylpyruvate_dioxygenase" title="4-Hydroxyphenylpyruvate dioxygenase">4-Hydroxyphenylpyruvate dioxygenase</a></li> <li><a href="/wiki/Homogentisate_1,2-dioxygenase" title="Homogentisate 1,2-dioxygenase">Homogentisate 1,2-dioxygenase</a></li> <li><a href="/wiki/Fumarylacetoacetate_hydrolase" title="Fumarylacetoacetate hydrolase">Fumarylacetoacetate hydrolase</a></li></ul> <ul><li><a href="/wiki/Tyrosine" title="Tyrosine">tyrosine</a>→<a href="/wiki/Melanin" title="Melanin">melanin</a>: <a href="/wiki/Tyrosinase" title="Tyrosinase">Tyrosinase</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">G→<a href="/wiki/Oxaloacetic_acid" title="Oxaloacetic acid">oxaloacetate</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Asparagine" title="Asparagine">asparagine</a>→<a href="/wiki/Aspartate" class="mw-redirect" title="Aspartate">aspartate</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Asparaginase" title="Asparaginase">Asparaginase</a>/<a href="/wiki/Asparagine_synthetase" title="Asparagine synthetase">Asparagine synthetase</a></li> <li><a href="/wiki/Aspartate_transaminase" title="Aspartate transaminase">Aspartate transaminase</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235"><style data-mw-deduplicate="TemplateStyles:r1038841319">.mw-parser-output .tooltip-dotted{border-bottom:1px dotted;cursor:help}</style><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1038841319"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1038841319"></div><div role="navigation" class="navbox authority-control" aria-labelledby="Authority_control_databases_frameless&#124;text-top&#124;10px&#124;alt=Edit_this_at_Wikidata&#124;link=https&#58;//www.wikidata.org/wiki/Q8066#identifiers&#124;class=noprint&#124;Edit_this_at_Wikidata" style="padding:3px"><table class="nowraplinks hlist mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><div id="Authority_control_databases_frameless&#124;text-top&#124;10px&#124;alt=Edit_this_at_Wikidata&#124;link=https&#58;//www.wikidata.org/wiki/Q8066#identifiers&#124;class=noprint&#124;Edit_this_at_Wikidata" style="font-size:114%;margin:0 4em"><a href="/wiki/Help:Authority_control" title="Help:Authority control">Authority control databases</a> <span class="mw-valign-text-top noprint" typeof="mw:File/Frameless"><a href="https://www.wikidata.org/wiki/Q8066#identifiers" title="Edit this at Wikidata"><img alt="Edit this at Wikidata" 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States</a></span></li><li><span class="uid"><span class="rt-commentedText tooltip tooltip-dotted" title="Acides aminés"><a rel="nofollow" class="external text" href="https://catalogue.bnf.fr/ark:/12148/cb11944322s">France</a></span></span></li><li><span class="uid"><span class="rt-commentedText tooltip tooltip-dotted" title="Acides aminés"><a rel="nofollow" class="external text" href="https://data.bnf.fr/ark:/12148/cb11944322s">BnF data</a></span></span></li><li><span class="uid"><a rel="nofollow" class="external text" href="https://id.ndl.go.jp/auth/ndlna/00560236">Japan</a></span></li><li><span class="uid"><span class="rt-commentedText tooltip tooltip-dotted" title="aminokyseliny"><a rel="nofollow" class="external text" href="https://aleph.nkp.cz/F/?func=find-c&local_base=aut&ccl_term=ica=ph117172&CON_LNG=ENG">Czech Republic</a></span></span></li><li><span class="uid"><a rel="nofollow" class="external text" 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