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data-event-name="pinnable-header.vector-toc.pin">move to sidebar</button> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-unpin-button" data-event-name="pinnable-header.vector-toc.unpin">hide</button> </div> <ul class="vector-toc-contents" id="mw-panel-toc-list"> <li id="toc-mw-content-text" class="vector-toc-list-item vector-toc-level-1"> <a href="#" class="vector-toc-link"> <div class="vector-toc-text">(Top)</div> </a> </li> <li id="toc-Elements_of_biosynthesis" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Elements_of_biosynthesis"> <div class="vector-toc-text"> <span class="vector-toc-numb">1</span> <span>Elements of biosynthesis</span> </div> </a> <ul id="toc-Elements_of_biosynthesis-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Properties_of_chemical_reactions" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" 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class="vector-toc-numb">3.1</span> <span>Eukaryotic phospholipids</span> </div> </a> <ul id="toc-Eukaryotic_phospholipids-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Sphingolipids" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Sphingolipids"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.2</span> <span>Sphingolipids</span> </div> </a> <ul id="toc-Sphingolipids-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Cholesterol" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Cholesterol"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.3</span> <span>Cholesterol</span> </div> </a> <ul id="toc-Cholesterol-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Nucleotides" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Nucleotides"> <div class="vector-toc-text"> <span class="vector-toc-numb">4</span> <span>Nucleotides</span> </div> </a> <button aria-controls="toc-Nucleotides-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 Nucleotides subsection</span> </button> <ul id="toc-Nucleotides-sublist" class="vector-toc-list"> <li id="toc-Purine_nucleotides" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Purine_nucleotides"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.1</span> <span>Purine nucleotides</span> </div> </a> <ul id="toc-Purine_nucleotides-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Pyrimidine_nucleotides" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Pyrimidine_nucleotides"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.2</span> <span>Pyrimidine nucleotides</span> </div> </a> <ul id="toc-Pyrimidine_nucleotides-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-DNA" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#DNA"> <div class="vector-toc-text"> <span class="vector-toc-numb">5</span> <span>DNA</span> </div> </a> <ul id="toc-DNA-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Amino_acids" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Amino_acids"> <div class="vector-toc-text"> <span class="vector-toc-numb">6</span> <span>Amino acids</span> </div> </a> <button aria-controls="toc-Amino_acids-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 Amino acids subsection</span> </button> <ul id="toc-Amino_acids-sublist" class="vector-toc-list"> <li id="toc-Amino_acid_basic_structure" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Amino_acid_basic_structure"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.1</span> <span>Amino acid basic structure</span> </div> </a> <ul id="toc-Amino_acid_basic_structure-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Nitrogen_source" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Nitrogen_source"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.2</span> <span>Nitrogen source</span> </div> </a> <ul id="toc-Nitrogen_source-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-The_glutamate_family_of_amino_acids" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#The_glutamate_family_of_amino_acids"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.3</span> <span>The glutamate family of amino acids</span> </div> </a> <ul id="toc-The_glutamate_family_of_amino_acids-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-The_serine_family_of_amino_acids" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#The_serine_family_of_amino_acids"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.4</span> <span>The serine family of amino acids</span> </div> </a> <ul id="toc-The_serine_family_of_amino_acids-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-The_aspartate_family_of_amino_acids" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#The_aspartate_family_of_amino_acids"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.5</span> <span>The aspartate family of amino acids</span> </div> </a> <ul id="toc-The_aspartate_family_of_amino_acids-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Proteins" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Proteins"> <div class="vector-toc-text"> <span class="vector-toc-numb">7</span> <span>Proteins</span> </div> </a> <button aria-controls="toc-Proteins-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 Proteins subsection</span> </button> <ul id="toc-Proteins-sublist" class="vector-toc-list"> <li id="toc-Additional_background" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Additional_background"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.1</span> <span>Additional background</span> </div> </a> <ul id="toc-Additional_background-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Translation_in_steps" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Translation_in_steps"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.2</span> <span>Translation in steps</span> </div> </a> <ul id="toc-Translation_in_steps-sublist" class="vector-toc-list"> <li id="toc-Step_1:_Initiation" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Step_1:_Initiation"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.2.1</span> <span>Step 1: Initiation</span> </div> </a> <ul id="toc-Step_1:_Initiation-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Step_2:_Elongation" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Step_2:_Elongation"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.2.2</span> <span>Step 2: Elongation</span> </div> </a> <ul id="toc-Step_2:_Elongation-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Step_3:_Termination" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Step_3:_Termination"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.2.3</span> <span>Step 3: Termination</span> </div> </a> <ul id="toc-Step_3:_Termination-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> </ul> </li> <li id="toc-Diseases_associated_with_macromolecule_deficiency" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Diseases_associated_with_macromolecule_deficiency"> <div class="vector-toc-text"> <span class="vector-toc-numb">8</span> <span>Diseases associated with macromolecule deficiency</span> </div> </a> <ul id="toc-Diseases_associated_with_macromolecule_deficiency-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-See_also" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#See_also"> <div class="vector-toc-text"> <span class="vector-toc-numb">9</span> <span>See also</span> </div> </a> <ul id="toc-See_also-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-References" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> <span class="vector-toc-numb">10</span> <span>References</span> </div> </a> <ul id="toc-References-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">Biosynthesis</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 44 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-44" 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">44 languages</span> </label> <div class="vector-dropdown-content"> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="interlanguage-link interwiki-ar mw-list-item"><a href="https://ar.wikipedia.org/wiki/%D8%A7%D8%B5%D8%B7%D9%86%D8%A7%D8%B9_%D8%AD%D9%8A%D9%88%D9%8A" title="اصطناع حيوي – Arabic" lang="ar" hreflang="ar" data-title="اصطناع حيوي" data-language-autonym="العربية" data-language-local-name="Arabic" class="interlanguage-link-target"><span>العربية</span></a></li><li class="interlanguage-link interwiki-az mw-list-item"><a href="https://az.wikipedia.org/wiki/Biosintez" title="Biosintez – Azerbaijani" lang="az" hreflang="az" data-title="Biosintez" data-language-autonym="Azərbaycanca" data-language-local-name="Azerbaijani" class="interlanguage-link-target"><span>Azərbaycanca</span></a></li><li class="interlanguage-link interwiki-be mw-list-item"><a href="https://be.wikipedia.org/wiki/%D0%91%D1%96%D1%8F%D1%81%D1%96%D0%BD%D1%82%D1%8D%D0%B7" title="Біясінтэз – Belarusian" lang="be" hreflang="be" data-title="Біясінтэз" data-language-autonym="Беларуская" data-language-local-name="Belarusian" class="interlanguage-link-target"><span>Беларуская</span></a></li><li class="interlanguage-link interwiki-bg mw-list-item"><a href="https://bg.wikipedia.org/wiki/%D0%91%D0%B8%D0%BE%D1%81%D0%B8%D0%BD%D1%82%D0%B5%D0%B7" title="Биосинтез – Bulgarian" lang="bg" hreflang="bg" data-title="Биосинтез" 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/Biosinteza" title="Biosinteza – Bosnian" lang="bs" hreflang="bs" data-title="Biosinteza" 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/Bios%C3%ADntesi" title="Biosíntesi – Catalan" lang="ca" hreflang="ca" data-title="Biosíntesi" data-language-autonym="Català" data-language-local-name="Catalan" class="interlanguage-link-target"><span>Català</span></a></li><li class="interlanguage-link interwiki-cs mw-list-item"><a href="https://cs.wikipedia.org/wiki/Biosynt%C3%A9za" title="Biosyntéza – Czech" lang="cs" hreflang="cs" data-title="Biosyntéza" data-language-autonym="Čeština" data-language-local-name="Czech" class="interlanguage-link-target"><span>Čeština</span></a></li><li class="interlanguage-link interwiki-da mw-list-item"><a href="https://da.wikipedia.org/wiki/Biosyntese" title="Biosyntese – Danish" lang="da" hreflang="da" data-title="Biosyntese" data-language-autonym="Dansk" data-language-local-name="Danish" class="interlanguage-link-target"><span>Dansk</span></a></li><li class="interlanguage-link interwiki-de mw-list-item"><a href="https://de.wikipedia.org/wiki/Biosynthese" title="Biosynthese – German" lang="de" hreflang="de" data-title="Biosynthese" 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/Bios%C3%BCntees" title="Biosüntees – Estonian" lang="et" hreflang="et" data-title="Biosüntees" 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%92%CE%B9%CE%BF%CF%83%CF%8D%CE%BD%CE%B8%CE%B5%CF%83%CE%B7" title="Βιοσύνθεση – Greek" lang="el" hreflang="el" data-title="Βιοσύνθεση" 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/Bios%C3%ADntesis" title="Biosíntesis – Spanish" lang="es" hreflang="es" data-title="Biosíntesis" 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/Biosintezo" title="Biosintezo – Esperanto" lang="eo" hreflang="eo" data-title="Biosintezo" 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/Biosintesi" title="Biosintesi – Basque" lang="eu" hreflang="eu" data-title="Biosintesi" 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%A8%DB%8C%D9%88%D8%B3%D9%86%D8%AA%D8%B2" title="بیوسنتز – Persian" lang="fa" hreflang="fa" data-title="بیوسنتز" data-language-autonym="فارسی" data-language-local-name="Persian" class="interlanguage-link-target"><span>فارسی</span></a></li><li class="interlanguage-link interwiki-fr mw-list-item"><a href="https://fr.wikipedia.org/wiki/Biosynth%C3%A8se" title="Biosynthèse – French" lang="fr" hreflang="fr" data-title="Biosynthèse" data-language-autonym="Français" data-language-local-name="French" class="interlanguage-link-target"><span>Français</span></a></li><li class="interlanguage-link interwiki-ko mw-list-item"><a href="https://ko.wikipedia.org/wiki/%EC%83%9D%ED%95%A9%EC%84%B1" title="생합성 – Korean" lang="ko" hreflang="ko" data-title="생합성" data-language-autonym="한국어" data-language-local-name="Korean" class="interlanguage-link-target"><span>한국어</span></a></li><li class="interlanguage-link interwiki-hi mw-list-item"><a href="https://hi.wikipedia.org/wiki/%E0%A4%9C%E0%A5%88%E0%A4%B5%E0%A4%B8%E0%A4%82%E0%A4%B6%E0%A5%8D%E0%A4%B2%E0%A5%87%E0%A4%B7%E0%A4%A3" title="जैवसंश्लेषण – Hindi" lang="hi" hreflang="hi" data-title="जैवसंश्लेषण" data-language-autonym="हिन्दी" data-language-local-name="Hindi" class="interlanguage-link-target"><span>हिन्दी</span></a></li><li class="interlanguage-link interwiki-id mw-list-item"><a href="https://id.wikipedia.org/wiki/Biosintesis" title="Biosintesis – Indonesian" lang="id" hreflang="id" data-title="Biosintesis" 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-it mw-list-item"><a href="https://it.wikipedia.org/wiki/Biosintesi" title="Biosintesi – Italian" lang="it" hreflang="it" data-title="Biosintesi" data-language-autonym="Italiano" data-language-local-name="Italian" class="interlanguage-link-target"><span>Italiano</span></a></li><li class="interlanguage-link interwiki-ka mw-list-item"><a href="https://ka.wikipedia.org/wiki/%E1%83%91%E1%83%98%E1%83%9D%E1%83%A1%E1%83%98%E1%83%9C%E1%83%97%E1%83%94%E1%83%96%E1%83%98" title="ბიოსინთეზი – Georgian" lang="ka" hreflang="ka" data-title="ბიოსინთეზი" data-language-autonym="ქართული" data-language-local-name="Georgian" class="interlanguage-link-target"><span>ქართული</span></a></li><li class="interlanguage-link interwiki-kk mw-list-item"><a href="https://kk.wikipedia.org/wiki/%D0%91%D0%B8%D0%BE%D1%81%D0%B8%D0%BD%D1%82%D0%B5%D0%B7" title="Биосинтез – Kazakh" lang="kk" hreflang="kk" data-title="Биосинтез" data-language-autonym="Қазақша" data-language-local-name="Kazakh" class="interlanguage-link-target"><span>Қазақша</span></a></li><li class="interlanguage-link interwiki-ky mw-list-item"><a href="https://ky.wikipedia.org/wiki/%D0%91%D0%B8%D0%BE%D1%81%D0%B8%D0%BD%D1%82%D0%B5%D0%B7" title="Биосинтез – Kyrgyz" lang="ky" hreflang="ky" data-title="Биосинтез" data-language-autonym="Кыргызча" data-language-local-name="Kyrgyz" class="interlanguage-link-target"><span>Кыргызча</span></a></li><li class="interlanguage-link interwiki-ms mw-list-item"><a href="https://ms.wikipedia.org/wiki/Biosintesis" title="Biosintesis – Malay" lang="ms" hreflang="ms" data-title="Biosintesis" 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-nl mw-list-item"><a href="https://nl.wikipedia.org/wiki/Biosynthese" title="Biosynthese – Dutch" lang="nl" hreflang="nl" data-title="Biosynthese" 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/%E7%94%9F%E5%90%88%E6%88%90" title="生合成 – Japanese" lang="ja" hreflang="ja" data-title="生合成" 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-no mw-list-item"><a href="https://no.wikipedia.org/wiki/Biosyntese" title="Biosyntese – Norwegian Bokmål" lang="nb" hreflang="nb" data-title="Biosyntese" 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-uz mw-list-item"><a href="https://uz.wikipedia.org/wiki/Biosintez" title="Biosintez – Uzbek" lang="uz" hreflang="uz" data-title="Biosintez" 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-ps mw-list-item"><a href="https://ps.wikipedia.org/wiki/%D8%A8%D8%A7%D9%8A%D9%88%D8%B3%D9%8A%D9%86%D8%AA%D9%8A%D8%B3%D8%B2_(%D8%AF_%DA%98%D9%88%D9%86%D8%AF%D9%8A%D9%88_%DA%98%D9%88%D9%8A%D9%88_%D8%AA%D8%B1%DA%A9%D9%8A%D8%A8/%D8%AF_%D8%A8%D8%B1%D8%AE%D9%88_%D9%8A%D9%88_%DA%81%D8%A7%DB%8C_%DA%A9%DB%90%D8%AF%D9%84)" title="بايوسينتيسز (د ژونديو ژويو ترکيب/د برخو يو ځای کېدل) – Pashto" lang="ps" hreflang="ps" data-title="بايوسينتيسز (د ژونديو ژويو ترکيب/د برخو يو ځای کېدل)" data-language-autonym="پښتو" data-language-local-name="Pashto" class="interlanguage-link-target"><span>پښتو</span></a></li><li class="interlanguage-link interwiki-pl mw-list-item"><a href="https://pl.wikipedia.org/wiki/Biosynteza" title="Biosynteza – Polish" lang="pl" hreflang="pl" data-title="Biosynteza" 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/Bioss%C3%ADntese" title="Biossíntese – Portuguese" lang="pt" hreflang="pt" data-title="Biossíntese" data-language-autonym="Português" data-language-local-name="Portuguese" class="interlanguage-link-target"><span>Português</span></a></li><li class="interlanguage-link interwiki-ro mw-list-item"><a href="https://ro.wikipedia.org/wiki/Biosintez%C4%83" title="Biosinteză – Romanian" lang="ro" hreflang="ro" data-title="Biosinteză" 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%91%D0%B8%D0%BE%D1%81%D0%B8%D0%BD%D1%82%D0%B5%D0%B7" title="Биосинтез – Russian" lang="ru" hreflang="ru" data-title="Биосинтез" data-language-autonym="Русский" data-language-local-name="Russian" class="interlanguage-link-target"><span>Русский</span></a></li><li class="interlanguage-link interwiki-simple mw-list-item"><a href="https://simple.wikipedia.org/wiki/Biosynthesis" title="Biosynthesis – Simple English" lang="en-simple" hreflang="en-simple" data-title="Biosynthesis" 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-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/Biosinteza" title="Biosinteza – Serbian" lang="sr" hreflang="sr" data-title="Biosinteza" 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/Biosinteza" title="Biosinteza – Serbo-Croatian" lang="sh" hreflang="sh" data-title="Biosinteza" 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-fi mw-list-item"><a href="https://fi.wikipedia.org/wiki/Biosynteesi" title="Biosynteesi – Finnish" lang="fi" hreflang="fi" data-title="Biosynteesi" 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/Biosyntes" title="Biosyntes – Swedish" lang="sv" hreflang="sv" data-title="Biosyntes" 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/Biosintesis" title="Biosintesis – Tagalog" lang="tl" hreflang="tl" data-title="Biosintesis" data-language-autonym="Tagalog" data-language-local-name="Tagalog" class="interlanguage-link-target"><span>Tagalog</span></a></li><li class="interlanguage-link interwiki-th mw-list-item"><a href="https://th.wikipedia.org/wiki/%E0%B8%8A%E0%B8%B5%E0%B8%A7%E0%B8%AA%E0%B8%B1%E0%B8%87%E0%B9%80%E0%B8%84%E0%B8%A3%E0%B8%B2%E0%B8%B0%E0%B8%AB%E0%B9%8C" title="ชีวสังเคราะห์ – Thai" lang="th" hreflang="th" data-title="ชีวสังเคราะห์" 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%91%D0%B8%D0%BE%D1%81%D0%B8%D0%BD%D1%82%D0%B5%D0%B7" title="Биосинтез – Tajik" lang="tg" hreflang="tg" 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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">Process where substrates are converted into more complex products in living organisms</div> <style data-mw-deduplicate="TemplateStyles:r1251242444">.mw-parser-output .ambox{border:1px solid #a2a9b1;border-left:10px solid #36c;background-color:#fbfbfb;box-sizing:border-box}.mw-parser-output .ambox+link+.ambox,.mw-parser-output .ambox+link+style+.ambox,.mw-parser-output .ambox+link+link+.ambox,.mw-parser-output .ambox+.mw-empty-elt+link+.ambox,.mw-parser-output .ambox+.mw-empty-elt+link+style+.ambox,.mw-parser-output .ambox+.mw-empty-elt+link+link+.ambox{margin-top:-1px}html body.mediawiki .mw-parser-output .ambox.mbox-small-left{margin:4px 1em 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.compact-ambox .hide-when-compact{display:none}</style><table class="box-Multiple_issues plainlinks metadata ambox ambox-content ambox-multiple_issues compact-ambox" role="presentation"><tbody><tr><td class="mbox-image"><div class="mbox-image-div"><span typeof="mw:File"><span><img alt="" src="//upload.wikimedia.org/wikipedia/en/thumb/b/b4/Ambox_important.svg/40px-Ambox_important.svg.png" decoding="async" width="40" height="40" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/b/b4/Ambox_important.svg/60px-Ambox_important.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/b/b4/Ambox_important.svg/80px-Ambox_important.svg.png 2x" data-file-width="40" data-file-height="40" /></span></span></div></td><td class="mbox-text"><div class="mbox-text-span"><div class="multiple-issues-text mw-collapsible"><b>This article has multiple issues.</b> Please help <b><a href="/wiki/Special:EditPage/Biosynthesis" title="Special:EditPage/Biosynthesis">improve it</a></b> or discuss these issues on the <b><a href="/wiki/Talk:Biosynthesis" title="Talk:Biosynthesis">talk page</a></b>. <small><i>(<a href="/wiki/Help:Maintenance_template_removal" title="Help:Maintenance template removal">Learn how and when to remove these messages</a>)</i></small> <div class="mw-collapsible-content"> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1251242444"><table class="box-Expert_needed plainlinks metadata ambox ambox-content" role="presentation"><tbody><tr><td class="mbox-image"><div class="mbox-image-div"><span typeof="mw:File"><span><img alt="" src="//upload.wikimedia.org/wikipedia/en/thumb/b/b4/Ambox_important.svg/40px-Ambox_important.svg.png" decoding="async" width="40" height="40" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/b/b4/Ambox_important.svg/60px-Ambox_important.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/b/b4/Ambox_important.svg/80px-Ambox_important.svg.png 2x" data-file-width="40" data-file-height="40" /></span></span></div></td><td class="mbox-text"><div class="mbox-text-span">This article <b>needs attention from an expert in biochemistry</b>. The specific problem is: <b>someone with a solid grasp of the full scope of this subject and of its secondary and advanced teaching literatures needs to address A, the clear structural issues of the article (e.g., general absence of catabolic biosynthetic pathways, insertion of macromolecule anabolic paths before all building blocks covered, etc.); B, discrepancies in scope vs. other major articles, cf. <a href="/wiki/Nucleic_acid_metabolism" title="Nucleic acid metabolism">Nucleic acid metabolism</a>; C, remaining gross factual errors (only those in the lead having yet been superficially addressed); etc..</b><span class="hide-when-compact"> <a href="/wiki/Wikipedia:WikiProject_Biochemistry" class="mw-redirect" title="Wikipedia:WikiProject Biochemistry">WikiProject Biochemistry</a> may be able to help recruit an expert.</span> <span class="date-container"><i>(<span class="date">July 2024</span>)</i></span></div></td></tr></tbody></table> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1251242444"><table class="box-Lead_rewrite plainlinks metadata ambox ambox-style ambox-lead_rewrite" role="presentation"><tbody><tr><td class="mbox-image"><div class="mbox-image-div"><span typeof="mw:File"><span><img alt="" src="//upload.wikimedia.org/wikipedia/en/thumb/f/f2/Edit-clear.svg/40px-Edit-clear.svg.png" decoding="async" width="40" height="40" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/f/f2/Edit-clear.svg/60px-Edit-clear.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/f/f2/Edit-clear.svg/80px-Edit-clear.svg.png 2x" data-file-width="48" data-file-height="48" /></span></span></div></td><td class="mbox-text"><div class="mbox-text-span">The article's <a href="/wiki/Wikipedia:Manual_of_Style/Lead_section" title="Wikipedia:Manual of Style/Lead section">lead section</a> <b>may need to be rewritten</b>. The reason given is: <b>to ensure, per WP:INTRO, that the lead properly summarises the article, and introduces no material that does not already appear validly and verifiably sourced to secondary sources within the article.</b><span class="hide-when-compact"> Please help <a class="external text" href="https://en.wikipedia.org/w/index.php?title=Biosynthesis&action=edit">improve the lead</a> and read the <a href="/wiki/Wikipedia:Manual_of_Style/Lead_section" title="Wikipedia:Manual of Style/Lead section">lead layout guide</a>.</span> <span class="date-container"><i>(<span class="date">July 2024</span>)</i></span><span class="hide-when-compact"><i> (<small><a href="/wiki/Help:Maintenance_template_removal" title="Help:Maintenance template removal">Learn how and when to remove this message</a></small>)</i></span></div></td></tr></tbody></table> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1251242444"><table class="box-Cite_check plainlinks metadata ambox ambox-content" role="presentation"><tbody><tr><td class="mbox-image"><div class="mbox-image-div"><span typeof="mw:File"><span><img src="//upload.wikimedia.org/wikipedia/commons/thumb/a/a4/Text_document_with_red_question_mark.svg/40px-Text_document_with_red_question_mark.svg.png" decoding="async" width="40" height="40" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/a/a4/Text_document_with_red_question_mark.svg/60px-Text_document_with_red_question_mark.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/a/a4/Text_document_with_red_question_mark.svg/80px-Text_document_with_red_question_mark.svg.png 2x" data-file-width="48" data-file-height="48" /></span></span></div></td><td class="mbox-text"><div class="mbox-text-span">This article <b>may contain <a href="/wiki/Wikipedia:CITE" class="mw-redirect" title="Wikipedia:CITE">citations</a> that do not <a href="/wiki/Wikipedia:V" class="mw-redirect" title="Wikipedia:V">verify</a> the text</b>.<span class="hide-when-compact"> Please <a class="external text" href="https://en.wikipedia.org/w/index.php?title=Biosynthesis&action=edit">check for citation inaccuracies</a>.</span> <span class="date-container"><i>(<span class="date">July 2024</span>)</i></span><span class="hide-when-compact"><i> (<small><a href="/wiki/Help:Maintenance_template_removal" title="Help:Maintenance template removal">Learn how and when to remove this message</a></small>)</i></span></div></td></tr></tbody></table> </div> </div><span class="hide-when-compact"><i> (<small><a href="/wiki/Help:Maintenance_template_removal" title="Help:Maintenance template removal">Learn how and when to remove this message</a></small>)</i></span></div></td></tr></tbody></table> <p><b>Biosynthesis</b>, i.e., <a href="/wiki/Chemical_synthesis" title="Chemical synthesis">chemical synthesis</a> occurring in biological contexts, is a term most often referring to multi-step, <a href="/wiki/Enzyme" title="Enzyme">enzyme</a>-<a href="/wiki/Catalysis" title="Catalysis">catalyzed</a> processes where chemical substances absorbed as nutrients (or previously converted through biosynthesis) serve as enzyme <a href="/wiki/Substrate_(chemistry)" title="Substrate (chemistry)">substrates</a>, with conversion by the living organism either into simpler or more complex <a href="/wiki/Product_(chemistry)" title="Product (chemistry)">products</a>. Examples of biosynthetic pathways include those for the production of <a href="/wiki/Amino_acids" class="mw-redirect" title="Amino acids">amino acids</a>, <a href="/wiki/Lipid_membrane" class="mw-redirect" title="Lipid membrane">lipid membrane</a> components, and <a href="/wiki/Nucleotide" title="Nucleotide">nucleotides</a>, but also for the production of all classes of biological <a href="/wiki/Macromolecules" class="mw-redirect" title="Macromolecules">macromolecules</a>, and of <a href="/wiki/Acetyl-coenzyme_A" class="mw-redirect" title="Acetyl-coenzyme A">acetyl-coenzyme A</a>, <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">adenosine triphosphate</a>, <a href="/wiki/Nicotinamide_adenine_dinucleotide" title="Nicotinamide adenine dinucleotide">nicotinamide adenine dinucleotide</a> and other key intermediate and transactional molecules needed for <a href="/wiki/Metabolism" title="Metabolism">metabolism</a>. Thus, in biosynthesis, any of an array of <a href="/wiki/Chemical_compound" title="Chemical compound">compounds</a>, from simple to complex, are converted into other compounds, and so it includes both the <a href="/wiki/Catabolism" title="Catabolism">catabolism</a> and <a href="/wiki/Anabolism" title="Anabolism">anabolism</a> (building up and breaking down) of complex molecules (including <a href="/wiki/Macromolecules" class="mw-redirect" title="Macromolecules">macromolecules</a>). Biosynthetic processes are often represented via charts of <a href="/wiki/Metabolic_pathway" title="Metabolic pathway">metabolic pathways</a>. A particular biosynthetic pathway may be located within a single cellular <a href="/wiki/Organelle" title="Organelle">organelle</a> (e.g., mitochondrial fatty acid synthesis pathways), while others involve enzymes that are located across an array of cellular organelles and structures (e.g., the biosynthesis of glycosylated cell surface proteins). </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="Elements_of_biosynthesis">Elements of biosynthesis</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=1" title="Edit section: Elements of biosynthesis"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1251242444"><table class="box-Unreferenced_section plainlinks metadata ambox ambox-content ambox-Unreferenced" role="presentation"><tbody><tr><td class="mbox-image"><div class="mbox-image-div"><span typeof="mw:File"><a href="/wiki/File:Question_book-new.svg" class="mw-file-description"><img alt="" src="//upload.wikimedia.org/wikipedia/en/thumb/9/99/Question_book-new.svg/50px-Question_book-new.svg.png" decoding="async" width="50" height="39" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/9/99/Question_book-new.svg/75px-Question_book-new.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/9/99/Question_book-new.svg/100px-Question_book-new.svg.png 2x" data-file-width="512" data-file-height="399" /></a></span></div></td><td class="mbox-text"><div class="mbox-text-span">This section <b>does not <a href="/wiki/Wikipedia:Citing_sources" title="Wikipedia:Citing sources">cite</a> any <a href="/wiki/Wikipedia:Verifiability" title="Wikipedia:Verifiability">sources</a></b>.<span class="hide-when-compact"> Please help <a href="/wiki/Special:EditPage/Biosynthesis" title="Special:EditPage/Biosynthesis">improve this section</a> by <a href="/wiki/Help:Referencing_for_beginners" title="Help:Referencing for beginners">adding citations to reliable sources</a>. Unsourced material may be challenged and <a href="/wiki/Wikipedia:Verifiability#Burden_of_evidence" title="Wikipedia:Verifiability">removed</a>.</span> <span class="date-container"><i>(<span class="date">July 2024</span>)</i></span><span class="hide-when-compact"><i> (<small><a href="/wiki/Help:Maintenance_template_removal" title="Help:Maintenance template removal">Learn how and when to remove this message</a></small>)</i></span></div></td></tr></tbody></table> <p>Elements of biosynthesis include: <a href="/wiki/Precursor_(chemistry)" title="Precursor (chemistry)">precursor</a> compounds, <a href="/wiki/Chemical_energy" title="Chemical energy">chemical energy</a> (e.g. <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a>), and catalytic enzymes which may need <a href="/wiki/Coenzymes" class="mw-redirect" title="Coenzymes">coenzymes</a> (e.g. <a href="/wiki/NADH" class="mw-redirect" title="NADH">NADH</a>, <a href="/wiki/NADPH" class="mw-redirect" title="NADPH">NADPH</a>). These elements create <a href="/wiki/Monomers" class="mw-redirect" title="Monomers">monomers</a>, the building blocks for macromolecules. Some important biological macromolecules include: <a href="/wiki/Proteins" class="mw-redirect" title="Proteins">proteins</a>, which are composed of <a href="/wiki/Amino_acid" title="Amino acid">amino acid</a> monomers joined via <a href="/wiki/Peptide_bonds" class="mw-redirect" title="Peptide bonds">peptide bonds</a>, and <a href="/wiki/DNA" title="DNA">DNA</a> molecules, which are composed of nucleotides joined via <a href="/wiki/Phosphodiester_bonds" class="mw-redirect" title="Phosphodiester bonds">phosphodiester bonds</a>. </p> <div class="mw-heading mw-heading2"><h2 id="Properties_of_chemical_reactions">Properties of chemical reactions</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=2" title="Edit section: Properties of chemical reactions"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Biosynthesis occurs due to a series of chemical reactions. For these reactions to take place, the following elements are necessary:<sup id="cite_ref-isbn0-8153-3218-1_1-0" class="reference"><a href="#cite_note-isbn0-8153-3218-1-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> </p> <ul><li><a href="/wiki/Precursor_(chemistry)" title="Precursor (chemistry)">Precursor compounds</a>: these compounds are the starting molecules or <a href="/wiki/Substrate_(biochemistry)" class="mw-redirect" title="Substrate (biochemistry)">substrates</a> in a reaction. These may also be viewed as the <a href="/wiki/Reactants" class="mw-redirect" title="Reactants">reactants</a> in a given chemical process.</li> <li><a href="/wiki/Chemical_energy" title="Chemical energy">Chemical energy</a>: chemical energy can be found in the form of high energy molecules. These molecules are required for energetically unfavourable reactions. Furthermore, the <a href="/wiki/Hydrolysis" title="Hydrolysis">hydrolysis</a> of these compounds drives a reaction forward. High energy molecules, such as <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a>, have three <a href="/wiki/Phosphates" class="mw-redirect" title="Phosphates">phosphates</a>. Often, the terminal phosphate is split off during hydrolysis and transferred to another molecule.</li> <li><a href="/wiki/Catalysis" title="Catalysis">Catalysts</a>: these may be for example <a href="/wiki/Metal_ions" class="mw-redirect" title="Metal ions">metal ions</a> or <a href="/wiki/Coenzymes" class="mw-redirect" title="Coenzymes">coenzymes</a> and they catalyze a reaction by increasing the <a href="/wiki/Reaction_rate" title="Reaction rate">rate of the reaction</a> and lowering the <a href="/wiki/Activation_energy" title="Activation energy">activation energy</a>.</li></ul> <p>In the simplest sense, the reactions that occur in biosynthesis have the following format:<sup id="cite_ref-Zumdahl_2-0" class="reference"><a href="#cite_note-Zumdahl-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> </p> <dl><dd><dl><dd><span class="mwe-math-element"><span class="mwe-math-mathml-inline mwe-math-mathml-a11y" style="display: none;"><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle {\ce {Reactant ->[][enzyme] Product}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mtext>Reactant</mtext> <mrow class="MJX-TeXAtom-REL"> <munderover> <mo>→</mo> <mpadded width="+0.611em" lspace="0.278em" voffset="-.24em"> <mi>e</mi> <mi>n</mi> <mi>z</mi> <mi>y</mi> <mi>m</mi> <mi>e</mi> </mpadded> <mpadded width="+0.611em" lspace="0.278em" voffset=".15em" /> </munderover> </mrow> <mtext>Product</mtext> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle {\ce {Reactant ->[][enzyme] Product}}}</annotation> </semantics> </math></span><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/d97fbef58f64fb0b7d05d90fa0a73b05f5919fc8" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -1.992ex; margin-top: -0.452ex; margin-bottom: -0.513ex; width:25.543ex; height:4.843ex;" alt="{\displaystyle {\ce {Reactant ->[][enzyme] Product}}}"></span></dd></dl></dd></dl> <p>Some variations of this basic equation which will be discussed later in more detail are:<sup id="cite_ref-Voet_3-0" class="reference"><a href="#cite_note-Voet-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> </p> <ol><li>Simple compounds which are converted into other compounds, usually as part of a multiple step reaction pathway. Two examples of this type of reaction occur during the formation of <a href="/wiki/Nucleic_acid" title="Nucleic acid">nucleic acids</a> and the <a href="/wiki/Aminoacyl_tRNA_synthetase" title="Aminoacyl tRNA synthetase">charging</a> of <a href="/wiki/TRNA" class="mw-redirect" title="TRNA">tRNA</a> prior to <a href="/wiki/Translation_(biology)" title="Translation (biology)">translation</a>. For some of these steps, chemical energy is required: <dl><dd><dl><dd><span class="mwe-math-element"><span class="mwe-math-mathml-inline mwe-math-mathml-a11y" style="display: none;"><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle {\ce {{Precursor~molecule}+ATP<=>{product~AMP}+PP_{i}}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mtext>Precursor</mtext> <mtext> </mtext> <mtext>molecule</mtext> </mrow> <mo>+</mo> <mtext>ATP</mtext> <mrow class="MJX-TeXAtom-REL"> <mover> <mrow class="MJX-TeXAtom-OP MJX-fixedlimits"> <mrow class="MJX-TeXAtom-ORD"> <mpadded height="0" depth="0"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">↽</mo> </mrow> <mspace width="negativethinmathspace" /> <mspace width="negativethinmathspace" /> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> </mpadded> </mrow> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> <mspace width="negativethinmathspace" /> <mspace width="negativethinmathspace" /> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">⇀</mo> </mrow> </mrow> </mstyle> </mrow> </mover> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mtext>product</mtext> <mtext> </mtext> <mtext>AMP</mtext> </mrow> <mo>+</mo> <msubsup> <mtext>PP</mtext> <mrow class="MJX-TeXAtom-ORD"> <mtext>i</mtext> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mspace width="0pt" height="0pt" depth=".2em" /> </mrow> </msubsup> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle {\ce {{Precursor~molecule}+ATP<=>{product~AMP}+PP_{i}}}}</annotation> </semantics> </math></span><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/ffba88c19542c42b99277427e886017d841fae02" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -1.005ex; width:52.23ex; height:3.343ex;" alt="{\displaystyle {\ce {{Precursor~molecule}+ATP<=>{product~AMP}+PP_{i}}}}"></span></dd></dl></dd></dl></li> <li>Simple compounds that are converted into other compounds with the assistance of cofactors. For example, the synthesis of <a href="/wiki/Phospholipid" title="Phospholipid">phospholipids</a> requires acetyl CoA, while the synthesis of another membrane component, <a href="/wiki/Sphingolipid" title="Sphingolipid">sphingolipids</a>, requires NADH and FADH for the formation the <a href="/wiki/Sphingosine" title="Sphingosine">sphingosine</a> backbone. The general equation for these examples is: <dl><dd><dl><dd><span class="mwe-math-element"><span class="mwe-math-mathml-inline mwe-math-mathml-a11y" style="display: none;"><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle {\ce {{Precursor~molecule}+Cofactor->[][enzyme]macromolecule}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mtext>Precursor</mtext> <mtext> </mtext> <mtext>molecule</mtext> </mrow> <mo>+</mo> <mtext>Cofactor</mtext> <mrow class="MJX-TeXAtom-REL"> <munderover> <mo>→</mo> <mpadded width="+0.611em" lspace="0.278em" voffset="-.24em"> <mi>e</mi> <mi>n</mi> <mi>z</mi> <mi>y</mi> <mi>m</mi> <mi>e</mi> </mpadded> <mpadded width="+0.611em" lspace="0.278em" voffset=".15em" /> </munderover> </mrow> <mtext>macromolecule</mtext> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle {\ce {{Precursor~molecule}+Cofactor->[][enzyme]macromolecule}}}</annotation> </semantics> </math></span><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/b192f25eec9ceebed179bfeb43ae27795f3a91be" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -1.992ex; margin-top: -0.452ex; margin-bottom: -0.513ex; width:53.831ex; height:4.843ex;" alt="{\displaystyle {\ce {{Precursor~molecule}+Cofactor->[][enzyme]macromolecule}}}"></span></dd></dl></dd></dl></li> <li>Simple compounds that join to create a macromolecule. For example, <a href="/wiki/Fatty_acid" title="Fatty acid">fatty acids</a> join to form phospholipids. In turn, phospholipids and <a href="/wiki/Cholesterol" title="Cholesterol">cholesterol</a> interact <a href="/wiki/Noncovalent_bonding" class="mw-redirect" title="Noncovalent bonding">noncovalently</a> in order to form the <a href="/wiki/Lipid_bilayer" title="Lipid bilayer">lipid bilayer</a>. This reaction may be depicted as follows: <dl><dd><dl><dd><span class="mwe-math-element"><span class="mwe-math-mathml-inline mwe-math-mathml-a11y" style="display: none;"><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle {\ce {{Molecule~1}+Molecule~2->macromolecule}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mtext>Molecule</mtext> <mtext> </mtext> <mn>1</mn> <mspace width="thinmathspace" /> </mrow> <mo>+</mo> <mtext>Molecule</mtext> <mtext> </mtext> <mn>2</mn> <mspace width="thinmathspace" /> <mo stretchy="false">⟶</mo> <mtext>macromolecule</mtext> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle {\ce {{Molecule~1}+Molecule~2->macromolecule}}}</annotation> </semantics> </math></span><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/011820012574473a4bfff3bffd1cd87a6e83b0f1" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -0.505ex; width:45.137ex; height:2.343ex;" alt="{\displaystyle {\ce {{Molecule~1}+Molecule~2->macromolecule}}}"></span></dd></dl></dd></dl></li></ol> <div class="mw-heading mw-heading2"><h2 id="Lipid">Lipid</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=3" title="Edit section: Lipid"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-halign-left" typeof="mw:File/Thumb"><a href="/wiki/File:The_lipid_and_lipid_bilayer.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/7/79/The_lipid_and_lipid_bilayer.png/220px-The_lipid_and_lipid_bilayer.png" decoding="async" width="220" height="260" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/7/79/The_lipid_and_lipid_bilayer.png 1.5x" data-file-width="300" data-file-height="354" /></a><figcaption>Lipid membrane bilayer</figcaption></figure> <p>Many intricate macromolecules are synthesized in a pattern of simple, repeated structures.<sup id="cite_ref-Molecular_Cell_Biology_4-0" class="reference"><a href="#cite_note-Molecular_Cell_Biology-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> For example, the simplest structures of lipids are <a href="/wiki/Fatty_acids" class="mw-redirect" title="Fatty acids">fatty acids</a>. Fatty acids are <a href="/wiki/Hydrocarbon" title="Hydrocarbon">hydrocarbon</a> derivatives; they contain a <a href="/wiki/Carboxyl_group" class="mw-redirect" title="Carboxyl group">carboxyl group</a> "head" and a hydrocarbon chain "tail".<sup id="cite_ref-Molecular_Cell_Biology_4-1" class="reference"><a href="#cite_note-Molecular_Cell_Biology-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> These fatty acids create larger components, which in turn incorporate noncovalent interactions to form the lipid bilayer.<sup id="cite_ref-Molecular_Cell_Biology_4-2" class="reference"><a href="#cite_note-Molecular_Cell_Biology-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Fatty acid chains are found in two major components of membrane lipids: <a href="/wiki/Phospholipids" class="mw-redirect" title="Phospholipids">phospholipids</a> and <a href="/wiki/Sphingolipids" class="mw-redirect" title="Sphingolipids">sphingolipids</a>. A third major membrane component, <a href="/wiki/Cholesterol" title="Cholesterol">cholesterol</a>, does not contain these fatty acid units.<sup id="cite_ref-Lehninger_5-0" class="reference"><a href="#cite_note-Lehninger-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Eukaryotic_phospholipids">Eukaryotic phospholipids</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=4" title="Edit section: Eukaryotic phospholipids"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></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">See also: <a href="/wiki/Phospholipid#Phospholipid_synthesis" title="Phospholipid">Phospholipid § Phospholipid synthesis</a></div> <p>The foundation of all <a href="/wiki/Biomembrane" class="mw-redirect" title="Biomembrane">biomembranes</a> consists of a <a href="/wiki/Bilayer" title="Bilayer">bilayer</a> structure of phospholipids.<sup id="cite_ref-Hanin_6-0" class="reference"><a href="#cite_note-Hanin-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> The phospholipid molecule is <a href="/wiki/Amphipathic" class="mw-redirect" title="Amphipathic">amphipathic</a>; it contains a <a href="/wiki/Hydrophilic" class="mw-redirect" title="Hydrophilic">hydrophilic</a> polar head and a <a href="/wiki/Hydrophobic" class="mw-redirect" title="Hydrophobic">hydrophobic</a> nonpolar tail.<sup id="cite_ref-Molecular_Cell_Biology_4-3" class="reference"><a href="#cite_note-Molecular_Cell_Biology-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> The phospholipid heads interact with each other and aqueous media, while the hydrocarbon tails orient themselves in the center, away from water.<sup id="cite_ref-Vance_7-0" class="reference"><a href="#cite_note-Vance-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> These latter interactions drive the bilayer structure that acts as a barrier for ions and molecules.<sup id="cite_ref-Katsaras_8-0" class="reference"><a href="#cite_note-Katsaras-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> </p><p>There are various types of phospholipids; consequently, their synthesis pathways differ. However, the first step in phospholipid synthesis involves the formation of <a href="/wiki/Phosphatidate" class="mw-redirect" title="Phosphatidate">phosphatidate</a> or <a href="/wiki/Diacylglycerol_3-phosphate" class="mw-redirect" title="Diacylglycerol 3-phosphate">diacylglycerol 3-phosphate</a> at the <a href="/wiki/Endoplasmic_reticulum" title="Endoplasmic reticulum">endoplasmic reticulum</a> and <a href="/wiki/Outer_mitochondrial_membrane" class="mw-redirect" title="Outer mitochondrial membrane">outer mitochondrial membrane</a>.<sup id="cite_ref-Vance_7-1" class="reference"><a href="#cite_note-Vance-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> The synthesis pathway is found below: </p> <figure class="mw-halign-center" typeof="mw:File/Frameless"><a href="/wiki/File:Phosphatidic_acid_synthesis.svg" class="mw-file-description" title="Phosphatidic acid synthesis"><img alt="Phosphatidic acid synthesis" src="//upload.wikimedia.org/wikipedia/commons/thumb/3/37/Phosphatidic_acid_synthesis.svg/663px-Phosphatidic_acid_synthesis.svg.png" decoding="async" width="663" height="181" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/3/37/Phosphatidic_acid_synthesis.svg/995px-Phosphatidic_acid_synthesis.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/3/37/Phosphatidic_acid_synthesis.svg/1326px-Phosphatidic_acid_synthesis.svg.png 2x" data-file-width="813" data-file-height="222" /></a><figcaption>Phosphatidic acid synthesis</figcaption></figure> <p>The pathway starts with glycerol 3-phosphate, which gets converted to <a href="/wiki/Lysophosphatidate" class="mw-redirect" title="Lysophosphatidate">lysophosphatidate</a> via the addition of a fatty acid chain provided by <a href="/wiki/Acyl_coenzyme_a" class="mw-redirect" title="Acyl coenzyme a">acyl coenzyme A</a>.<sup id="cite_ref-Stryer_9-0" class="reference"><a href="#cite_note-Stryer-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> Then, lysophosphatidate is converted to phosphatidate via the addition of another fatty acid chain contributed by a second acyl CoA; all of these steps are catalyzed by the glycerol phosphate <a href="/wiki/Acyltransferase" title="Acyltransferase">acyltransferase</a> enzyme.<sup id="cite_ref-Stryer_9-1" class="reference"><a href="#cite_note-Stryer-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> Phospholipid synthesis continues in the endoplasmic reticulum, and the biosynthesis pathway diverges depending on the components of the particular phospholipid.<sup id="cite_ref-Stryer_9-2" class="reference"><a href="#cite_note-Stryer-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Sphingolipids">Sphingolipids</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=5" title="Edit section: Sphingolipids"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Like phospholipids, these fatty acid derivatives have a polar head and nonpolar tails.<sup id="cite_ref-Lehninger_5-1" class="reference"><a href="#cite_note-Lehninger-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> Unlike phospholipids, sphingolipids have a <a href="/wiki/Sphingosine" title="Sphingosine">sphingosine</a> backbone.<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> Sphingolipids exist in <a href="/wiki/Eukaryotic" class="mw-redirect" title="Eukaryotic">eukaryotic</a> cells and are particularly abundant in the <a href="/wiki/Central_nervous_system" title="Central nervous system">central nervous system</a>.<sup id="cite_ref-Vance_7-2" class="reference"><a href="#cite_note-Vance-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> For example, <a href="/wiki/Sphingomyelin" title="Sphingomyelin">sphingomyelin</a> is part of the <a href="/wiki/Myelin_sheath" class="mw-redirect" title="Myelin sheath">myelin sheath</a> of nerve fibers.<sup id="cite_ref-Siegel_11-0" class="reference"><a href="#cite_note-Siegel-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> </p><p>Sphingolipids are formed from <a href="/wiki/Ceramide" title="Ceramide">ceramides</a> that consist of a fatty acid chain attached to the amino group of a sphingosine backbone. These ceramides are synthesized from the <a href="/wiki/Acylation" title="Acylation">acylation</a> of sphingosine.<sup id="cite_ref-Siegel_11-1" class="reference"><a href="#cite_note-Siegel-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> The biosynthetic pathway for sphingosine is found below: </p> <figure class="mw-halign-center" typeof="mw:File/Frameless"><a href="/wiki/File:Sphingosine_synthesis_corrected.png" class="mw-file-description" title="Sphingosine synthesis"><img alt="Sphingosine synthesis" src="//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Sphingosine_synthesis_corrected.png/760px-Sphingosine_synthesis_corrected.png" decoding="async" width="760" height="153" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Sphingosine_synthesis_corrected.png/1140px-Sphingosine_synthesis_corrected.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Sphingosine_synthesis_corrected.png/1520px-Sphingosine_synthesis_corrected.png 2x" data-file-width="2389" data-file-height="482" /></a><figcaption>Sphingosine synthesis</figcaption></figure> <p>As the image denotes, during sphingosine synthesis, <a href="/wiki/Palmitoyl_CoA" class="mw-redirect" title="Palmitoyl CoA">palmitoyl CoA</a> and <a href="/wiki/Serine" title="Serine">serine</a> undergo a <a href="/wiki/Condensation_reaction" title="Condensation reaction">condensation reaction</a> which results in the formation of 3-dehydrosphinganine.<sup id="cite_ref-Vance_7-3" class="reference"><a href="#cite_note-Vance-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> This product is then reduced to form dihydrospingosine, which is converted to sphingosine via the <a href="/wiki/Oxidation_reaction" class="mw-redirect" title="Oxidation reaction">oxidation reaction</a> by <a href="/wiki/Flavin_adenine_dinucleotide" title="Flavin adenine dinucleotide">FAD</a>.<sup id="cite_ref-Vance_7-4" class="reference"><a href="#cite_note-Vance-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Cholesterol">Cholesterol</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=6" title="Edit section: Cholesterol"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>This <a href="/wiki/Lipid" title="Lipid">lipid</a> belongs to a class of molecules called <a href="/wiki/Sterols" class="mw-redirect" title="Sterols">sterols</a>.<sup id="cite_ref-Lehninger_5-2" class="reference"><a href="#cite_note-Lehninger-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> Sterols have four fused rings and a <a href="/wiki/Hydroxyl_group" class="mw-redirect" title="Hydroxyl group">hydroxyl group</a>.<sup id="cite_ref-Lehninger_5-3" class="reference"><a href="#cite_note-Lehninger-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> Cholesterol is a particularly important molecule. Not only does it serve as a component of lipid membranes, it is also a precursor to several <a href="/wiki/Steroid" title="Steroid">steroid</a> hormones, including <a href="/wiki/Cortisol" title="Cortisol">cortisol</a>, <a href="/wiki/Testosterone" title="Testosterone">testosterone</a>, and <a href="/wiki/Estrogen" title="Estrogen">estrogen</a>.<sup id="cite_ref-Harris_12-0" class="reference"><a href="#cite_note-Harris-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> </p><p>Cholesterol is synthesized from <a href="/wiki/Acetyl_CoA" class="mw-redirect" title="Acetyl CoA">acetyl CoA</a>.<sup id="cite_ref-Harris_12-1" class="reference"><a href="#cite_note-Harris-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> The pathway is shown below: </p> <figure class="mw-halign-center" typeof="mw:File/Frameless"><a href="/wiki/File:HMG-CoA_reductase_pathway.svg" class="mw-file-description" title="Cholesterol synthesis pathway"><img alt="Cholesterol synthesis pathway" src="//upload.wikimedia.org/wikipedia/commons/thumb/1/17/HMG-CoA_reductase_pathway.svg/400px-HMG-CoA_reductase_pathway.svg.png" decoding="async" width="400" height="729" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/1/17/HMG-CoA_reductase_pathway.svg/600px-HMG-CoA_reductase_pathway.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/1/17/HMG-CoA_reductase_pathway.svg/800px-HMG-CoA_reductase_pathway.svg.png 2x" data-file-width="500" data-file-height="911" /></a><figcaption>Cholesterol synthesis pathway</figcaption></figure> <p>More generally, this synthesis occurs in three stages, with the first stage taking place in the <a href="/wiki/Cytoplasm" title="Cytoplasm">cytoplasm</a> and the second and third stages occurring in the endoplasmic reticulum.<sup id="cite_ref-Stryer_9-3" class="reference"><a href="#cite_note-Stryer-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> The stages are as follows:<sup id="cite_ref-Harris_12-2" class="reference"><a href="#cite_note-Harris-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> </p> <dl><dd><dl><dd>1. The synthesis of <a href="/wiki/Isopentenyl_pyrophosphate" title="Isopentenyl pyrophosphate">isopentenyl pyrophosphate</a>, the "building block" of cholesterol</dd></dl></dd></dl> <dl><dd><dl><dd>2. The formation of <a href="/wiki/Squalene" title="Squalene">squalene</a> via the condensation of six molecules of isopentenyl phosphate</dd></dl></dd></dl> <dl><dd><dl><dd>3. The conversion of squalene into cholesterol via several enzymatic reactions</dd></dl></dd></dl> <div style="clear:both;" class=""></div> <div class="mw-heading mw-heading2"><h2 id="Nucleotides">Nucleotides</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=7" title="Edit section: Nucleotides"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The biosynthesis of <a href="/wiki/Nucleotide" title="Nucleotide">nucleotides</a> involves enzyme-<a href="/wiki/Catalyst" class="mw-redirect" title="Catalyst">catalyzed</a> reactions that convert substrates into more complex products.<sup id="cite_ref-isbn0-8153-3218-1_1-1" class="reference"><a href="#cite_note-isbn0-8153-3218-1-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> Nucleotides are the building blocks of <a href="/wiki/DNA" title="DNA">DNA</a> and <a href="/wiki/RNA" title="RNA">RNA</a>. Nucleotides are composed of a five-membered ring formed from <a href="/wiki/Ribose" title="Ribose">ribose</a> sugar in RNA, and <a href="/wiki/Deoxyribose" title="Deoxyribose">deoxyribose</a> sugar in DNA; these sugars are linked to a <a href="/wiki/Purine" title="Purine">purine</a> or <a href="/wiki/Pyrimidine" title="Pyrimidine">pyrimidine</a> base with a <a href="/wiki/Glycosidic_bond" title="Glycosidic bond">glycosidic bond</a> and a <a href="/wiki/Phosphate" title="Phosphate">phosphate</a> group at the <a href="/wiki/Ribonucleotide" title="Ribonucleotide">5' location</a> of the sugar.<sup id="cite_ref-Watson's_Molecular_Biology_of_the_Gene_13-0" class="reference"><a href="#cite_note-Watson's_Molecular_Biology_of_the_Gene-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Purine_nucleotides">Purine nucleotides</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=8" title="Edit section: Purine nucleotides"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure typeof="mw:File/Thumb"><a href="/wiki/File:Nucleotides_syn1.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/2/25/Nucleotides_syn1.svg/380px-Nucleotides_syn1.svg.png" decoding="async" width="380" height="343" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/2/25/Nucleotides_syn1.svg/570px-Nucleotides_syn1.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/2/25/Nucleotides_syn1.svg/760px-Nucleotides_syn1.svg.png 2x" data-file-width="1062" data-file-height="958" /></a><figcaption><div style="border-width: 0px; border-bottom: 1px solid black; text-align: left;"><b>The synthesis of IMP</b>.</div></figcaption></figure> <p>The DNA nucleotides <a href="/wiki/Adenosine" title="Adenosine">adenosine</a> and <a href="/wiki/Guanosine" title="Guanosine">guanosine</a> consist of a purine base attached to a ribose sugar with a glycosidic bond. In the case of RNA nucleotides <a href="/wiki/Deoxyadenosine" title="Deoxyadenosine">deoxyadenosine</a> and <a href="/wiki/Deoxyguanosine" title="Deoxyguanosine">deoxyguanosine</a>, the purine bases are attached to a deoxyribose sugar with a glycosidic bond. The purine bases on DNA and RNA nucleotides are synthesized in a twelve-step reaction mechanism present in most single-celled organisms. Higher <a href="/wiki/Eukaryotes" class="mw-redirect" title="Eukaryotes">eukaryotes</a> employ a similar <a href="/wiki/Reaction_mechanism" title="Reaction mechanism">reaction mechanism</a> in ten reaction steps. Purine bases are synthesized by converting <a href="/wiki/Phosphoribosyl_pyrophosphate" title="Phosphoribosyl pyrophosphate">phosphoribosyl pyrophosphate</a> (PRPP) to <a href="/wiki/Inosine_monophosphate" class="mw-redirect" title="Inosine monophosphate">inosine monophosphate</a> (IMP), which is the first key intermediate in purine base biosynthesis.<sup id="cite_ref-Kappock/Purine_14-0" class="reference"><a href="#cite_note-Kappock/Purine-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> Further enzymatic modification of <a href="/wiki/Inosine_monophosphate" class="mw-redirect" title="Inosine monophosphate">IMP</a> produces the adenosine and guanosine bases of nucleotides. </p> <ol><li>The first step in purine biosynthesis is a <a href="/wiki/Condensation_reaction" title="Condensation reaction">condensation reaction</a>, performed by <a href="/wiki/Amidophosphoribosyltransferase" title="Amidophosphoribosyltransferase">glutamine-PRPP amidotransferase</a>. This enzyme transfers the <a href="/wiki/Amino_group" class="mw-redirect" title="Amino group">amino group</a> from <a href="/wiki/Glutamine" title="Glutamine">glutamine</a> to PRPP, forming <a href="/wiki/5-phosphoribosylamine" class="mw-redirect" title="5-phosphoribosylamine">5-phosphoribosylamine</a>. The following step requires the activation of <a href="/wiki/Glycine" title="Glycine">glycine</a> by the addition of a <a href="/wiki/Phosphate" title="Phosphate">phosphate</a> group from <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a>.</li> <li>GAR synthetase<sup id="cite_ref-15" class="reference"><a href="#cite_note-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup> performs the condensation of activated glycine onto PRPP, forming <a href="/wiki/Glycineamide_ribonucleotide" title="Glycineamide ribonucleotide">glycineamide ribonucleotide</a> (GAR).</li> <li><a href="/wiki/GAR_transformylase" class="mw-redirect" title="GAR transformylase">GAR transformylase</a> adds a <a href="/wiki/Formyl_group" class="mw-redirect" title="Formyl group">formyl group</a> onto the amino group of GAR, forming formylglycinamide ribonucleotide (FGAR).</li> <li>FGAR amidotransferase<sup id="cite_ref-16" class="reference"><a href="#cite_note-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> catalyzes the addition of a nitrogen group to FGAR, forming formylglycinamidine ribonucleotide (FGAM).</li> <li><a href="/wiki/AIR_synthetase_(FGAM_cyclase)" title="AIR synthetase (FGAM cyclase)">FGAM cyclase</a> catalyzes ring closure, which involves removal of a water molecule, forming the 5-membered <a href="/wiki/Imidazole" title="Imidazole">imidazole</a> ring <a href="/wiki/5-Aminoimidazole_ribotide" title="5-Aminoimidazole ribotide">5-aminoimidazole ribonucleotide</a> (AIR).</li> <li>N5-CAIR synthetase transfers a <a href="/wiki/Carboxyl" class="mw-redirect" title="Carboxyl">carboxyl</a> group, forming the intermediate N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).<sup id="cite_ref-17" class="reference"><a href="#cite_note-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/5-(carboxyamino)imidazole_ribonucleotide_mutase" title="5-(carboxyamino)imidazole ribonucleotide mutase">N5-CAIR mutase</a> rearranges the carboxyl functional group and transfers it onto the imidazole ring, forming <a href="/wiki/5%27-phosphoribosyl-4-carboxy-5-aminoimidazole" class="mw-redirect" title="5'-phosphoribosyl-4-carboxy-5-aminoimidazole">carboxyamino- imidazole ribonucleotide</a> (CAIR). The two step mechanism of CAIR formation from AIR is mostly found in single celled organisms. Higher eukaryotes contain the enzyme AIR carboxylase,<sup id="cite_ref-18" class="reference"><a href="#cite_note-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> which transfers a carboxyl group directly to AIR imidazole ring, forming CAIR.</li> <li><a href="/wiki/Phosphoribosylaminoimidazolesuccinocarboxamide_synthase" title="Phosphoribosylaminoimidazolesuccinocarboxamide synthase">SAICAR synthetase</a> forms a <a href="/wiki/Peptide_bond" title="Peptide bond">peptide bond</a> between <a href="/wiki/Aspartate" class="mw-redirect" title="Aspartate">aspartate</a> and the added carboxyl group of the imidazole ring, forming <a href="/wiki/Phosphoribosylaminoimidazolesuccinocarboxamide" title="Phosphoribosylaminoimidazolesuccinocarboxamide">N-succinyl-5-aminoimidazole-4-carboxamide ribonucleotide</a> (SAICAR).</li> <li><a href="/wiki/Adenylosuccinate_lyase" title="Adenylosuccinate lyase">SAICAR lyase</a> removes the carbon skeleton of the added aspartate, leaving the amino group and forming <a href="/wiki/AICA_ribonucleotide" title="AICA ribonucleotide">5-aminoimidazole-4-carboxamide ribonucleotide</a> (AICAR).</li> <li><a href="/wiki/AICAR_transformylase" class="mw-redirect" title="AICAR transformylase">AICAR transformylase</a> transfers a carbonyl group to AICAR, forming <a href="/wiki/5-Formamidoimidazole-4-carboxamide_ribotide" title="5-Formamidoimidazole-4-carboxamide ribotide">N-formylaminoimidazole- 4-carboxamide ribonucleotide</a> (FAICAR).</li> <li>The final step involves the enzyme <a href="/wiki/Inosine_monophosphate_synthase" title="Inosine monophosphate synthase">IMP synthase</a>, which performs the purine ring closure and forms the inosine monophosphate intermediate.<sup id="cite_ref-Lehninger_5-4" class="reference"><a href="#cite_note-Lehninger-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup></li></ol> <div class="mw-heading mw-heading3"><h3 id="Pyrimidine_nucleotides">Pyrimidine nucleotides</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=9" title="Edit section: Pyrimidine nucleotides"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-halign-right" typeof="mw:File/Frame"><a href="/wiki/File:Nucleotides_syn2.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/6/6b/Nucleotides_syn2.png" decoding="async" width="526" height="519" class="mw-file-element" data-file-width="526" data-file-height="519" /></a><figcaption>Uridine monophosphate (UMP) biosynthesis</figcaption></figure> <p>Other DNA and RNA nucleotide bases that are linked to the ribose sugar via a glycosidic bond are <a href="/wiki/Thymine" title="Thymine">thymine</a>, <a href="/wiki/Cytosine" title="Cytosine">cytosine</a> and <a href="/wiki/Uracil" title="Uracil">uracil</a> (which is only found in RNA). <a href="/wiki/Uridine_monophosphate" title="Uridine monophosphate">Uridine monophosphate</a> biosynthesis involves an enzyme that is located in the <a href="/wiki/Inner_mitochondrial_membrane" title="Inner mitochondrial membrane">mitochondrial inner membrane</a> and multifunctional enzymes that are located in the <a href="/wiki/Cytosol" title="Cytosol">cytosol</a>.<sup id="cite_ref-Srere/Metabolic_enzymes_19-0" class="reference"><a href="#cite_note-Srere/Metabolic_enzymes-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> </p> <ol><li>The first step involves the enzyme <a href="/wiki/Carbamoyl_phosphate_synthase" class="mw-redirect" title="Carbamoyl phosphate synthase">carbamoyl phosphate synthase</a> combining <a href="/wiki/Glutamine" title="Glutamine">glutamine</a> with <a href="/wiki/CO2" class="mw-redirect" title="CO2">CO<sub>2</sub></a> in an ATP dependent reaction to form <a href="/wiki/Carbamoyl_phosphate" title="Carbamoyl phosphate">carbamoyl phosphate</a>.</li> <li><a href="/wiki/Aspartate_carbamoyltransferase" title="Aspartate carbamoyltransferase">Aspartate carbamoyltransferase</a> <a href="/wiki/Condensation_reaction" title="Condensation reaction">condenses</a> carbamoyl phosphate with aspartate to form uridosuccinate.</li> <li><a href="/wiki/Dihydroorotase" title="Dihydroorotase">Dihydroorotase</a> performs <a href="/wiki/Ring-closure_reaction" class="mw-redirect" title="Ring-closure reaction">ring closure</a>, a reaction that loses water, to form <a href="/wiki/Dihydroorotate" class="mw-redirect" title="Dihydroorotate">dihydroorotate</a>.</li> <li><a href="/wiki/Dihydroorotate_dehydrogenase" title="Dihydroorotate dehydrogenase">Dihydroorotate dehydrogenase</a>, located within the mitochondrial inner membrane,<sup id="cite_ref-Srere/Metabolic_enzymes_19-1" class="reference"><a href="#cite_note-Srere/Metabolic_enzymes-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> oxidizes dihydroorotate to <a href="/wiki/Orotate" class="mw-redirect" title="Orotate">orotate</a>.</li> <li>Orotate phosphoribosyl hydrolase (OMP pyrophosphorylase) condenses orotate with <a href="/wiki/PRPP" class="mw-redirect" title="PRPP">PRPP</a> to form <a href="/wiki/Orotidine_5%27-monophosphate" title="Orotidine 5'-monophosphate">orotidine-5'-phosphate</a>.</li> <li><a href="/wiki/OMP_decarboxylase" class="mw-redirect" title="OMP decarboxylase">OMP decarboxylase</a> catalyzes the conversion of orotidine-5'-phosphate to <a href="/wiki/Uridine_monophosphate" title="Uridine monophosphate">UMP</a>.<sup id="cite_ref-Broach/Yeast_nucleotide_20-0" class="reference"><a href="#cite_note-Broach/Yeast_nucleotide-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup></li></ol> <p>After the uridine nucleotide base is synthesized, the other bases, cytosine and thymine are synthesized. Cytosine biosynthesis is a two-step reaction which involves the conversion of UMP to <a href="/wiki/Uridine_triphosphate" title="Uridine triphosphate">UTP</a>. <a href="/wiki/Phosphate" title="Phosphate">Phosphate</a> addition to UMP is catalyzed by a <a href="/wiki/Kinase" title="Kinase">kinase</a> enzyme. The enzyme <a href="/wiki/CTP_synthase" class="mw-redirect" title="CTP synthase">CTP synthase</a> catalyzes the next reaction step: the conversion of UTP to <a href="/wiki/Cytidine_triphosphate" title="Cytidine triphosphate">CTP</a> by transferring an <a href="/wiki/Amino_group" class="mw-redirect" title="Amino group">amino group</a> from glutamine to uridine; this forms the cytosine base of CTP.<sup id="cite_ref-O'Donovan/_pyrimidine_microorg_21-0" class="reference"><a href="#cite_note-O'Donovan/_pyrimidine_microorg-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> The mechanism, which depicts the reaction UTP + ATP + glutamine ⇔ CTP + ADP + glutamate, is below: </p> <figure class="mw-halign-right" typeof="mw:File/Frameless"><a href="/wiki/File:Thymidylate_synthase_reaction.svg" class="mw-file-description" title="'Thymidylate synthase reaction: dUMP + 5,10-methylenetetrahydrofolate ⇔ dTMP + dihydrofolate"><img alt="'Thymidylate synthase reaction: dUMP + 5,10-methylenetetrahydrofolate ⇔ dTMP + dihydrofolate" src="//upload.wikimedia.org/wikipedia/commons/thumb/8/8b/Thymidylate_synthase_reaction.svg/247px-Thymidylate_synthase_reaction.svg.png" decoding="async" width="247" height="250" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/8/8b/Thymidylate_synthase_reaction.svg/371px-Thymidylate_synthase_reaction.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/8/8b/Thymidylate_synthase_reaction.svg/494px-Thymidylate_synthase_reaction.svg.png 2x" data-file-width="512" data-file-height="518" /></a><figcaption>'Thymidylate synthase reaction: dUMP + 5,10-methylenetetrahydrofolate ⇔ dTMP + dihydrofolate</figcaption></figure> <figure class="mw-halign-center" typeof="mw:File/Frameless"><a href="/wiki/File:Ctp_synthase_mechanism.jpg" class="mw-file-description" title="Ctp synthase mechanism: UTP + ATP + glutamine ⇔ CTP + ADP + glutamate"><img alt="Ctp synthase mechanism: UTP + ATP + glutamine ⇔ CTP + ADP + glutamate" src="//upload.wikimedia.org/wikipedia/commons/thumb/7/7f/Ctp_synthase_mechanism.jpg/480px-Ctp_synthase_mechanism.jpg" decoding="async" width="480" height="112" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/7/7f/Ctp_synthase_mechanism.jpg/720px-Ctp_synthase_mechanism.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/7/7f/Ctp_synthase_mechanism.jpg/960px-Ctp_synthase_mechanism.jpg 2x" data-file-width="1092" data-file-height="255" /></a><figcaption>Ctp synthase mechanism: UTP + ATP + glutamine ⇔ CTP + ADP + glutamate</figcaption></figure> <p>Cytosine is a nucleotide that is present in both DNA and RNA. However, uracil is only found in RNA. Therefore, after UTP is synthesized, it is must be converted into a <a href="/wiki/Deoxy" class="mw-redirect" title="Deoxy">deoxy</a> form to be incorporated into DNA. This conversion involves the enzyme <a href="/wiki/Ribonucleoside-triphosphate_reductase" title="Ribonucleoside-triphosphate reductase">ribonucleoside triphosphate reductase</a>. This reaction that removes the 2'-OH of the ribose sugar to generate deoxyribose is not affected by the bases attached to the sugar. This non-specificity allows ribonucleoside triphosphate reductase to convert all <a href="/wiki/Nucleotide_triphosphates" class="mw-redirect" title="Nucleotide triphosphates">nucleotide triphosphates</a> to <a href="/wiki/Deoxyribonucleotide" title="Deoxyribonucleotide">deoxyribonucleotide</a> by a similar mechanism.<sup id="cite_ref-O'Donovan/_pyrimidine_microorg_21-1" class="reference"><a href="#cite_note-O'Donovan/_pyrimidine_microorg-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> </p><p>In contrast to uracil, thymine bases are found mostly in DNA, not RNA. Cells do not normally contain thymine bases that are linked to ribose sugars in RNA, thus indicating that cells only synthesize deoxyribose-linked thymine. The enzyme <a href="/wiki/Thymidylate_synthetase" class="mw-redirect" title="Thymidylate synthetase">thymidylate synthetase</a> is responsible for synthesizing thymine residues from <a href="/wiki/DUMP" class="mw-redirect" title="DUMP">dUMP</a> to <a href="/wiki/DTMP" class="mw-redirect" title="DTMP">dTMP</a>. This reaction transfers a <a href="/wiki/Methyl" class="mw-redirect" title="Methyl">methyl</a> group onto the uracil base of dUMP to generate dTMP.<sup id="cite_ref-O'Donovan/_pyrimidine_microorg_21-2" class="reference"><a href="#cite_note-O'Donovan/_pyrimidine_microorg-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> The thymidylate synthase reaction, dUMP + 5,10-methylenetetrahydrofolate ⇔ dTMP + dihydrofolate, is shown to the right. </p> <div style="clear:both;" class=""></div> <div class="mw-heading mw-heading2"><h2 id="DNA">DNA</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=10" title="Edit section: DNA"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-halign-right" typeof="mw:File/Frame"><a href="/wiki/File:DNA_replication_en.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/8/8f/DNA_replication_en.svg/691px-DNA_replication_en.svg.png" decoding="async" width="691" height="336" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/8/8f/DNA_replication_en.svg/1037px-DNA_replication_en.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/8/8f/DNA_replication_en.svg/1382px-DNA_replication_en.svg.png 2x" data-file-width="691" data-file-height="336" /></a><figcaption>As DNA polymerase moves in a 3' to 5' direction along the template strand, it synthesizes a new strand in the 5' to 3' direction</figcaption></figure> <p>Although there are differences between <a href="/wiki/Eukaryotic" class="mw-redirect" title="Eukaryotic">eukaryotic</a> and <a href="/wiki/Prokaryotic" class="mw-redirect" title="Prokaryotic">prokaryotic</a> DNA synthesis, the following section denotes key characteristics of DNA replication shared by both organisms. </p><p><a href="/wiki/DNA" title="DNA">DNA</a> is composed of <a href="/wiki/Nucleotide" title="Nucleotide">nucleotides</a> that are joined by <a href="/wiki/Phosphodiester_bonds" class="mw-redirect" title="Phosphodiester bonds">phosphodiester bonds</a>.<sup id="cite_ref-Molecular_Cell_Biology_4-4" class="reference"><a href="#cite_note-Molecular_Cell_Biology-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> <a href="/wiki/DNA_replication" title="DNA replication">DNA synthesis</a>, which takes place in the <a href="/wiki/Cell_nucleus" title="Cell nucleus">nucleus</a>, is a <a href="/wiki/Semiconservative_replication" title="Semiconservative replication">semiconservative</a> process, which means that the resulting DNA molecule contains an original strand from the parent structure and a new strand.<sup id="cite_ref-Karp's_Cell_and_Molecular_Biology_22-0" class="reference"><a href="#cite_note-Karp's_Cell_and_Molecular_Biology-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> DNA synthesis is catalyzed by a family of <a href="/wiki/DNA_polymerases" class="mw-redirect" title="DNA polymerases">DNA polymerases</a> that require four deoxynucleoside triphosphates, a <a href="/wiki/Template_strand#Elongation" class="mw-redirect" title="Template strand">template strand</a>, and a <a href="/wiki/Rna_primer" class="mw-redirect" title="Rna primer">primer</a> with a free 3'OH in which to incorporate nucleotides.<sup id="cite_ref-Griffiths_23-0" class="reference"><a href="#cite_note-Griffiths-23"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup> </p><p>In order for DNA replication to occur, a <a href="/wiki/Replication_fork#Replication_fork" class="mw-redirect" title="Replication fork">replication fork</a> is created by enzymes called <a href="/wiki/Helicase" title="Helicase">helicases</a> which unwind the DNA helix.<sup id="cite_ref-Griffiths_23-1" class="reference"><a href="#cite_note-Griffiths-23"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup> <a href="/wiki/Topoisomerase" title="Topoisomerase">Topoisomerases</a> at the replication fork remove <a href="/wiki/DNA_supercoil" title="DNA supercoil">supercoils</a> caused by DNA unwinding, and <a href="/wiki/Single-strand_binding_protein" class="mw-redirect" title="Single-strand binding protein">single-stranded DNA binding proteins</a> maintain the two single-stranded DNA templates stabilized prior to replication.<sup id="cite_ref-Watson's_Molecular_Biology_of_the_Gene_13-1" class="reference"><a href="#cite_note-Watson's_Molecular_Biology_of_the_Gene-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup> </p><p>DNA synthesis is initiated by the <a href="/wiki/RNA_polymerase" title="RNA polymerase">RNA polymerase</a> <a href="/wiki/Primase" title="Primase">primase</a>, which makes an RNA primer with a free 3'OH.<sup id="cite_ref-Griffiths_23-2" class="reference"><a href="#cite_note-Griffiths-23"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup> This primer is attached to the single-stranded DNA template, and DNA polymerase elongates the chain by incorporating nucleotides; DNA polymerase also proofreads the newly synthesized DNA strand.<sup id="cite_ref-Griffiths_23-3" class="reference"><a href="#cite_note-Griffiths-23"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup> </p><p>During the polymerization reaction catalyzed by DNA polymerase, a <a href="/wiki/Nucleophilic_attack" class="mw-redirect" title="Nucleophilic attack">nucleophilic attack</a> occurs by the 3'OH of the growing chain on the innermost phosphorus atom of a deoxynucleoside triphosphate; this yields the formation of a <a href="/wiki/Phosphodiester_bridges" class="mw-redirect" title="Phosphodiester bridges">phosphodiester bridge</a> that attaches a new nucleotide and releases <a href="/wiki/Pyrophosphate" title="Pyrophosphate">pyrophosphate</a>.<sup id="cite_ref-Stryer_9-4" class="reference"><a href="#cite_note-Stryer-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> </p><p>Two types of strands are created simultaneously during replication: the <a href="/wiki/Leading_strand#Replication_fork" class="mw-redirect" title="Leading strand">leading strand</a>, which is synthesized continuously and grows towards the replication fork, and the <a href="/wiki/Lagging_strand#Replication_fork" class="mw-redirect" title="Lagging strand">lagging strand</a>, which is made discontinuously in <a href="/wiki/Okazaki_fragments" title="Okazaki fragments">Okazaki fragments</a> and grows away from the replication fork.<sup id="cite_ref-Karp's_Cell_and_Molecular_Biology_22-1" class="reference"><a href="#cite_note-Karp's_Cell_and_Molecular_Biology-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> Okazaki fragments are <a href="/wiki/Covalently" class="mw-redirect" title="Covalently">covalently</a> joined by <a href="/wiki/DNA_ligase" title="DNA ligase">DNA ligase</a> to form a continuous strand.<sup id="cite_ref-Karp's_Cell_and_Molecular_Biology_22-2" class="reference"><a href="#cite_note-Karp's_Cell_and_Molecular_Biology-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> Then, to complete DNA replication, RNA primers are removed, and the resulting gaps are replaced with DNA and joined via DNA ligase.<sup id="cite_ref-Karp's_Cell_and_Molecular_Biology_22-3" class="reference"><a href="#cite_note-Karp's_Cell_and_Molecular_Biology-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> </p> <div style="clear:both;" class=""></div> <div class="mw-heading mw-heading2"><h2 id="Amino_acids">Amino acids</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=11" title="Edit section: 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/Amino_acid_synthesis" title="Amino acid synthesis">Amino acid synthesis</a></div> <p>A protein is a polymer that is composed from <a href="/wiki/Amino_acid" title="Amino acid">amino acids</a> that are linked by <a href="/wiki/Peptide_bond" title="Peptide bond">peptide bonds</a>. There are more than <a href="/wiki/Amino_acid#Non-standard_amino_acids" title="Amino acid">300 amino acids</a> found in nature of which only twenty two, known as the <a href="/wiki/Proteinogenic_amino_acids" class="mw-redirect" title="Proteinogenic amino acids">proteinogenic amino acids</a>, are the building blocks for protein.<sup id="cite_ref-AA_structure_24-0" class="reference"><a href="#cite_note-AA_structure-24"><span class="cite-bracket">[</span>24<span class="cite-bracket">]</span></a></sup> Only <a href="/wiki/Green_plants" class="mw-redirect" title="Green plants">green plants</a> and most <a href="/wiki/Microbes" class="mw-redirect" title="Microbes">microbes</a> are able to <a href="/wiki/Amino_acid_synthesis" title="Amino acid synthesis">synthesize</a> all of the 20 standard amino acids that are needed by all living species. <a href="/wiki/Mammal" title="Mammal">Mammals</a> can only synthesize ten of the twenty standard amino acids. The other amino acids, <a href="/wiki/Valine" title="Valine">valine</a>, <a href="/wiki/Methionine" title="Methionine">methionine</a>, <a href="/wiki/Leucine" title="Leucine">leucine</a>, <a href="/wiki/Isoleucine" title="Isoleucine">isoleucine</a>, <a href="/wiki/Phenylalanine" title="Phenylalanine">phenylalanine</a>, <a href="/wiki/Lysine" title="Lysine">lysine</a>, <a href="/wiki/Threonine" title="Threonine">threonine</a> and <a href="/wiki/Tryptophan" title="Tryptophan">tryptophan</a> for adults and <a href="/wiki/Histidine" title="Histidine">histidine</a>, and <a href="/wiki/Arginine" title="Arginine">arginine</a> for babies are obtained through diet.<sup id="cite_ref-25" class="reference"><a href="#cite_note-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Amino_acid_basic_structure">Amino acid basic structure</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=12" title="Edit section: Amino acid basic structure"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-halign-left" typeof="mw:File/Frame"><a href="/wiki/File:L-amino_acid_general.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/1/1c/L-amino_acid_general.svg/195px-L-amino_acid_general.svg.png" decoding="async" width="195" height="156" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/1/1c/L-amino_acid_general.svg/293px-L-amino_acid_general.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/1/1c/L-amino_acid_general.svg/390px-L-amino_acid_general.svg.png 2x" data-file-width="195" data-file-height="156" /></a><figcaption>L-amino acid</figcaption></figure><p>The general structure of the standard amino acids includes a <a href="/wiki/Amine" title="Amine">primary amino group</a>, a <a href="/wiki/Carboxyl_group" class="mw-redirect" title="Carboxyl group">carboxyl group</a> and the <a href="/wiki/Functional_group" title="Functional group">functional group</a> attached to the <a href="/wiki/Alpha-carbon" class="mw-redirect" title="Alpha-carbon">α-carbon</a>. The different amino acids are identified by the functional group. As a result of the three different groups attached to the α-carbon, amino acids are <a href="/wiki/Chirality_(chemistry)#Definition" title="Chirality (chemistry)">asymmetrical molecules</a>. For all standard amino acids, except <a href="/wiki/Glycine" title="Glycine">glycine</a>, the α-carbon is a <a href="/wiki/Chiral_center" class="mw-redirect" title="Chiral center">chiral center</a>. In the case of glycine, the α-carbon has two hydrogen atoms, thus adding symmetry to this molecule. With the exception of <a href="/wiki/Proline" title="Proline">proline</a>, all of the amino acids found in life have the <a href="/wiki/Chirality_(chemistry)#By_configuration:_D-_and_L-" title="Chirality (chemistry)">L-isoform</a> conformation. Proline has a functional group on the α-carbon that forms a ring with the amino group.<sup id="cite_ref-AA_structure_24-1" class="reference"><a href="#cite_note-AA_structure-24"><span class="cite-bracket">[</span>24<span class="cite-bracket">]</span></a></sup> </p><figure class="mw-halign-right" typeof="mw:File/Frameless"><a href="/wiki/File:Glutamine_oxoglutarate_aminotransferase_and_Glutamine_synthetase.svg" class="mw-file-description" title="Glutamine oxoglutarate aminotransferase and glutamine synthetase"><img alt="Glutamine oxoglutarate aminotransferase and glutamine synthetase" src="//upload.wikimedia.org/wikipedia/commons/thumb/7/73/Glutamine_oxoglutarate_aminotransferase_and_Glutamine_synthetase.svg/240px-Glutamine_oxoglutarate_aminotransferase_and_Glutamine_synthetase.svg.png" decoding="async" width="240" height="182" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/7/73/Glutamine_oxoglutarate_aminotransferase_and_Glutamine_synthetase.svg/360px-Glutamine_oxoglutarate_aminotransferase_and_Glutamine_synthetase.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/7/73/Glutamine_oxoglutarate_aminotransferase_and_Glutamine_synthetase.svg/480px-Glutamine_oxoglutarate_aminotransferase_and_Glutamine_synthetase.svg.png 2x" data-file-width="620" data-file-height="469" /></a><figcaption>Glutamine oxoglutarate aminotransferase and glutamine synthetase</figcaption></figure> <div class="mw-heading mw-heading3"><h3 id="Nitrogen_source">Nitrogen source</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=13" title="Edit section: Nitrogen source"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>One major step in amino acid biosynthesis involves incorporating a nitrogen group onto the α-carbon. In cells, there are two major pathways of incorporating nitrogen groups. One pathway involves the enzyme <a href="/wiki/Glutamine_oxoglutarate_aminotransferase" class="mw-redirect" title="Glutamine oxoglutarate aminotransferase">glutamine oxoglutarate aminotransferase</a> (GOGAT) which removes the <a href="/wiki/Amide" title="Amide">amide</a> amino group of <a href="/wiki/Glutamine" title="Glutamine">glutamine</a> and transfers it onto <a href="/wiki/2-oxoglutarate" class="mw-redirect" title="2-oxoglutarate">2-oxoglutarate</a>, producing two <a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a> molecules. In this catalysis reaction, glutamine serves as the nitrogen source. An image illustrating this reaction is found to the right. </p><p>The other pathway for incorporating nitrogen onto the α-carbon of amino acids involves the enzyme <a href="/wiki/Glutamate_dehydrogenase" title="Glutamate dehydrogenase">glutamate dehydrogenase</a> (GDH). GDH is able to transfer <a href="/wiki/Ammonia" title="Ammonia">ammonia</a> onto 2-oxoglutarate and form glutamate. Furthermore, the enzyme <a href="/wiki/Glutamine_synthetase" title="Glutamine synthetase">glutamine synthetase</a> (GS) is able to transfer ammonia onto glutamate and synthesize glutamine, replenishing glutamine.<sup id="cite_ref-AA_Metabolism_Miflin_26-0" class="reference"><a href="#cite_note-AA_Metabolism_Miflin-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="The_glutamate_family_of_amino_acids">The glutamate family of amino acids</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=14" title="Edit section: The glutamate family of amino acids"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a> family of amino acids includes the amino acids that derive from the amino acid glutamate. This family includes: glutamate, <a href="/wiki/Glutamine" title="Glutamine">glutamine</a>, <a href="/wiki/Proline" title="Proline">proline</a>, and <a href="/wiki/Arginine" title="Arginine">arginine</a>. This family also includes the amino acid <a href="/wiki/Lysine" title="Lysine">lysine</a>, which is derived from <a href="/wiki/%CE%91-ketoglutarate" class="mw-redirect" title="Α-ketoglutarate">α-ketoglutarate</a>.<sup id="cite_ref-Amino_Families_27-0" class="reference"><a href="#cite_note-Amino_Families-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup> </p><p>The biosynthesis of glutamate and glutamine is a key step in the nitrogen assimilation discussed above. The enzymes <a href="/wiki/GOGAT" class="mw-redirect" title="GOGAT">GOGAT</a> and <a href="/wiki/Glutamate_dehydrogenase" title="Glutamate dehydrogenase">GDH</a> catalyze the <a href="/wiki/Nitrogen_assimilation" title="Nitrogen assimilation">nitrogen assimilation</a> reactions. </p><p>In bacteria, the enzyme <a href="/wiki/Glutamate_5-kinase" title="Glutamate 5-kinase">glutamate 5-kinase</a> initiates the biosynthesis of proline by transferring a phosphate group from ATP onto glutamate. The next reaction is catalyzed by the enzyme <a href="/wiki/Glutamate-5-semialdehyde_dehydrogenase" title="Glutamate-5-semialdehyde dehydrogenase">pyrroline-5-carboxylate synthase</a> (P5CS), which catalyzes the reduction of the <a href="/wiki/Gamma-carboxylation" class="mw-redirect" title="Gamma-carboxylation">ϒ-carboxyl</a> group of L-glutamate 5-phosphate. This results in the formation of glutamate semialdehyde, which spontaneously cyclizes to pyrroline-5-carboxylate. Pyrroline-5-carboxylate is further reduced by the enzyme pyrroline-5-carboxylate reductase (P5CR) to yield a proline amino acid.<sup id="cite_ref-28" class="reference"><a href="#cite_note-28"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup> </p><p>In the first step of arginine biosynthesis in bacteria, glutamate is <a href="/wiki/Acetylated" class="mw-redirect" title="Acetylated">acetylated</a> by transferring the acetyl group from acetyl-CoA at the N-α position; this prevents spontaneous cyclization. The enzyme <a href="/wiki/N-acetylglutamate_synthase" class="mw-redirect" title="N-acetylglutamate synthase">N-acetylglutamate synthase</a> (glutamate N-acetyltransferase) is responsible for catalyzing the acetylation step. Subsequent steps are catalyzed by the enzymes <a href="/wiki/Acetylglutamate_kinase" title="Acetylglutamate kinase">N-acetylglutamate kinase</a>, <a href="/wiki/N-acetyl-gamma-glutamyl-phosphate_reductase" title="N-acetyl-gamma-glutamyl-phosphate reductase">N-acetyl-gamma-glutamyl-phosphate reductase</a>, and <a href="/wiki/Acetylornithine_transaminase" title="Acetylornithine transaminase">acetylornithine/succinyldiamino pimelate aminotransferase</a> and yield the N-acetyl-L-ornithine. The acetyl group of acetylornithine is removed by the enzyme <a href="/wiki/Acetylornithine_deacetylase" title="Acetylornithine deacetylase">acetylornithinase</a> (AO) or <a href="/wiki/Glutamate_N-acetyltransferase" title="Glutamate N-acetyltransferase">ornithine acetyltransferase</a> (OAT), and this yields <a href="/wiki/Ornithine" title="Ornithine">ornithine</a>. Then, the enzymes <a href="/wiki/Citrulline" title="Citrulline">citrulline</a> and <a href="/wiki/Argininosuccinate" class="mw-redirect" title="Argininosuccinate">argininosuccinate</a> convert ornithine to arginine.<sup id="cite_ref-29" class="reference"><a href="#cite_note-29"><span class="cite-bracket">[</span>29<span class="cite-bracket">]</span></a></sup> </p> <figure class="mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:Lysine_Biosynthesis.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/c/cd/Lysine_Biosynthesis.png/500px-Lysine_Biosynthesis.png" decoding="async" width="500" height="478" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/c/cd/Lysine_Biosynthesis.png/750px-Lysine_Biosynthesis.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/c/cd/Lysine_Biosynthesis.png/1000px-Lysine_Biosynthesis.png 2x" data-file-width="2227" data-file-height="2130" /></a><figcaption>The diaminopimelic acid pathway</figcaption></figure> <p>There are two distinct lysine biosynthetic pathways: the diaminopimelic acid pathway and the <a href="/wiki/Alpha-aminoadipate_pathway" class="mw-redirect" title="Alpha-aminoadipate pathway">α-aminoadipate pathway</a>. The most common of the two synthetic pathways is the diaminopimelic acid pathway; it consists of several enzymatic reactions that add carbon groups to aspartate to yield lysine:<sup id="cite_ref-30" class="reference"><a href="#cite_note-30"><span class="cite-bracket">[</span>30<span class="cite-bracket">]</span></a></sup> </p> <ol><li><a href="/wiki/Aspartate_kinase" title="Aspartate kinase">Aspartate kinase</a> initiates the diaminopimelic acid pathway by phosphorylating aspartate and producing aspartyl phosphate.</li> <li><a href="/wiki/Aspartate-semialdehyde_dehydrogenase" title="Aspartate-semialdehyde dehydrogenase">Aspartate semialdehyde dehydrogenase</a> catalyzes the <a href="/wiki/NADPH" class="mw-redirect" title="NADPH">NADPH</a>-dependent reduction of aspartyl phosphate to yield aspartate semialdehyde.</li> <li><a href="/wiki/4-hydroxy-tetrahydrodipicolinate_synthase" class="mw-redirect" title="4-hydroxy-tetrahydrodipicolinate synthase">4-hydroxy-tetrahydrodipicolinate synthase</a> adds a <a href="/wiki/Pyruvic_acid" title="Pyruvic acid">pyruvate</a> group to the β-aspartyl-4-semialdehyde, and a water molecule is removed. This causes <a href="/wiki/Cyclic_compound" title="Cyclic compound">cyclization</a> and gives rise to (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate.</li> <li><a href="/wiki/Dihydrodipicolinate_reductase" class="mw-redirect" title="Dihydrodipicolinate reductase">4-hydroxy-tetrahydrodipicolinate reductase</a> catalyzes the reduction of (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate by NADPH to yield Δ'-piperideine-2,6-dicarboxylate (2,3,4,5-tetrahydrodipicolinate) and H<sub>2</sub>O.</li> <li><a href="/wiki/Tetrahydrodipicolinate_N-acetyltransferase" title="Tetrahydrodipicolinate N-acetyltransferase">Tetrahydrodipicolinate acyltransferase</a> catalyzes the acetylation reaction that results in ring opening and yields N-acetyl α-amino-ε-ketopimelate.</li> <li><a href="/wiki/Succinyldiaminopimelate_transaminase" title="Succinyldiaminopimelate transaminase">N-succinyl-α-amino-ε-ketopimelate-glutamate aminotransaminase</a> catalyzes the transamination reaction that removes the keto group of N-acetyl α-amino-ε-ketopimelate and replaces it with an amino group to yield N-succinyl-L-diaminopimelate.<sup id="cite_ref-31" class="reference"><a href="#cite_note-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Succinyl-diaminopimelate_desuccinylase" title="Succinyl-diaminopimelate desuccinylase">N-acyldiaminopimelate deacylase</a> catalyzes the deacylation of N-succinyl-L-diaminopimelate to yield L,L-diaminopimelate.<sup id="cite_ref-32" class="reference"><a href="#cite_note-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Diaminopimelate_epimerase" title="Diaminopimelate epimerase">DAP epimerase</a> catalyzes the conversion of L,L-diaminopimelate to the <a href="/wiki/Meso_form" class="mw-redirect" title="Meso form">meso</a> form of L,L-diaminopimelate.<sup id="cite_ref-33" class="reference"><a href="#cite_note-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Diaminopimelate_decarboxylase" title="Diaminopimelate decarboxylase">DAP decarboxylase</a> catalyzes the removal of the carboxyl group, yielding L-lysine.</li></ol> <div class="mw-heading mw-heading3"><h3 id="The_serine_family_of_amino_acids">The serine family of amino acids</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=15" title="Edit section: The serine family of amino acids"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/wiki/Serine" title="Serine">serine</a> family of amino acid includes: serine, <a href="/wiki/Cysteine" title="Cysteine">cysteine</a>, and <a href="/wiki/Glycine" title="Glycine">glycine</a>. Most microorganisms and plants obtain the sulfur for synthesizing <a href="/wiki/Methionine" title="Methionine">methionine</a> from the amino acid cysteine. Furthermore, the conversion of serine to glycine provides the carbons needed for the biosynthesis of the methionine and <a href="/wiki/Histidine" title="Histidine">histidine</a>.<sup id="cite_ref-Amino_Families_27-1" class="reference"><a href="#cite_note-Amino_Families-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup> </p><p>During serine biosynthesis,<sup id="cite_ref-34" class="reference"><a href="#cite_note-34"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup> the enzyme <a href="/wiki/Phosphoglycerate_dehydrogenase" title="Phosphoglycerate dehydrogenase">phosphoglycerate dehydrogenase</a> catalyzes the initial reaction that <a href="/wiki/Oxidizes" class="mw-redirect" title="Oxidizes">oxidizes</a> <a href="/wiki/3-phospho-D-glycerate" class="mw-redirect" title="3-phospho-D-glycerate">3-phospho-D-glycerate</a> to yield <a href="/wiki/Phosphohydroxypyruvic_acid" title="Phosphohydroxypyruvic acid">3-phosphonooxypyruvate</a>.<sup id="cite_ref-35" class="reference"><a href="#cite_note-35"><span class="cite-bracket">[</span>35<span class="cite-bracket">]</span></a></sup> The following reaction is catalyzed by the enzyme <a href="/wiki/Phosphoserine_aminotransferase" class="mw-redirect" title="Phosphoserine aminotransferase">phosphoserine aminotransferase</a>, which transfers an amino group from glutamate onto 3-phosphonooxypyruvate to yield <a href="/wiki/Phosphoserine" title="Phosphoserine">L-phosphoserine</a>.<sup id="cite_ref-36" class="reference"><a href="#cite_note-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup> The final step is catalyzed by the enzyme <a href="/wiki/Phosphoserine_phosphatase" title="Phosphoserine phosphatase">phosphoserine phosphatase</a>, which <a href="/wiki/Dephosphorylation" title="Dephosphorylation">dephosphorylates</a> L-phosphoserine to yield <a href="/wiki/L-serine" class="mw-redirect" title="L-serine">L-serine</a>.<sup id="cite_ref-37" class="reference"><a href="#cite_note-37"><span class="cite-bracket">[</span>37<span class="cite-bracket">]</span></a></sup> </p><p>There are two known pathways for the biosynthesis of glycine. Organisms that use <a href="/wiki/Ethanol" title="Ethanol">ethanol</a> and <a href="/wiki/Acetate" title="Acetate">acetate</a> as the major carbon source utilize the <a href="/wiki/Glyconeogenesis" title="Glyconeogenesis">glyconeogenic</a> pathway to synthesize <a href="/wiki/Glycine" title="Glycine">glycine</a>. The other pathway of glycine biosynthesis is known as the <a href="/wiki/Glycolytic" class="mw-redirect" title="Glycolytic">glycolytic</a> pathway. This pathway converts serine synthesized from the intermediates of <a href="/wiki/Glycolysis" title="Glycolysis">glycolysis</a> to glycine. In the glycolytic pathway, the enzyme <a href="/wiki/Serine_hydroxymethyltransferase" title="Serine hydroxymethyltransferase">serine hydroxymethyltransferase</a> catalyzes the cleavage of serine to yield glycine and transfers the cleaved carbon group of serine onto <a href="/wiki/Tetrahydrofolate" class="mw-redirect" title="Tetrahydrofolate">tetrahydrofolate</a>, forming <a href="/wiki/5,10-Methylenetetrahydrofolate" title="5,10-Methylenetetrahydrofolate">5,10-methylene-tetrahydrofolate</a>.<sup id="cite_ref-38" class="reference"><a href="#cite_note-38"><span class="cite-bracket">[</span>38<span class="cite-bracket">]</span></a></sup> </p><p>Cysteine biosynthesis is a two-step reaction that involves the incorporation of inorganic <a href="/wiki/Sulfur" title="Sulfur">sulfur</a>. In microorganisms and plants, the enzyme <a href="/wiki/Serine_O-acetyltransferase" title="Serine O-acetyltransferase">serine acetyltransferase</a> catalyzes the transfer of acetyl group from <a href="/wiki/Acetyl-CoA" title="Acetyl-CoA">acetyl-CoA</a> onto L-serine to yield <a href="/wiki/O-acetyl-L-serine" class="mw-redirect" title="O-acetyl-L-serine">O-acetyl-L-serine</a>.<sup id="cite_ref-39" class="reference"><a href="#cite_note-39"><span class="cite-bracket">[</span>39<span class="cite-bracket">]</span></a></sup> The following reaction step, catalyzed by the enzyme <a href="/wiki/Cysteine_synthase" title="Cysteine synthase">O-acetyl serine (thiol) lyase</a>, replaces the acetyl group of O-acetyl-L-serine with sulfide to yield cysteine.<sup id="cite_ref-40" class="reference"><a href="#cite_note-40"><span class="cite-bracket">[</span>40<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="The_aspartate_family_of_amino_acids">The aspartate family of amino acids</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=16" title="Edit section: The aspartate family of amino acids"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/wiki/Aspartate" class="mw-redirect" title="Aspartate">aspartate</a> family of amino acids includes: <a href="/wiki/Threonine" title="Threonine">threonine</a>, <a href="/wiki/Lysine" title="Lysine">lysine</a>, <a href="/wiki/Methionine" title="Methionine">methionine</a>, <a href="/wiki/Isoleucine" title="Isoleucine">isoleucine</a>, and aspartate. Lysine and isoleucine are considered part of the aspartate family even though part of their carbon skeleton is derived from <a href="/wiki/Pyruvate" class="mw-redirect" title="Pyruvate">pyruvate</a>. In the case of methionine, the methyl carbon is derived from serine and the sulfur group, but in most organisms, it is derived from cysteine.<sup id="cite_ref-Amino_Families_27-2" class="reference"><a href="#cite_note-Amino_Families-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup> </p><p> The biosynthesis of aspartate is a one step reaction that is catalyzed by a single enzyme. The enzyme <a href="/wiki/Aspartate_aminotransferase" class="mw-redirect" title="Aspartate aminotransferase">aspartate aminotransferase</a> catalyzes the transfer of an amino group from aspartate onto <a href="/wiki/%CE%91-ketoglutarate" class="mw-redirect" title="Α-ketoglutarate">α-ketoglutarate</a> to yield glutamate and <a href="/wiki/Oxaloacetate" class="mw-redirect" title="Oxaloacetate">oxaloacetate</a>.<sup id="cite_ref-41" class="reference"><a href="#cite_note-41"><span class="cite-bracket">[</span>41<span class="cite-bracket">]</span></a></sup> Asparagine is synthesized by an ATP-dependent addition of an amino group onto aspartate; <a href="/wiki/Asparagine_synthetase" title="Asparagine synthetase">asparagine synthetase</a> catalyzes the addition of nitrogen from glutamine or soluble ammonia to aspartate to yield asparagine.<sup id="cite_ref-42" class="reference"><a href="#cite_note-42"><span class="cite-bracket">[</span>42<span class="cite-bracket">]</span></a></sup> </p><figure typeof="mw:File/Thumb"><a href="/wiki/File:Lysine_Biosynthesis.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/c/cd/Lysine_Biosynthesis.png/400px-Lysine_Biosynthesis.png" decoding="async" width="400" height="383" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/c/cd/Lysine_Biosynthesis.png/600px-Lysine_Biosynthesis.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/c/cd/Lysine_Biosynthesis.png/800px-Lysine_Biosynthesis.png 2x" data-file-width="2227" data-file-height="2130" /></a><figcaption>The diaminopimelic acid lysine biosynthetic pathway</figcaption></figure> <p>The diaminopimelic acid biosynthetic pathway of lysine belongs to the aspartate family of amino acids. This pathway involves nine enzyme-catalyzed reactions that convert aspartate to lysine.<sup id="cite_ref-Lysine_pathways_43-0" class="reference"><a href="#cite_note-Lysine_pathways-43"><span class="cite-bracket">[</span>43<span class="cite-bracket">]</span></a></sup> </p> <ol><li><a href="/wiki/Aspartate_kinase" title="Aspartate kinase">Aspartate kinase</a> catalyzes the initial step in the diaminopimelic acid pathway by transferring a <a href="/wiki/Phosphoryl" class="mw-redirect" title="Phosphoryl">phosphoryl</a> from ATP onto the carboxylate group of aspartate, which yields aspartyl-β-phosphate.<sup id="cite_ref-44" class="reference"><a href="#cite_note-44"><span class="cite-bracket">[</span>44<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Aspartate-semialdehyde_dehydrogenase" title="Aspartate-semialdehyde dehydrogenase">Aspartate-semialdehyde dehydrogenase</a> catalyzes the reduction reaction by <a href="/wiki/Dephosphorylation" title="Dephosphorylation">dephosphorylation</a> of aspartyl-β-phosphate to yield aspartate-β-semialdehyde.<sup id="cite_ref-45" class="reference"><a href="#cite_note-45"><span class="cite-bracket">[</span>45<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/4-hydroxy-tetrahydrodipicolinate_synthase" class="mw-redirect" title="4-hydroxy-tetrahydrodipicolinate synthase">Dihydrodipicolinate synthase</a> catalyzes the <a href="/wiki/Condensation_reaction" title="Condensation reaction">condensation</a> reaction of aspartate-β-semialdehyde with pyruvate to yield dihydrodipicolinic acid.<sup id="cite_ref-46" class="reference"><a href="#cite_note-46"><span class="cite-bracket">[</span>46<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Dihydrodipicolinate_reductase" class="mw-redirect" title="Dihydrodipicolinate reductase">4-hydroxy-tetrahydrodipicolinate reductase</a> catalyzes the reduction of dihydrodipicolinic acid to yield tetrahydrodipicolinic acid.<sup id="cite_ref-47" class="reference"><a href="#cite_note-47"><span class="cite-bracket">[</span>47<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/2,3,4,5-tetrahydropyridine-2,6-dicarboxylate_N-succinyltransferase" title="2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase">Tetrahydrodipicolinate N-succinyltransferase</a> catalyzes the transfer of a succinyl group from succinyl-CoA on to tetrahydrodipicolinic acid to yield N-succinyl-L-2,6-diaminoheptanedioate.<sup id="cite_ref-48" class="reference"><a href="#cite_note-48"><span class="cite-bracket">[</span>48<span class="cite-bracket">]</span></a></sup></li> <li>N-succinyldiaminopimelate aminotransferase catalyzes the transfer of an amino group from glutamate onto N-succinyl-L-2,6-diaminoheptanedioate to yield N-succinyl-L,L-diaminopimelic acid.<sup id="cite_ref-49" class="reference"><a href="#cite_note-49"><span class="cite-bracket">[</span>49<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Succinyldiaminopimelate_transaminase" title="Succinyldiaminopimelate transaminase">Succinyl-diaminopimelate desuccinylase</a> catalyzes the removal of acyl group from N-succinyl-L,L-diaminopimelic acid to yield L,L-diaminopimelic acid.<sup id="cite_ref-50" class="reference"><a href="#cite_note-50"><span class="cite-bracket">[</span>50<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Diaminopimelate_epimerase" title="Diaminopimelate epimerase">Diaminopimelate epimerase</a> catalyzes the inversion of the α-carbon of L,L-diaminopimelic acid to yield <a href="/wiki/Meso-diaminopimelic_acid" class="mw-redirect" title="Meso-diaminopimelic acid">meso-diaminopimelic acid</a>.<sup id="cite_ref-51" class="reference"><a href="#cite_note-51"><span class="cite-bracket">[</span>51<span class="cite-bracket">]</span></a></sup></li> <li>Siaminopimelate decarboxylase catalyzes the final step in lysine biosynthesis that removes the carbon dioxide group from meso-diaminopimelic acid to yield L-lysine.<sup id="cite_ref-52" class="reference"><a href="#cite_note-52"><span class="cite-bracket">[</span>52<span class="cite-bracket">]</span></a></sup></li></ol> <div style="clear:both;" class=""></div> <div class="mw-heading mw-heading2"><h2 id="Proteins">Proteins</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=17" title="Edit section: Proteins"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-halign-right" typeof="mw:File/Frame"><a href="/wiki/File:Peptide_syn.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/4/42/Peptide_syn.svg/512px-Peptide_syn.svg.png" decoding="async" width="512" height="314" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/4/42/Peptide_syn.svg/768px-Peptide_syn.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/4/42/Peptide_syn.svg/1024px-Peptide_syn.svg.png 2x" data-file-width="512" data-file-height="314" /></a><figcaption>The tRNA anticodon interacts with the mRNA codon in order to bind an amino acid to growing polypeptide chain.</figcaption></figure><figure class="mw-halign-right" typeof="mw:File/Frame"><a href="/wiki/File:Charge_tRNA.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/3/3f/Charge_tRNA.png" decoding="async" width="720" height="459" class="mw-file-element" data-file-width="720" data-file-height="459" /></a><figcaption>The process of tRNA charging</figcaption></figure> <p>Protein synthesis occurs via a process called <a href="/wiki/Translation_(biology)" title="Translation (biology)">translation</a>.<sup id="cite_ref-Weaver_53-0" class="reference"><a href="#cite_note-Weaver-53"><span class="cite-bracket">[</span>53<span class="cite-bracket">]</span></a></sup> During translation, genetic material called <a href="/wiki/MRNA" class="mw-redirect" title="MRNA">mRNA</a> is read by <a href="/wiki/Ribosomes" class="mw-redirect" title="Ribosomes">ribosomes</a> to generate a protein <a href="/wiki/Polypeptide" class="mw-redirect" title="Polypeptide">polypeptide</a> chain.<sup id="cite_ref-Weaver_53-1" class="reference"><a href="#cite_note-Weaver-53"><span class="cite-bracket">[</span>53<span class="cite-bracket">]</span></a></sup> This process requires <a href="/wiki/TRNA" class="mw-redirect" title="TRNA">transfer RNA</a> (tRNA) which serves as an adaptor by binding <a href="/wiki/Amino_acids" class="mw-redirect" title="Amino acids">amino acids</a> on one end and interacting with mRNA at the other end; the latter pairing between the tRNA and mRNA ensures that the correct amino acid is added to the chain.<sup id="cite_ref-Weaver_53-2" class="reference"><a href="#cite_note-Weaver-53"><span class="cite-bracket">[</span>53<span class="cite-bracket">]</span></a></sup> Protein synthesis occurs in three phases: initiation, elongation, and termination.<sup id="cite_ref-Watson's_Molecular_Biology_of_the_Gene_13-2" class="reference"><a href="#cite_note-Watson's_Molecular_Biology_of_the_Gene-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup> Prokaryotic (<a href="/wiki/Archaeal_translation" title="Archaeal translation">archaeal</a> and <a href="/wiki/Bacterial_translation" title="Bacterial translation">bacterial</a>) translation differs from <a href="/wiki/Eukaryotic_translation" title="Eukaryotic translation">eukaryotic translation</a>; however, this section will mostly focus on the commonalities between the two organisms. </p> <div class="mw-heading mw-heading3"><h3 id="Additional_background">Additional background</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=18" title="Edit section: Additional background"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Before translation can begin, the process of binding a specific amino acid to its corresponding tRNA must occur. This reaction, called tRNA charging, is catalyzed by <a href="/wiki/Aminoacyl_tRNA_synthetase" title="Aminoacyl tRNA synthetase">aminoacyl tRNA synthetase</a>.<sup id="cite_ref-Copper_54-0" class="reference"><a href="#cite_note-Copper-54"><span class="cite-bracket">[</span>54<span class="cite-bracket">]</span></a></sup> A specific tRNA synthetase is responsible for recognizing and charging a particular amino acid.<sup id="cite_ref-Copper_54-1" class="reference"><a href="#cite_note-Copper-54"><span class="cite-bracket">[</span>54<span class="cite-bracket">]</span></a></sup> Furthermore, this enzyme has special discriminator regions to ensure the correct binding between tRNA and its cognate amino acid.<sup id="cite_ref-Copper_54-2" class="reference"><a href="#cite_note-Copper-54"><span class="cite-bracket">[</span>54<span class="cite-bracket">]</span></a></sup> The first step for joining an amino acid to its corresponding tRNA is the formation of aminoacyl-AMP:<sup id="cite_ref-Copper_54-3" class="reference"><a href="#cite_note-Copper-54"><span class="cite-bracket">[</span>54<span class="cite-bracket">]</span></a></sup> </p> <dl><dd><span class="mwe-math-element"><span class="mwe-math-mathml-inline mwe-math-mathml-a11y" style="display: none;"><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle {\ce {{Amino~acid}+ATP<=>{aminoacyl-AMP}+PP_{i}}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mtext>Amino</mtext> <mtext> </mtext> <mtext>acid</mtext> </mrow> <mo>+</mo> <mtext>ATP</mtext> <mrow class="MJX-TeXAtom-REL"> <mover> <mrow class="MJX-TeXAtom-OP MJX-fixedlimits"> <mrow class="MJX-TeXAtom-ORD"> <mpadded height="0" depth="0"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">↽</mo> </mrow> <mspace width="negativethinmathspace" /> <mspace width="negativethinmathspace" /> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> </mpadded> </mrow> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> <mspace width="negativethinmathspace" /> <mspace width="negativethinmathspace" /> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">⇀</mo> </mrow> </mrow> </mstyle> </mrow> </mover> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mtext>aminoacyl</mtext> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> <mtext>AMP</mtext> </mrow> <mo>+</mo> <msubsup> <mtext>PP</mtext> <mrow class="MJX-TeXAtom-ORD"> <mtext>i</mtext> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mspace width="0pt" height="0pt" depth=".2em" /> </mrow> </msubsup> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle {\ce {{Amino~acid}+ATP<=>{aminoacyl-AMP}+PP_{i}}}}</annotation> </semantics> </math></span><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/08bd22068b711a8005d83099789daafa59c93c41" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -1.005ex; width:48.218ex; height:3.343ex;" alt="{\displaystyle {\ce {{Amino~acid}+ATP<=>{aminoacyl-AMP}+PP_{i}}}}"></span></dd></dl> <p>This is followed by the transfer of the aminoacyl group from aminoacyl-AMP to a tRNA molecule. The resulting molecule is <a href="/wiki/Aminoacyl-tRNA" title="Aminoacyl-tRNA">aminoacyl-tRNA</a>:<sup id="cite_ref-Copper_54-4" class="reference"><a href="#cite_note-Copper-54"><span class="cite-bracket">[</span>54<span class="cite-bracket">]</span></a></sup> </p> <dl><dd><span class="mwe-math-element"><span class="mwe-math-mathml-inline mwe-math-mathml-a11y" style="display: none;"><math xmlns="http://www.w3.org/1998/Math/MathML" alttext="{\displaystyle {\ce {{Aminoacyl-AMP}+ tRNA <=> {aminoacyl-tRNA}+ AMP}}}"> <semantics> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="true" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mtext>Aminoacyl</mtext> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> <mtext>AMP</mtext> </mrow> <mo>+</mo> <mtext>tRNA</mtext> <mrow class="MJX-TeXAtom-REL"> <mover> <mrow class="MJX-TeXAtom-OP MJX-fixedlimits"> <mrow class="MJX-TeXAtom-ORD"> <mpadded height="0" depth="0"> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">↽</mo> </mrow> <mspace width="negativethinmathspace" /> <mspace width="negativethinmathspace" /> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> </mpadded> </mrow> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mstyle displaystyle="false" scriptlevel="0"> <mrow class="MJX-TeXAtom-ORD"> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> <mspace width="negativethinmathspace" /> <mspace width="negativethinmathspace" /> <mrow class="MJX-TeXAtom-ORD"> <mo stretchy="false">⇀</mo> </mrow> </mrow> </mstyle> </mrow> </mover> </mrow> <mrow class="MJX-TeXAtom-ORD"> <mtext>aminoacyl</mtext> <mrow class="MJX-TeXAtom-ORD"> <mo>−</mo> </mrow> <mtext>tRNA</mtext> </mrow> <mo>+</mo> <mtext>AMP</mtext> </mrow> </mstyle> </mrow> <annotation encoding="application/x-tex">{\displaystyle {\ce {{Aminoacyl-AMP}+ tRNA <=> {aminoacyl-tRNA}+ AMP}}}</annotation> </semantics> </math></span><img src="https://wikimedia.org/api/rest_v1/media/math/render/svg/7eba418c3ced70065d0034d0772664286e1b5d34" class="mwe-math-fallback-image-inline mw-invert skin-invert" aria-hidden="true" style="vertical-align: -0.671ex; width:58.181ex; height:3.009ex;" alt="{\displaystyle {\ce {{Aminoacyl-AMP}+ tRNA <=> {aminoacyl-tRNA}+ AMP}}}"></span></dd></dl> <p>The combination of these two steps, both of which are catalyzed by aminoacyl tRNA synthetase, produces a charged tRNA that is ready to add amino acids to the growing polypeptide chain. </p><p>In addition to binding an amino acid, tRNA has a three nucleotide unit called an <a href="/wiki/Anticodon#Anticodon" class="mw-redirect" title="Anticodon">anticodon</a> that <a href="/wiki/Base_pair" title="Base pair">base pairs</a> with specific nucleotide triplets on the mRNA called <a href="/wiki/Codons" class="mw-redirect" title="Codons">codons</a>; codons encode a specific amino acid.<sup id="cite_ref-Jackson_55-0" class="reference"><a href="#cite_note-Jackson-55"><span class="cite-bracket">[</span>55<span class="cite-bracket">]</span></a></sup> This interaction is possible thanks to the ribosome, which serves as the site for protein synthesis. The ribosome possesses three tRNA binding sites: the aminoacyl site (A site), the peptidyl site (P site), and the exit site (E site).<sup id="cite_ref-Green_56-0" class="reference"><a href="#cite_note-Green-56"><span class="cite-bracket">[</span>56<span class="cite-bracket">]</span></a></sup> </p><p>There are numerous codons within an mRNA transcript, and it is very common for an amino acid to be specified by more than one codon; this phenomenon is called <a href="/wiki/Codon_degeneracy" title="Codon degeneracy">degeneracy</a>.<sup id="cite_ref-Weissbach_57-0" class="reference"><a href="#cite_note-Weissbach-57"><span class="cite-bracket">[</span>57<span class="cite-bracket">]</span></a></sup> In all, there are 64 codons, 61 of each code for one of the 20 amino acids, while the remaining codons specify chain termination.<sup id="cite_ref-Weissbach_57-1" class="reference"><a href="#cite_note-Weissbach-57"><span class="cite-bracket">[</span>57<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Translation_in_steps">Translation in steps</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=19" title="Edit section: Translation in steps"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>As previously mentioned, translation occurs in three phases: initiation, elongation, and termination. </p> <figure class="mw-halign-left" typeof="mw:File/Frame"><a href="/wiki/File:TRNA_ribosomes_diagram_en.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/1/10/TRNA_ribosomes_diagram_en.svg/311px-TRNA_ribosomes_diagram_en.svg.png" decoding="async" width="311" height="500" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/1/10/TRNA_ribosomes_diagram_en.svg/467px-TRNA_ribosomes_diagram_en.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/1/10/TRNA_ribosomes_diagram_en.svg/622px-TRNA_ribosomes_diagram_en.svg.png 2x" data-file-width="311" data-file-height="500" /></a><figcaption>Translation</figcaption></figure> <div class="mw-heading mw-heading4"><h4 id="Step_1:_Initiation">Step 1: Initiation</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=20" title="Edit section: Step 1: Initiation"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The completion of the initiation phase is dependent on the following three events:<sup id="cite_ref-Watson's_Molecular_Biology_of_the_Gene_13-3" class="reference"><a href="#cite_note-Watson's_Molecular_Biology_of_the_Gene-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup> </p><p>1. The recruitment of the ribosome to mRNA </p><p>2. The binding of a charged initiator tRNA into the P site of the ribosome </p><p>3. The proper alignment of the ribosome with mRNA's start codon </p> <div class="mw-heading mw-heading4"><h4 id="Step_2:_Elongation">Step 2: Elongation</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=21" title="Edit section: Step 2: Elongation"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Following initiation, the polypeptide chain is extended via anticodon:codon interactions, with the ribosome adding amino acids to the polypeptide chain one at a time. The following steps must occur to ensure the correct addition of amino acids:<sup id="cite_ref-Frank_58-0" class="reference"><a href="#cite_note-Frank-58"><span class="cite-bracket">[</span>58<span class="cite-bracket">]</span></a></sup> </p><p>1. The binding of the correct tRNA into the A site of the ribosome </p><p>2. The formation of a <a href="/wiki/Peptide_bond" title="Peptide bond">peptide bond</a> between the tRNA in the A site and the polypeptide chain attached to the tRNA in the P site </p><p>3. <a href="/wiki/Protein_translocation#Protein_translocation" class="mw-redirect" title="Protein translocation">Translocation</a> or advancement of the tRNA-mRNA complex by three nucleotides </p><p>Translocation "kicks off" the tRNA at the E site and shifts the tRNA from the A site into the P site, leaving the A site free for an incoming tRNA to add another amino acid. </p> <div class="mw-heading mw-heading4"><h4 id="Step_3:_Termination">Step 3: Termination</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=22" title="Edit section: Step 3: Termination"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The last stage of translation occurs when a <a href="/wiki/Stop_codon" title="Stop codon">stop codon</a> enters the A site.<sup id="cite_ref-isbn0-8153-3218-1_1-2" class="reference"><a href="#cite_note-isbn0-8153-3218-1-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> Then, the following steps occur: </p><p>1. The recognition of codons by <a href="/wiki/Release_factor" title="Release factor">release factors</a>, which causes the <a href="/wiki/Hydrolysis" title="Hydrolysis">hydrolysis</a> of the polypeptide chain from the tRNA located in the P site<sup id="cite_ref-isbn0-8153-3218-1_1-3" class="reference"><a href="#cite_note-isbn0-8153-3218-1-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> </p><p>2. The release of the polypeptide chain<sup id="cite_ref-Weissbach_57-2" class="reference"><a href="#cite_note-Weissbach-57"><span class="cite-bracket">[</span>57<span class="cite-bracket">]</span></a></sup> </p><p>3. The dissociation and "recycling" of the ribosome for future translation processes<sup id="cite_ref-Weissbach_57-3" class="reference"><a href="#cite_note-Weissbach-57"><span class="cite-bracket">[</span>57<span class="cite-bracket">]</span></a></sup> </p><p>A summary table of the key players in translation is found below: </p> <table class="wikitable"> <caption> </caption> <tbody><tr> <th><b>Key players in Translation</b></th> <th><b>Translation Stage</b></th> <th><b>Purpose</b> </th></tr> <tr> <td align="">tRNA synthetase</td> <td>before initiation</td> <td>Responsible for tRNA charging </td></tr> <tr> <td align="">mRNA</td> <td>initiation, elongation, termination</td> <td>Template for protein synthesis; contains regions named codons which encode amino acids </td></tr> <tr> <td align="">tRNA</td> <td>initiation, elongation, termination</td> <td>Binds ribosomes sites A, P, E; anticodon base pairs with mRNA codon to ensure that the correct amino acid is incorporated into the growing polypeptide chain </td></tr> <tr> <td align="">ribosome</td> <td>initiation, elongation, termination</td> <td>Directs protein synthesis and catalyzes the formation of the peptide bond </td></tr> </tbody></table> <div style="clear:both;" class=""></div> <div class="mw-heading mw-heading2"><h2 id="Diseases_associated_with_macromolecule_deficiency">Diseases associated with macromolecule deficiency</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Biosynthesis&action=edit&section=23" title="Edit section: Diseases associated with macromolecule deficiency"><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:Xanthelasma_palpebrarum.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/e/e3/Xanthelasma_palpebrarum.jpg/180px-Xanthelasma_palpebrarum.jpg" decoding="async" width="180" height="120" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/e/e3/Xanthelasma_palpebrarum.jpg/270px-Xanthelasma_palpebrarum.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/e/e3/Xanthelasma_palpebrarum.jpg/360px-Xanthelasma_palpebrarum.jpg 2x" data-file-width="1200" data-file-height="799" /></a><figcaption>Familial hypercholesterolemia causes cholesterol deposits</figcaption></figure> <p>Errors in biosynthetic pathways can have deleterious consequences including the malformation of macromolecules or the underproduction of functional molecules. Below are examples that illustrate the disruptions that occur due to these inefficiencies. </p> <ul><li><a href="/wiki/Familial_hypercholesterolemia" title="Familial hypercholesterolemia">Familial hypercholesterolemia</a>: this disorder is characterized by the absence of functional <a href="/wiki/Receptor_(biochemistry)" title="Receptor (biochemistry)">receptors</a> for <a href="/wiki/LDL" class="mw-redirect" title="LDL">LDL</a>.<sup id="cite_ref-Bandeali-_Familial_hypercholesterolemia_59-0" class="reference"><a href="#cite_note-Bandeali-_Familial_hypercholesterolemia-59"><span class="cite-bracket">[</span>59<span class="cite-bracket">]</span></a></sup> Deficiencies in the formation of LDL receptors may cause faulty receptors which disrupt the <a href="/wiki/Endocytosis" title="Endocytosis">endocytic</a> pathway, inhibiting the entry of LDL into the liver and other cells.<sup id="cite_ref-Bandeali-_Familial_hypercholesterolemia_59-1" class="reference"><a href="#cite_note-Bandeali-_Familial_hypercholesterolemia-59"><span class="cite-bracket">[</span>59<span class="cite-bracket">]</span></a></sup> This causes a buildup of LDL in the blood plasma, which results in <a href="/wiki/Atherosclerotic_plaques" class="mw-redirect" title="Atherosclerotic plaques">atherosclerotic plaques</a> that narrow arteries and increase the risk of heart attacks.<sup id="cite_ref-Bandeali-_Familial_hypercholesterolemia_59-2" class="reference"><a href="#cite_note-Bandeali-_Familial_hypercholesterolemia-59"><span class="cite-bracket">[</span>59<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Lesch%E2%80%93Nyhan_syndrome" title="Lesch–Nyhan syndrome">Lesch–Nyhan syndrome</a>: this genetic disease is characterized by <a href="/wiki/Self_mutilation" class="mw-redirect" title="Self mutilation">self- mutilation</a>, mental deficiency, and <a href="/wiki/Gout" title="Gout">gout</a>.<sup id="cite_ref-Kang-_Lesch-Nyhan_syndrome_60-0" class="reference"><a href="#cite_note-Kang-_Lesch-Nyhan_syndrome-60"><span class="cite-bracket">[</span>60<span class="cite-bracket">]</span></a></sup> It is caused by the absence of <a href="/wiki/Hypoxanthine-guanine_phosphoribosyltransferase" title="Hypoxanthine-guanine phosphoribosyltransferase">hypoxanthine-guanine phosphoribosyltransferase</a>, which is a necessary enzyme for purine nucleotide formation.<sup id="cite_ref-Kang-_Lesch-Nyhan_syndrome_60-1" class="reference"><a href="#cite_note-Kang-_Lesch-Nyhan_syndrome-60"><span class="cite-bracket">[</span>60<span class="cite-bracket">]</span></a></sup> The lack of enzyme reduces the level of necessary nucleotides and causes the accumulation of biosynthesis <a href="/wiki/Reaction_intermediate" title="Reaction intermediate">intermediates</a>, which results in the aforementioned unusual behavior.<sup id="cite_ref-Kang-_Lesch-Nyhan_syndrome_60-2" class="reference"><a href="#cite_note-Kang-_Lesch-Nyhan_syndrome-60"><span class="cite-bracket">[</span>60<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Severe_combined_immunodeficiency" title="Severe combined immunodeficiency">Severe combined immunodeficiency (SCID)</a>: SCID is characterized by a loss of <a href="/wiki/T_cells" class="mw-redirect" title="T cells">T cells</a>.<sup id="cite_ref-Janeway's_Immunobiology_61-0" class="reference"><a href="#cite_note-Janeway's_Immunobiology-61"><span class="cite-bracket">[</span>61<span class="cite-bracket">]</span></a></sup> Shortage of these immune system components increases the susceptibility to infectious agents because the affected individuals cannot develop <a href="/wiki/Immunological_memory" title="Immunological memory">immunological memory</a>.<sup id="cite_ref-Janeway's_Immunobiology_61-1" class="reference"><a href="#cite_note-Janeway's_Immunobiology-61"><span class="cite-bracket">[</span>61<span class="cite-bracket">]</span></a></sup> This immunological disorder results from a deficiency in <a href="/wiki/Adenosine_deaminase" title="Adenosine deaminase">adenosine deaminase</a> activity, which causes a buildup of <a href="/wiki/DATP" class="mw-redirect" title="DATP">dATP</a>. These dATP molecules then inhibit ribonucleotide reductase, which prevents of DNA synthesis.<sup id="cite_ref-Janeway's_Immunobiology_61-2" class="reference"><a href="#cite_note-Janeway's_Immunobiology-61"><span class="cite-bracket">[</span>61<span class="cite-bracket">]</span></a></sup></li> <li><a href="/wiki/Huntington%27s_disease" title="Huntington's disease">Huntington's disease</a>: this <a href="/wiki/Neurological" class="mw-redirect" title="Neurological">neurological</a> disease is caused from errors that occur during DNA synthesis.<sup id="cite_ref-Hughes_Huntington's_62-0" class="reference"><a href="#cite_note-Hughes_Huntington's-62"><span class="cite-bracket">[</span>62<span class="cite-bracket">]</span></a></sup> These errors or mutations lead to the expression of a mutant <a href="/wiki/Huntingtin" title="Huntingtin">huntingtin</a> protein, which contains repetitive <a href="/wiki/Glutamine" title="Glutamine">glutamine</a> residues that are encoded by expanding <a href="/wiki/Trinucleotide_repeat#CAG_Repeats" class="mw-redirect" title="Trinucleotide repeat">CAG trinucleotide repeats</a> in the gene.<sup id="cite_ref-Hughes_Huntington's_62-1" class="reference"><a href="#cite_note-Hughes_Huntington's-62"><span class="cite-bracket">[</span>62<span class="cite-bracket">]</span></a></sup> Huntington's disease is characterized by neuronal loss and <a href="/wiki/Gliosis" title="Gliosis">gliosis</a>. Symptoms of the disease include: movement disorder, <a href="/wiki/Cognitive" class="mw-redirect" title="Cognitive">cognitive</a> decline, and behavioral disorder.<sup id="cite_ref-Biglan-_Huntington's_63-0" class="reference"><a href="#cite_note-Biglan-_Huntington's-63"><span class="cite-bracket">[</span>63<span class="cite-bracket">]</span></a></sup></li></ul> <div style="clear:both;" class=""></div> <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=Biosynthesis&action=edit&section=24" 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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class="mw-redirect" title="Codon table">Codon table</a></li> <li><a href="/wiki/Prostaglandin" title="Prostaglandin">Prostaglandin</a></li> <li><a href="/wiki/Porphyrin#Synthesis" title="Porphyrin">Porphyrins</a></li> <li><a href="/wiki/Chlorophyllide" title="Chlorophyllide">Chlorophylls and bacteriochlorophylls</a></li> <li><a href="/wiki/Biosynthesis_of_cobalamin" class="mw-redirect" title="Biosynthesis of cobalamin">Vitamin B<sub>12</sub></a></li></ul> <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=Biosynthesis&action=edit&section=25" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}</style><div class="reflist"> <div class="mw-references-wrap mw-references-columns"><ol class="references"> <li id="cite_note-isbn0-8153-3218-1-1"><span class="mw-cite-backlink">^ <a href="#cite_ref-isbn0-8153-3218-1_1-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-isbn0-8153-3218-1_1-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-isbn0-8153-3218-1_1-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-isbn0-8153-3218-1_1-3"><sup><i><b>d</b></i></sup></a></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="CITEREFAlberts,_Bruce2008" class="citation book cs1">Alberts, Bruce (2008). <i>Molecular Biology of the Cell</i> (5th ed.). New York: Garland Science. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0815341055" title="Special:BookSources/978-0815341055"><bdi>978-0815341055</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Molecular+Biology+of+the+Cell&rft.place=New+York&rft.edition=5th&rft.pub=Garland+Science&rft.date=2008&rft.isbn=978-0815341055&rft.au=Alberts%2C+Bruce&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span></span> </li> <li id="cite_note-Zumdahl-2"><span class="mw-cite-backlink"><b><a href="#cite_ref-Zumdahl_2-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFZumdahl2008" class="citation book cs1">Zumdahl, Steven S. Zumdahl, Susan A. (2008). <i>Chemistry</i> (8th ed.). CA: Cengage Learning. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0547125329" title="Special:BookSources/978-0547125329"><bdi>978-0547125329</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Chemistry&rft.place=CA&rft.edition=8th&rft.pub=Cengage+Learning&rft.date=2008&rft.isbn=978-0547125329&rft.aulast=Zumdahl&rft.aufirst=Steven+S.+Zumdahl%2C+Susan+A.&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span><span class="cs1-maint citation-comment"><code class="cs1-code">{{<a href="/wiki/Template:Cite_book" title="Template:Cite book">cite book</a>}}</code>: CS1 maint: multiple names: authors list (<a href="/wiki/Category:CS1_maint:_multiple_names:_authors_list" title="Category:CS1 maint: multiple names: authors list">link</a>)</span></span> </li> <li id="cite_note-Voet-3"><span class="mw-cite-backlink"><b><a href="#cite_ref-Voet_3-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFVoetVoetPratt2013" class="citation book cs1">Voet, Donald; Voet, Judith G.; Pratt, Charlotte W. (2013). <i>Fundamentals of Biochemistry: Life at the Molecular Level</i> (4th ed.). Hoboken, NJ: Wiley. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0470547847" title="Special:BookSources/978-0470547847"><bdi>978-0470547847</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Fundamentals+of+Biochemistry%3A+Life+at+the+Molecular+Level&rft.place=Hoboken%2C+NJ&rft.edition=4th&rft.pub=Wiley&rft.date=2013&rft.isbn=978-0470547847&rft.aulast=Voet&rft.aufirst=Donald&rft.au=Voet%2C+Judith+G.&rft.au=Pratt%2C+Charlotte+W.&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span></span> </li> <li id="cite_note-Molecular_Cell_Biology-4"><span class="mw-cite-backlink">^ <a href="#cite_ref-Molecular_Cell_Biology_4-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Molecular_Cell_Biology_4-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Molecular_Cell_Biology_4-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Molecular_Cell_Biology_4-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Molecular_Cell_Biology_4-4"><sup><i><b>e</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFLodish2007" class="citation book cs1">Lodish, Harvey; et al. (2007). <a rel="nofollow" class="external text" href="https://archive.org/details/molecularcellbio00harv"><i>Molecular cell biology</i></a> (6th ed.). New York: W.H. Freeman. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0716743668" title="Special:BookSources/978-0716743668"><bdi>978-0716743668</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Molecular+cell+biology&rft.place=New+York&rft.edition=6th&rft.pub=W.H.+Freeman&rft.date=2007&rft.isbn=978-0716743668&rft.aulast=Lodish&rft.aufirst=Harvey&rft_id=https%3A%2F%2Farchive.org%2Fdetails%2Fmolecularcellbio00harv&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span></span> </li> <li id="cite_note-Lehninger-5"><span class="mw-cite-backlink">^ <a href="#cite_ref-Lehninger_5-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Lehninger_5-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Lehninger_5-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Lehninger_5-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Lehninger_5-4"><sup><i><b>e</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFCox2008" class="citation book cs1">Cox, David L. Nelson, Michael M. (2008). <a rel="nofollow" class="external text" href="https://archive.org/details/lehningerprincip00lehn_1"><i>Lehninger principles of biochemistry</i></a> (5th ed.). New York: W.H. Freeman. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/9780716771081" title="Special:BookSources/9780716771081"><bdi>9780716771081</bdi></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.place=New+York&rft.edition=5th&rft.pub=W.H.+Freeman&rft.date=2008&rft.isbn=9780716771081&rft.aulast=Cox&rft.aufirst=David+L.+Nelson%2C+Michael+M.&rft_id=https%3A%2F%2Farchive.org%2Fdetails%2Flehningerprincip00lehn_1&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span><span class="cs1-maint citation-comment"><code class="cs1-code">{{<a href="/wiki/Template:Cite_book" title="Template:Cite book">cite book</a>}}</code>: CS1 maint: multiple names: authors list (<a href="/wiki/Category:CS1_maint:_multiple_names:_authors_list" title="Category:CS1 maint: multiple names: authors list">link</a>)</span></span> </li> <li id="cite_note-Hanin-6"><span class="mw-cite-backlink"><b><a href="#cite_ref-Hanin_6-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFHanin2013" class="citation book cs1">Hanin, Israel (2013). <i>Phospholipids: Biochemical, Pharmaceutical, and Analytical Considerations</i>. Springer. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-1475713664" title="Special:BookSources/978-1475713664"><bdi>978-1475713664</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Phospholipids%3A+Biochemical%2C+Pharmaceutical%2C+and+Analytical+Considerations&rft.pub=Springer&rft.date=2013&rft.isbn=978-1475713664&rft.aulast=Hanin&rft.aufirst=Israel&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span></span> </li> <li id="cite_note-Vance-7"><span class="mw-cite-backlink">^ <a href="#cite_ref-Vance_7-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Vance_7-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Vance_7-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Vance_7-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Vance_7-4"><sup><i><b>e</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFVanceVance,_Jean_E.2008" class="citation book cs1">Vance, Dennis E.; Vance, Jean E. (2008). <i>Biochemistry of lipids, lipoproteins and membranes</i> (5th ed.). Amsterdam: Elsevier. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0444532190" title="Special:BookSources/978-0444532190"><bdi>978-0444532190</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Biochemistry+of+lipids%2C+lipoproteins+and+membranes&rft.place=Amsterdam&rft.edition=5th&rft.pub=Elsevier&rft.date=2008&rft.isbn=978-0444532190&rft.aulast=Vance&rft.aufirst=Dennis+E.&rft.au=Vance%2C+Jean+E.&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span></span> </li> <li id="cite_note-Katsaras-8"><span class="mw-cite-backlink"><b><a href="#cite_ref-Katsaras_8-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFKatsaras2001" class="citation book cs1">Katsaras, J.; et al. 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Berlin [u.a.]: Springer. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-3540675556" title="Special:BookSources/978-3540675556"><bdi>978-3540675556</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Lipid+bilayers+%3A+structure+and+interactions+%3B+with+6+tables&rft.place=Berlin+%5Bu.a.%5D&rft.pub=Springer&rft.date=2001&rft.isbn=978-3540675556&rft.aulast=Katsaras&rft.aufirst=J.&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span></span> </li> <li id="cite_note-Stryer-9"><span class="mw-cite-backlink">^ <a href="#cite_ref-Stryer_9-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Stryer_9-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Stryer_9-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Stryer_9-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Stryer_9-4"><sup><i><b>e</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFStryer2007" class="citation book cs1">Stryer, Jeremy M. Berg; John L. Tymoczko; Lubert (2007). <i>Biochemistry</i> (6. ed., 3. print. ed.). New York: Freeman. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0716787242" title="Special:BookSources/978-0716787242"><bdi>978-0716787242</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Biochemistry&rft.place=New+York&rft.edition=6.+ed.%2C+3.+print.&rft.pub=Freeman&rft.date=2007&rft.isbn=978-0716787242&rft.aulast=Stryer&rft.aufirst=Jeremy+M.+Berg%3B+John+L.+Tymoczko%3B+Lubert&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span><span class="cs1-maint citation-comment"><code class="cs1-code">{{<a href="/wiki/Template:Cite_book" title="Template:Cite book">cite book</a>}}</code>: CS1 maint: multiple names: authors list (<a href="/wiki/Category:CS1_maint:_multiple_names:_authors_list" title="Category:CS1 maint: multiple names: authors list">link</a>)</span></span> </li> <li id="cite_note-10"><span class="mw-cite-backlink"><b><a href="#cite_ref-10">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFGaultLM_ObeidYA_Hannun2010" class="citation book cs1">Gault, CR; LM Obeid; YA Hannun (2010). "An Overview of Sphingolipid Metabolism: From Synthesis to Breakdown". <i>Sphingolipids as Signaling and Regulatory Molecules</i>. Advances in Experimental Medicine and Biology. Vol. 688. pp. 1–23. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1007%2F978-1-4419-6741-1_1">10.1007/978-1-4419-6741-1_1</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-1-4419-6740-4" title="Special:BookSources/978-1-4419-6740-4"><bdi>978-1-4419-6740-4</bdi></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/PMC3069696">3069696</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/20919643">20919643</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=An+Overview+of+Sphingolipid+Metabolism%3A+From+Synthesis+to+Breakdown&rft.btitle=Sphingolipids+as+Signaling+and+Regulatory+Molecules&rft.series=Advances+in+Experimental+Medicine+and+Biology&rft.pages=1-23&rft.date=2010&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3069696%23id-name%3DPMC&rft_id=info%3Apmid%2F20919643&rft_id=info%3Adoi%2F10.1007%2F978-1-4419-6741-1_1&rft.isbn=978-1-4419-6740-4&rft.aulast=Gault&rft.aufirst=CR&rft.au=LM+Obeid&rft.au=YA+Hannun&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span></span> </li> <li id="cite_note-Siegel-11"><span class="mw-cite-backlink">^ <a href="#cite_ref-Siegel_11-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Siegel_11-1"><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="CITEREFSiegel1999" class="citation book cs1">Siegel, George J. (1999). <i>Basic neurochemistry : molecular, cellular and medical aspects</i> (6. ed.). Philadelphia, Pa. [u.a.]: Lippincott Williams & Wilkins. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0397518203" title="Special:BookSources/978-0397518203"><bdi>978-0397518203</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Basic+neurochemistry+%3A+molecular%2C+cellular+and+medical+aspects&rft.place=Philadelphia%2C+Pa.+%5Bu.a.%5D&rft.edition=6.&rft.pub=Lippincott+Williams+%26+Wilkins&rft.date=1999&rft.isbn=978-0397518203&rft.aulast=Siegel&rft.aufirst=George+J.&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span></span> </li> <li id="cite_note-Harris-12"><span class="mw-cite-backlink">^ <a href="#cite_ref-Harris_12-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Harris_12-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Harris_12-2"><sup><i><b>c</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFHarris2010" class="citation book cs1">Harris, J. Robin (2010). <i>Cholesterol binding and cholesterol transport proteins : structure and function in health and disease</i>. Dordrecht: Springer. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-9048186211" title="Special:BookSources/978-9048186211"><bdi>978-9048186211</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Cholesterol+binding+and+cholesterol+transport+proteins+%3A+structure+and+function+in+health+and+disease&rft.place=Dordrecht&rft.pub=Springer&rft.date=2010&rft.isbn=978-9048186211&rft.aulast=Harris&rft.aufirst=J.+Robin&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span></span> </li> <li id="cite_note-Watson's_Molecular_Biology_of_the_Gene-13"><span class="mw-cite-backlink">^ <a href="#cite_ref-Watson's_Molecular_Biology_of_the_Gene_13-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Watson's_Molecular_Biology_of_the_Gene_13-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Watson's_Molecular_Biology_of_the_Gene_13-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Watson's_Molecular_Biology_of_the_Gene_13-3"><sup><i><b>d</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFWatson2007" class="citation book cs1">Watson, James D.; et al. 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"Modular evolution of the purine biosynthetic pathway". <i>Current Opinion in Chemical Biology</i>. <b>4</b> (5): 567–72. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fs1367-5931%2800%2900133-2">10.1016/s1367-5931(00)00133-2</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/11006546">11006546</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Opinion+in+Chemical+Biology&rft.atitle=Modular+evolution+of+the+purine+biosynthetic+pathway.&rft.volume=4&rft.issue=5&rft.pages=567-72&rft.date=2000-10&rft_id=info%3Adoi%2F10.1016%2Fs1367-5931%2800%2900133-2&rft_id=info%3Apmid%2F11006546&rft.aulast=Kappock&rft.aufirst=TJ&rft.au=Ealick%2C+SE&rft.au=Stubbe%2C+J&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span></span> </li> <li id="cite_note-15"><span class="mw-cite-backlink"><b><a href="#cite_ref-15">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFSampeiBaba,_SKanagawa,_MYanai,_H2010" class="citation journal cs1">Sampei, G; Baba, S; Kanagawa, M; Yanai, H; Ishii, T; Kawai, H; Fukai, Y; Ebihara, A; Nakagawa, N; Kawai, G (October 2010). "Crystal structures of glycinamide ribonucleotide synthetase, PurD, from thermophilic eubacteria". <i>Journal of Biochemistry</i>. <b>148</b> (4): 429–38. <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%2Fjb%2Fmvq088">10.1093/jb/mvq088</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/20716513">20716513</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Biochemistry&rft.atitle=Crystal+structures+of+glycinamide+ribonucleotide+synthetase%2C+PurD%2C+from+thermophilic+eubacteria.&rft.volume=148&rft.issue=4&rft.pages=429-38&rft.date=2010-10&rft_id=info%3Adoi%2F10.1093%2Fjb%2Fmvq088&rft_id=info%3Apmid%2F20716513&rft.aulast=Sampei&rft.aufirst=G&rft.au=Baba%2C+S&rft.au=Kanagawa%2C+M&rft.au=Yanai%2C+H&rft.au=Ishii%2C+T&rft.au=Kawai%2C+H&rft.au=Fukai%2C+Y&rft.au=Ebihara%2C+A&rft.au=Nakagawa%2C+N&rft.au=Kawai%2C+G&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span></span> </li> <li id="cite_note-16"><span class="mw-cite-backlink"><b><a href="#cite_ref-16">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFHoskinsAnand,_REalick,_SEStubbe,_J2004" class="citation journal cs1">Hoskins, AA; Anand, R; Ealick, SE; Stubbe, J (Aug 17, 2004). 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New York: Freeman. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0716731184" title="Special:BookSources/978-0716731184"><bdi>978-0716731184</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Modern+genetic+analysis&rft.place=New+York&rft.edition=2.+print.&rft.pub=Freeman&rft.date=1999&rft.isbn=978-0716731184&rft.aulast=Griffiths&rft.aufirst=Anthony+J.+F.&rft_id=https%3A%2F%2Farchive.org%2Fdetails%2Fmoderngeneticana0000unse&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span></span> </li> <li id="cite_note-AA_structure-24"><span class="mw-cite-backlink">^ <a href="#cite_ref-AA_structure_24-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-AA_structure_24-1"><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="CITEREFWu2009" class="citation journal cs1">Wu, G (May 2009). 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title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Movement+Disorders&rft.atitle=Motor+abnormalities+in+premanifest+persons+with+Huntington%27s+disease%3A+The+PREDICT-HD+study&rft.volume=24&rft.issue=12&rft.pages=1763-1772&rft.date=2009-06-26&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3048804%23id-name%3DPMC&rft_id=info%3Apmid%2F19562761&rft_id=info%3Adoi%2F10.1002%2Fmds.22601&rft.aulast=Biglan&rft.aufirst=Kevin+M.&rft.au=Ross%2C+Christopher+A.&rft.au=Langbehn%2C+Douglas+R.&rft.au=Aylward%2C+Elizabeth+H.&rft.au=Stout%2C+Julie+C.&rft.au=Queller%2C+Sarah&rft.au=Carlozzi%2C+Noelle+E.&rft.au=Duff%2C+Kevin&rft.au=Beglinger%2C+Leigh+J.&rft.au=Paulsen%2C+Jane+S.&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3048804&rfr_id=info%3Asid%2Fen.wikipedia.org%3ABiosynthesis" class="Z3988"></span></span> </li> </ol></div></div> <div class="navbox-styles"><style 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class="navbox-group" style="width:1%">Types</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/Artificial_gene_synthesis" title="Artificial gene synthesis">Artificial gene synthesis</a></li> <li><a href="/wiki/Biomimetic_synthesis" title="Biomimetic synthesis">Biomimetic synthesis</a></li> <li><a href="/wiki/Bioretrosynthesis" title="Bioretrosynthesis">Bioretrosynthesis</a></li> <li><a class="mw-selflink selflink">Biosynthesis</a></li> <li><a href="/wiki/Chemosynthesis_(nanotechnology)" title="Chemosynthesis (nanotechnology)">Chemosynthesis</a></li> <li><a href="/wiki/Convergent_synthesis" title="Convergent synthesis">Convergent synthesis</a></li> <li><a href="/wiki/Custom_peptide_synthesis" title="Custom peptide synthesis">Custom peptide synthesis</a></li> <li><a href="/wiki/Direct_process" title="Direct process">Direct process</a></li> <li><a href="/wiki/Divergent_synthesis" title="Divergent synthesis">Divergent synthesis</a></li> <li><a href="/wiki/Electrosynthesis" title="Electrosynthesis">Electrosynthesis</a></li> <li><a href="/wiki/Enantioselective_synthesis" title="Enantioselective synthesis">Enantioselective synthesis</a></li> <li><a href="/wiki/Fully_automated_synthesis" class="mw-redirect" title="Fully automated synthesis">Fully automated synthesis</a></li> <li><a href="/wiki/Hydrothermal_synthesis" title="Hydrothermal synthesis">Hydrothermal synthesis</a></li> <li><a href="/wiki/Laser_ablation_synthesis_in_solution" title="Laser ablation synthesis in solution">LASiS</a></li> <li><a href="/wiki/Mechanosynthesis" title="Mechanosynthesis">Mechanosynthesis</a></li> <li><a href="/wiki/One-pot_synthesis" title="One-pot synthesis">One-pot synthesis</a></li> <li><a href="/wiki/Organic_synthesis" title="Organic synthesis">Organic synthesis</a></li> <li><a href="/wiki/Peptide_synthesis" title="Peptide synthesis">Peptide synthesis</a></li> <li><a href="/wiki/Radiosynthesis" title="Radiosynthesis">Radiosynthesis</a></li> <li><a href="/wiki/Retrosynthetic_analysis" title="Retrosynthetic analysis">Retrosynthesis</a></li> <li><a href="/wiki/Semisynthesis" title="Semisynthesis">Semisynthesis</a></li> <li><a href="/wiki/Solid-phase_synthesis" title="Solid-phase synthesis">Solid-phase synthesis</a></li> <li><a href="/wiki/Solvothermal_synthesis" title="Solvothermal synthesis">Solvothermal synthesis</a></li> <li><a href="/wiki/Total_synthesis" title="Total synthesis">Total synthesis</a></li> <li><a href="/wiki/Volume_combustion_synthesis" title="Volume combustion synthesis">Volume combustion synthesis</a></li></ul> </div></td></tr><tr><td class="navbox-abovebelow" colspan="2"><div> <ul><li><span class="noviewer" typeof="mw:File"><span title="Category"><img alt="" src="//upload.wikimedia.org/wikipedia/en/thumb/9/96/Symbol_category_class.svg/16px-Symbol_category_class.svg.png" decoding="async" width="16" height="16" class="mw-file-element" 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title="commons:Category:Chemical synthesis">Commons</a></b></li> <li><span class="noviewer" typeof="mw:File"><a href="/wiki/File:Symbol_portal_class.svg" class="mw-file-description" title="Portal"><img alt="" src="//upload.wikimedia.org/wikipedia/en/thumb/e/e2/Symbol_portal_class.svg/16px-Symbol_portal_class.svg.png" decoding="async" width="16" height="16" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/e/e2/Symbol_portal_class.svg/23px-Symbol_portal_class.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/e/e2/Symbol_portal_class.svg/31px-Symbol_portal_class.svg.png 2x" data-file-width="180" data-file-height="185" /></a></span><b><a href="/wiki/Portal:Chemistry" title="Portal:Chemistry">Portal</a></b></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="Branches_of_chemistry" 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"><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:Branches_of_chemistry" title="Template:Branches of chemistry"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Branches_of_chemistry" title="Template talk:Branches of chemistry"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Branches_of_chemistry" title="Special:EditPage/Template:Branches of chemistry"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Branches_of_chemistry" style="font-size:114%;margin:0 4em">Branches of <a href="/wiki/Chemistry" title="Chemistry">chemistry</a></div></th></tr><tr><td class="navbox-abovebelow" colspan="2"><div> <ul><li><a href="/wiki/Glossary_of_chemical_formulae" title="Glossary of chemical formulae">Glossary of chemical formulae</a></li> <li><a href="/wiki/List_of_biomolecules" title="List of biomolecules">List of biomolecules</a></li> <li><a href="/wiki/List_of_inorganic_compounds" title="List of inorganic compounds">List of inorganic compounds</a></li> <li><a href="/wiki/Periodic_table" title="Periodic table">Periodic table</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Analytical_chemistry" title="Analytical chemistry">Analytical</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/Instrumental_chemistry" title="Instrumental chemistry">Instrumental chemistry</a></li> <li><a href="/wiki/Electroanalytical_methods" title="Electroanalytical methods">Electroanalytical methods</a></li> <li><a href="/wiki/Spectroscopy" title="Spectroscopy">Spectroscopy</a> <ul><li><a href="/wiki/Infrared_spectroscopy" title="Infrared spectroscopy">IR</a></li> <li><a href="/wiki/Raman_spectroscopy" title="Raman spectroscopy">Raman</a></li> <li><a href="/wiki/Ultraviolet%E2%80%93visible_spectroscopy" title="Ultraviolet–visible spectroscopy">UV-Vis</a></li> <li><a href="/wiki/Nuclear_magnetic_resonance_spectroscopy" title="Nuclear magnetic resonance spectroscopy">NMR</a></li></ul></li> <li><a href="/wiki/Mass_spectrometry" title="Mass spectrometry">Mass spectrometry</a> <ul><li><a href="/wiki/Electron_ionization" title="Electron ionization">EI</a></li> <li><a href="/wiki/Inductively_coupled_plasma_mass_spectrometry" title="Inductively coupled plasma mass spectrometry">ICP</a></li> <li><a href="/wiki/Matrix-assisted_laser_desorption/ionization" title="Matrix-assisted laser desorption/ionization">MALDI</a></li></ul></li> <li><a href="/wiki/Separation_process" title="Separation process">Separation process</a></li> <li><a href="/wiki/Chromatography" title="Chromatography">Chromatography</a> <ul><li><a href="/wiki/Gas_chromatography" title="Gas chromatography">GC</a></li> <li><a href="/wiki/High-performance_liquid_chromatography" title="High-performance liquid chromatography">HPLC</a></li></ul></li> <li><a href="/wiki/Crystallography" title="Crystallography">Crystallography</a></li> <li><a href="/wiki/Characterization_(materials_science)" title="Characterization (materials science)">Characterization</a></li> <li><a href="/wiki/Titration" title="Titration">Titration</a></li> <li><a href="/wiki/Wet_chemistry" title="Wet chemistry">Wet chemistry</a></li> <li><a href="/wiki/Calorimetry" title="Calorimetry">Calorimetry</a></li> <li><a href="/wiki/Elemental_analysis" title="Elemental analysis">Elemental analysis</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Theoretical_chemistry" title="Theoretical chemistry">Theoretical</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/Quantum_chemistry" title="Quantum chemistry">Quantum chemistry</a></li> <li><a href="/wiki/Computational_chemistry" title="Computational chemistry">Computational chemistry</a> <ul><li><a href="/wiki/Mathematical_chemistry" title="Mathematical chemistry">Mathematical chemistry</a></li></ul></li> <li><a href="/wiki/Molecular_modelling" title="Molecular modelling">Molecular modelling</a></li> <li><a href="/wiki/Molecular_mechanics" title="Molecular mechanics">Molecular mechanics</a></li> <li><a href="/wiki/Molecular_dynamics" title="Molecular dynamics">Molecular dynamics</a></li> <li><a href="/wiki/Molecular_geometry" title="Molecular geometry">Molecular geometry</a> <ul><li><a href="/wiki/VSEPR_theory" title="VSEPR theory">VSEPR theory</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Physical_chemistry" title="Physical chemistry">Physical</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/Electrochemistry" title="Electrochemistry">Electrochemistry</a> <ul><li><a href="/wiki/Spectroelectrochemistry" title="Spectroelectrochemistry">Spectroelectrochemistry</a></li> <li><a href="/wiki/Photoelectrochemistry" title="Photoelectrochemistry">Photoelectrochemistry</a></li></ul></li> <li><a href="/wiki/Thermochemistry" title="Thermochemistry">Thermochemistry</a></li> <li><a href="/wiki/Chemical_thermodynamics" title="Chemical thermodynamics">Chemical thermodynamics</a></li> <li><a href="/wiki/Surface_science" title="Surface science">Surface science</a></li> <li><a href="/wiki/Interface_and_colloid_science" title="Interface and colloid science">Interface and colloid science</a> <ul><li><a href="/wiki/Micromeritics" title="Micromeritics">Micromeritics</a></li></ul></li> <li><a href="/wiki/Cryochemistry" title="Cryochemistry">Cryochemistry</a></li> <li><a href="/wiki/Sonochemistry" title="Sonochemistry">Sonochemistry</a></li> <li><a href="/wiki/Structural_chemistry" title="Structural chemistry">Structural chemistry</a></li> <li><a href="/wiki/Chemical_physics" title="Chemical physics">Chemical physics</a> <ul><li><a href="/wiki/Molecular_physics" title="Molecular physics">Molecular physics</a></li></ul></li> <li><a href="/wiki/Femtochemistry" title="Femtochemistry">Femtochemistry</a></li> <li><a href="/wiki/Chemical_kinetics" title="Chemical kinetics">Chemical kinetics</a></li> <li><a href="/wiki/Spectroscopy" title="Spectroscopy">Spectroscopy</a></li> <li><a href="/wiki/Photochemistry" title="Photochemistry">Photochemistry</a></li> <li><a href="/wiki/Spin_chemistry" title="Spin chemistry">Spin chemistry</a></li> <li><a href="/wiki/Microwave_chemistry" title="Microwave chemistry">Microwave chemistry</a></li> <li><a href="/wiki/Equilibrium_chemistry" title="Equilibrium chemistry">Equilibrium chemistry</a></li> <li><a href="/wiki/Mechanochemistry" title="Mechanochemistry">Mechanochemistry</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Inorganic_chemistry" title="Inorganic chemistry">Inorganic</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/Coordination_complex" title="Coordination complex">Coordination chemistry</a></li> <li><a href="/wiki/Magnetochemistry" title="Magnetochemistry">Magnetochemistry</a></li> <li><a href="/wiki/Organometallic_chemistry" title="Organometallic chemistry">Organometallic chemistry</a> <ul><li><a href="/wiki/Organolanthanide_chemistry" title="Organolanthanide chemistry">Organolanthanide chemistry</a></li></ul></li> <li><a href="/wiki/Atom_cluster" class="mw-redirect" title="Atom cluster">Cluster chemistry</a></li> <li><a href="/wiki/Solid-state_chemistry" title="Solid-state chemistry">Solid-state chemistry</a></li> <li><a href="/wiki/Ceramic_chemistry" class="mw-redirect" title="Ceramic chemistry">Ceramic chemistry</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Organic_chemistry" title="Organic chemistry">Organic</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/Stereochemistry" title="Stereochemistry">Stereochemistry</a> <ul><li><a href="/wiki/Alkane_stereochemistry" class="mw-redirect" title="Alkane stereochemistry">Alkane stereochemistry</a></li></ul></li> <li><a href="/wiki/Physical_organic_chemistry" title="Physical organic chemistry">Physical organic chemistry</a></li> <li><a href="/wiki/Organic_reactions" class="mw-redirect" title="Organic reactions">Organic reactions</a></li> <li><a href="/wiki/Organic_synthesis" title="Organic synthesis">Organic synthesis</a></li> <li><a href="/wiki/Retrosynthetic_analysis" title="Retrosynthetic analysis">Retrosynthetic analysis</a></li> <li><a href="/wiki/Enantioselective_synthesis" title="Enantioselective synthesis">Enantioselective synthesis</a></li> <li><a href="/wiki/Total_synthesis" title="Total synthesis">Total synthesis</a> / <a href="/wiki/Semisynthesis" title="Semisynthesis">Semisynthesis</a></li> <li><a href="/wiki/Fullerene_chemistry" title="Fullerene chemistry">Fullerene chemistry</a></li> <li><a href="/wiki/Polymer_chemistry" title="Polymer chemistry">Polymer chemistry</a></li> <li><a href="/wiki/Petrochemistry" class="mw-redirect" title="Petrochemistry">Petrochemistry</a></li> <li><a href="/wiki/Dynamic_covalent_chemistry" title="Dynamic covalent chemistry">Dynamic covalent chemistry</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Biochemistry" title="Biochemistry">Biological</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/Biochemistry" title="Biochemistry">Biochemistry</a> <ul><li><a href="/wiki/Molecular_biology" title="Molecular biology">Molecular biology</a></li> <li><a href="/wiki/Cell_biology" title="Cell biology">Cell biology</a></li></ul></li> <li><a href="/wiki/Chemical_biology" title="Chemical biology">Chemical biology</a> <ul><li><a href="/wiki/Bioorthogonal_chemistry" title="Bioorthogonal chemistry">Bioorthogonal chemistry</a></li></ul></li> <li><a href="/wiki/Medicinal_chemistry" title="Medicinal chemistry">Medicinal chemistry</a> <ul><li><a href="/wiki/Pharmacology" title="Pharmacology">Pharmacology</a></li></ul></li> <li><a href="/wiki/Clinical_chemistry" title="Clinical chemistry">Clinical chemistry</a></li> <li><a href="/wiki/Neurochemistry" title="Neurochemistry">Neurochemistry</a></li> <li><a href="/wiki/Bioorganic_chemistry" title="Bioorganic chemistry">Bioorganic chemistry</a></li> <li><a href="/wiki/Bioorganometallic_chemistry" title="Bioorganometallic chemistry">Bioorganometallic chemistry</a></li> <li><a href="/wiki/Bioinorganic_chemistry" title="Bioinorganic chemistry">Bioinorganic chemistry</a></li> <li><a href="/wiki/Biophysical_chemistry" title="Biophysical chemistry">Biophysical chemistry</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Interdisciplinarity" title="Interdisciplinarity">Interdisciplinarity</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/Nuclear_chemistry" title="Nuclear chemistry">Nuclear chemistry</a> <ul><li><a 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href="/wiki/Combinatorial_chemistry" title="Combinatorial chemistry">Combinatorial chemistry</a></li> <li><a class="mw-selflink selflink">Biosynthesis</a></li></ul></li> <li><a href="/wiki/Chemical_engineering" title="Chemical engineering">Chemical engineering</a> <ul><li><a href="/wiki/Stoichiometry" title="Stoichiometry">Stoichiometry</a></li></ul></li> <li><a href="/wiki/Materials_science" title="Materials science">Materials science</a> <ul><li><a href="/wiki/Metallurgy" title="Metallurgy">Metallurgy</a></li> <li><a href="/wiki/Ceramic_engineering" title="Ceramic engineering">Ceramic engineering</a></li> <li><a href="/wiki/Polymer_science" title="Polymer science">Polymer science</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">See also</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/History_of_chemistry" title="History of chemistry">History of chemistry</a></li> <li><a href="/wiki/Nobel_Prize_in_Chemistry" title="Nobel Prize in Chemistry">Nobel Prize in Chemistry</a></li> <li><a href="/wiki/Timeline_of_chemistry" title="Timeline of chemistry">Timeline of chemistry</a> <ul><li><a href="/wiki/Discovery_of_chemical_elements" title="Discovery of chemical elements">of element discoveries</a></li></ul></li> <li>"<a href="/wiki/The_central_science" title="The central science">The central science</a>"</li> <li><a href="/wiki/Chemical_reaction" title="Chemical reaction">Chemical reaction</a> <ul><li><a href="/wiki/Catalysis" title="Catalysis">Catalysis</a></li></ul></li> <li><a href="/wiki/Chemical_element" title="Chemical element">Chemical element</a></li> <li><a href="/wiki/Chemical_compound" title="Chemical compound">Chemical compound</a></li> <li><a href="/wiki/Atom" title="Atom">Atom</a></li> <li><a href="/wiki/Molecule" title="Molecule">Molecule</a></li> <li><a href="/wiki/Ion" title="Ion">Ion</a></li> <li><a href="/wiki/Chemical_substance" title="Chemical substance">Chemical substance</a></li> <li><a href="/wiki/Chemical_bond" title="Chemical bond">Chemical bond</a></li> <li><a href="/wiki/Alchemy" title="Alchemy">Alchemy</a></li> <li><a href="/wiki/Quantum_mechanics" title="Quantum mechanics">Quantum mechanics</a></li></ul> </div></td></tr><tr><td class="navbox-abovebelow" colspan="2"><div> <ul><li><span class="noviewer" typeof="mw:File"><span title="Category"><img alt="" src="//upload.wikimedia.org/wikipedia/en/thumb/9/96/Symbol_category_class.svg/16px-Symbol_category_class.svg.png" decoding="async" width="16" height="16" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/en/thumb/9/96/Symbol_category_class.svg/23px-Symbol_category_class.svg.png 1.5x, //upload.wikimedia.org/wikipedia/en/thumb/9/96/Symbol_category_class.svg/31px-Symbol_category_class.svg.png 2x" data-file-width="180" data-file-height="185" /></span></span> <b><a href="/wiki/Category:Chemistry" 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