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<span>Oxaloacetate/aspartate: lysine, asparagine, methionine, threonine, and isoleucine</span> </div> </a> <button aria-controls="toc-Oxaloacetate/aspartate:_lysine,_asparagine,_methionine,_threonine,_and_isoleucine-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 Oxaloacetate/aspartate: lysine, asparagine, methionine, threonine, and isoleucine subsection</span> </button> <ul id="toc-Oxaloacetate/aspartate:_lysine,_asparagine,_methionine,_threonine,_and_isoleucine-sublist" class="vector-toc-list"> <li id="toc-Aspartate" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Aspartate"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.1</span> <span>Aspartate</span> </div> </a> <ul id="toc-Aspartate-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Lysine" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Lysine"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.2</span> <span>Lysine</span> </div> </a> <ul id="toc-Lysine-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Asparagine" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Asparagine"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.3</span> <span>Asparagine</span> </div> </a> <ul id="toc-Asparagine-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Methionine" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Methionine"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.4</span> <span>Methionine</span> </div> </a> <ul id="toc-Methionine-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Threonine" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Threonine"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.5</span> <span>Threonine</span> </div> </a> <ul id="toc-Threonine-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Isoleucine" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Isoleucine"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.6</span> <span>Isoleucine</span> </div> </a> <ul id="toc-Isoleucine-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Ribose_5-phosphates:_histidine" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Ribose_5-phosphates:_histidine"> <div class="vector-toc-text"> <span class="vector-toc-numb">4</span> <span>Ribose 5-phosphates: histidine</span> </div> </a> <ul id="toc-Ribose_5-phosphates:_histidine-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-3-Phosphoglycerates:_serine,_glycine,_cysteine" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#3-Phosphoglycerates:_serine,_glycine,_cysteine"> <div class="vector-toc-text"> <span class="vector-toc-numb">5</span> <span>3-Phosphoglycerates: serine, glycine, cysteine</span> </div> </a> <button aria-controls="toc-3-Phosphoglycerates:_serine,_glycine,_cysteine-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 3-Phosphoglycerates: serine, glycine, cysteine subsection</span> </button> <ul id="toc-3-Phosphoglycerates:_serine,_glycine,_cysteine-sublist" class="vector-toc-list"> <li id="toc-Serine" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Serine"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.1</span> <span>Serine</span> </div> </a> <ul id="toc-Serine-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Glycine" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Glycine"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.2</span> <span>Glycine</span> </div> </a> <ul id="toc-Glycine-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Cysteine" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Cysteine"> <div class="vector-toc-text"> <span class="vector-toc-numb">5.3</span> <span>Cysteine</span> </div> </a> <ul id="toc-Cysteine-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Pyruvate:_alanine,_valine,_and_leucine" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Pyruvate:_alanine,_valine,_and_leucine"> <div class="vector-toc-text"> <span class="vector-toc-numb">6</span> <span>Pyruvate: alanine, valine, and leucine</span> </div> </a> <button aria-controls="toc-Pyruvate:_alanine,_valine,_and_leucine-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 Pyruvate: alanine, valine, and leucine subsection</span> </button> <ul id="toc-Pyruvate:_alanine,_valine,_and_leucine-sublist" class="vector-toc-list"> <li id="toc-Alanine" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Alanine"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.1</span> <span>Alanine</span> </div> </a> <ul id="toc-Alanine-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Valine" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Valine"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.2</span> <span>Valine</span> </div> </a> <ul id="toc-Valine-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Leucine" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Leucine"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.3</span> <span>Leucine</span> </div> </a> <ul id="toc-Leucine-sublist" class="vector-toc-list"> <li id="toc-ilvEDA_operon" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#ilvEDA_operon"> <div class="vector-toc-text"> <span class="vector-toc-numb">6.3.1</span> <span>ilvEDA operon</span> </div> </a> <ul id="toc-ilvEDA_operon-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> </ul> </li> <li id="toc-Commercial_syntheses_of_amino_acids" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#Commercial_syntheses_of_amino_acids"> <div class="vector-toc-text"> <span class="vector-toc-numb">7</span> <span>Commercial syntheses of amino acids</span> </div> </a> <ul id="toc-Commercial_syntheses_of_amino_acids-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">8</span> <span>References</span> </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-External_links" class="vector-toc-list-item vector-toc-level-1 vector-toc-list-item-expanded"> <a class="vector-toc-link" href="#External_links"> <div class="vector-toc-text"> <span class="vector-toc-numb">9</span> <span>External links</span> </div> </a> <ul id="toc-External_links-sublist" class="vector-toc-list"> </ul> </li> </ul> </div> </div> </nav> </div> </div> <div class="mw-content-container"> <main id="content" class="mw-body"> <header class="mw-body-header vector-page-titlebar"> <nav aria-label="Contents" class="vector-toc-landmark"> <div id="vector-page-titlebar-toc" class="vector-dropdown vector-page-titlebar-toc vector-button-flush-left" title="Table of Contents" > <input type="checkbox" id="vector-page-titlebar-toc-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-page-titlebar-toc" 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Available in 14 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-14" 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">14 languages</span> </label> <div class="vector-dropdown-content"> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="interlanguage-link interwiki-ca mw-list-item"><a href="https://ca.wikipedia.org/wiki/S%C3%ADntesi_dels_amino%C3%A0cids" title="Síntesi dels aminoàcids – Catalan" lang="ca" hreflang="ca" data-title="Síntesi dels aminoàcids" data-language-autonym="Català" data-language-local-name="Catalan" class="interlanguage-link-target"><span>Català</span></a></li><li class="interlanguage-link interwiki-es mw-list-item"><a href="https://es.wikipedia.org/wiki/S%C3%ADntesis_de_amino%C3%A1cidos" title="Síntesis de aminoácidos – Spanish" lang="es" hreflang="es" data-title="Síntesis de aminoácidos" data-language-autonym="Español" data-language-local-name="Spanish" class="interlanguage-link-target"><span>Español</span></a></li><li class="interlanguage-link interwiki-fa mw-list-item"><a href="https://fa.wikipedia.org/wiki/%D8%B3%D9%86%D8%AA%D8%B2_%D8%A2%D9%85%DB%8C%D9%86%D9%88_%D8%A7%D8%B3%DB%8C%D8%AF" title="سنتز آمینو اسید – Persian" lang="fa" hreflang="fa" data-title="سنتز آمینو اسید" data-language-autonym="فارسی" data-language-local-name="Persian" class="interlanguage-link-target"><span>فارسی</span></a></li><li class="interlanguage-link interwiki-ko mw-list-item"><a href="https://ko.wikipedia.org/wiki/%EC%95%84%EB%AF%B8%EB%85%B8%EC%82%B0_%ED%95%A9%EC%84%B1" title="아미노산 합성 – Korean" lang="ko" hreflang="ko" data-title="아미노산 합성" data-language-autonym="한국어" data-language-local-name="Korean" class="interlanguage-link-target"><span>한국어</span></a></li><li class="interlanguage-link interwiki-id mw-list-item"><a href="https://id.wikipedia.org/wiki/Sintesis_asam_amino" title="Sintesis asam amino – Indonesian" lang="id" hreflang="id" data-title="Sintesis asam amino" data-language-autonym="Bahasa Indonesia" data-language-local-name="Indonesian" class="interlanguage-link-target"><span>Bahasa Indonesia</span></a></li><li class="interlanguage-link interwiki-ja mw-list-item"><a href="https://ja.wikipedia.org/wiki/%E3%82%A2%E3%83%9F%E3%83%8E%E9%85%B8%E5%90%88%E6%88%90" title="アミノ酸合成 – Japanese" lang="ja" hreflang="ja" data-title="アミノ酸合成" 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-pl mw-list-item"><a href="https://pl.wikipedia.org/wiki/Biosynteza_aminokwas%C3%B3w" title="Biosynteza aminokwasów – Polish" lang="pl" hreflang="pl" data-title="Biosynteza aminokwasów" 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/S%C3%ADntese_de_amino%C3%A1cidos" title="Síntese de aminoácidos – Portuguese" lang="pt" hreflang="pt" data-title="Síntese de aminoácidos" data-language-autonym="Português" data-language-local-name="Portuguese" class="interlanguage-link-target"><span>Português</span></a></li><li class="interlanguage-link interwiki-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/Sinteza_aminokiselina" title="Sinteza aminokiselina – Serbian" lang="sr" hreflang="sr" data-title="Sinteza aminokiselina" 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/Sinteza_aminokiselina" title="Sinteza aminokiselina – Serbo-Croatian" lang="sh" hreflang="sh" data-title="Sinteza aminokiselina" data-language-autonym="Srpskohrvatski / српскохрватски" data-language-local-name="Serbo-Croatian" class="interlanguage-link-target"><span>Srpskohrvatski / српскохрватски</span></a></li><li class="interlanguage-link interwiki-fi mw-list-item"><a href="https://fi.wikipedia.org/wiki/Aminohapposynteesi" title="Aminohapposynteesi – Finnish" lang="fi" hreflang="fi" data-title="Aminohapposynteesi" data-language-autonym="Suomi" data-language-local-name="Finnish" class="interlanguage-link-target"><span>Suomi</span></a></li><li class="interlanguage-link interwiki-th mw-list-item"><a href="https://th.wikipedia.org/wiki/%E0%B8%81%E0%B8%B2%E0%B8%A3%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%E0%B8%81%E0%B8%A3%E0%B8%94%E0%B8%AD%E0%B8%B0%E0%B8%A1%E0%B8%B4%E0%B9%82%E0%B8%99" title="การสังเคราะห์กรดอะมิโน – Thai" lang="th" hreflang="th" data-title="การสังเคราะห์กรดอะมิโน" data-language-autonym="ไทย" data-language-local-name="Thai" class="interlanguage-link-target"><span>ไทย</span></a></li><li class="interlanguage-link interwiki-vi mw-list-item"><a href="https://vi.wikipedia.org/wiki/T%E1%BB%95ng_h%E1%BB%A3p_amino_acid" title="Tổng hợp amino acid – Vietnamese" lang="vi" hreflang="vi" data-title="Tổng hợp amino acid" data-language-autonym="Tiếng Việt" data-language-local-name="Vietnamese" class="interlanguage-link-target"><span>Tiếng Việt</span></a></li><li class="interlanguage-link interwiki-zh mw-list-item"><a href="https://zh.wikipedia.org/wiki/%E6%B0%A8%E5%9F%BA%E9%85%B8%E5%90%88%E6%88%90" title="氨基酸合成 – Chinese" lang="zh" hreflang="zh" data-title="氨基酸合成" data-language-autonym="中文" data-language-local-name="Chinese" class="interlanguage-link-target"><span>中文</span></a></li> </ul> <div class="after-portlet after-portlet-lang"><span class="wb-langlinks-edit wb-langlinks-link"><a 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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">For the non-biological synthesis of amino acids, see <a href="/wiki/Strecker_amino_acid_synthesis" title="Strecker amino acid synthesis">Strecker amino acid synthesis</a>.</div> <figure typeof="mw:File/Thumb"><a href="/wiki/File:Amino_acid_biosynthesis.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Amino_acid_biosynthesis.svg/349px-Amino_acid_biosynthesis.svg.png" decoding="async" width="349" height="376" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Amino_acid_biosynthesis.svg/523px-Amino_acid_biosynthesis.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Amino_acid_biosynthesis.svg/697px-Amino_acid_biosynthesis.svg.png 2x" data-file-width="523" data-file-height="564" /></a><figcaption>Amino acid biosynthesis overview. The drawn molecules are in their neutral forms and do not fully correspond to their presented names. Humans can not synthesize all of these amino acids. </figcaption></figure> <p><b>Amino acid biosynthesis</b> is the set of <a href="/wiki/Biochemical" class="mw-redirect" title="Biochemical">biochemical</a> processes (<a href="/wiki/Metabolic_pathways" class="mw-redirect" title="Metabolic pathways">metabolic pathways</a>) by which the <a href="/wiki/Amino_acid" title="Amino acid">amino acids</a> are produced. The substrates for these processes are various compounds in the <a href="/wiki/Organism" title="Organism">organism</a>'s diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids. These 11 are called the <a href="/wiki/Non-essential_amino_acid" class="mw-redirect" title="Non-essential amino acid">non-essential amino acids</a>.<sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup> </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="α-Ketoglutarates:_glutamate,_glutamine,_proline,_arginine"><span id=".CE.B1-Ketoglutarates:_glutamate.2C_glutamine.2C_proline.2C_arginine"></span>α-Ketoglutarates: glutamate, glutamine, proline, arginine</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=1" title="Edit section: α-Ketoglutarates: glutamate, glutamine, proline, arginine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Most amino acids are synthesized from α-<a href="/wiki/Ketoacids" class="mw-redirect" title="Ketoacids">ketoacids</a>, and later <a href="/wiki/Transamination" title="Transamination">transaminated</a> from another amino acid, usually <a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a>. The enzyme involved in this reaction is an <a href="/wiki/Aminotransferase" class="mw-redirect" title="Aminotransferase">aminotransferase</a>. </p> <dl><dd>α-ketoacid + glutamate ⇄ amino acid + α-ketoglutarate</dd></dl> <p><a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">Glutamate</a> itself is formed by <a href="/wiki/Amination" title="Amination">amination</a> of <a href="/wiki/%CE%91-ketoglutarate" class="mw-redirect" title="Α-ketoglutarate">α-ketoglutarate</a>: </p> <dl><dd><a href="/wiki/%CE%91-Ketoglutaric_acid" title="Α-Ketoglutaric acid">α-ketoglutarate</a> + <span class="chemf nowrap">NH<span class="nowrap"><span style="display:inline-block;margin-bottom:-0.3em;vertical-align:-0.4em;line-height:1em;font-size:80%;text-align:left"><sup style="font-size:inherit;line-height:inherit;vertical-align:baseline">+</sup><br /><sub style="font-size:inherit;line-height:inherit;vertical-align:baseline">4</sub></span></span></span> ⇄ glutamate</dd></dl> <p>The α-ketoglutarate family of amino acid synthesis (synthesis of glutamate, glutamine, proline and arginine) begins with α-ketoglutarate, an intermediate in the Citric Acid Cycle. The concentration of α-ketoglutarate is dependent on the activity and metabolism within the cell along with the regulation of enzymatic activity. In <i>E. coli</i> citrate synthase, the <a href="/wiki/Enzyme" title="Enzyme">enzyme</a> involved in the condensation reaction initiating the Citric Acid Cycle is strongly inhibited by α-ketoglutarate feedback inhibition and can be inhibited by DPNH as well high concentrations of ATP.<sup id="cite_ref-shapiro_2-0" class="reference"><a href="#cite_note-shapiro-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> This is one of the initial regulations of the α-ketoglutarate family of amino acid synthesis. </p><p>The regulation of the synthesis of <a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a> from α-ketoglutarate is subject to regulatory control of the <a href="/wiki/Citric_Acid_Cycle" class="mw-redirect" title="Citric Acid Cycle">Citric Acid Cycle</a> as well as mass action dependent on the concentrations of reactants involved due to the reversible nature of the transamination and glutamate dehydrogenase reactions.<sup id="cite_ref-shapiro_2-1" class="reference"><a href="#cite_note-shapiro-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> </p><p>The conversion of glutamate to <a href="/wiki/Glutamine" title="Glutamine">glutamine</a> is regulated by <a href="/wiki/Glutamine_synthetase" title="Glutamine synthetase">glutamine synthetase</a> (GS) and is a key step in nitrogen metabolism.<sup id="cite_ref-shapiro_2-2" class="reference"><a href="#cite_note-shapiro-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> This enzyme is regulated by at least four different mechanisms: 1. Repression and depression due to <a href="/wiki/Nitrogen" title="Nitrogen">nitrogen</a> levels; 2. Activation and inactivation due to enzymatic forms (taut and relaxed); 3. Cumulative feedback inhibition through end product metabolites; and 4. Alterations of the enzyme due to <a href="/wiki/Adenylation" class="mw-redirect" title="Adenylation">adenylation</a> and <a href="/wiki/Deadenylation" class="mw-redirect" title="Deadenylation">deadenylation</a>.<sup id="cite_ref-shapiro_2-3" class="reference"><a href="#cite_note-shapiro-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> In rich nitrogenous media or growth conditions containing high quantities of <a href="/wiki/Ammonia" title="Ammonia">ammonia</a> there is a low level of GS, whereas in limiting quantities of ammonia the specific activity of the enzyme is 20-fold higher.<sup id="cite_ref-shapiro_2-4" class="reference"><a href="#cite_note-shapiro-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> The confirmation of the enzyme plays a role in regulation depending on if GS is in the taut or relaxed form. The taut form of GS is fully active but, the removal of <a href="/wiki/Manganese" title="Manganese">manganese</a> converts the enzyme to the relaxed state. The specific conformational state occurs based on the binding of specific divalent cations and is also related to adenylation.<sup id="cite_ref-shapiro_2-5" class="reference"><a href="#cite_note-shapiro-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> The feedback inhibition of GS is due to a cumulative feedback due to several metabolites including L-tryptophan, L-histidine, AMP, CTP, glucosamine-6-phosphate and carbamyl phosphate, alanine, and glycine.<sup id="cite_ref-shapiro_2-6" class="reference"><a href="#cite_note-shapiro-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> An excess of any one product does not individually inhibit the enzyme but a combination or accumulation of all the end products have a strong inhibitory effect on the synthesis of <a href="/wiki/Glutamine" title="Glutamine">glutamine</a>.<sup id="cite_ref-shapiro_2-7" class="reference"><a href="#cite_note-shapiro-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> Glutamine synthase activity is also inhibited via adenylation. The adenylation activity is catalyzed by the bifunctional adenylyltransferase/adenylyl removal (AT/AR) enzyme. Glutamine and a regulatory protein called PII act together to stimulate adenylation.<sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> </p> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Amino_acid_synthesis01_a-ketoglutarate_family.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/4/42/Amino_acid_synthesis01_a-ketoglutarate_family.png/220px-Amino_acid_synthesis01_a-ketoglutarate_family.png" decoding="async" width="220" height="168" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/4/42/Amino_acid_synthesis01_a-ketoglutarate_family.png/330px-Amino_acid_synthesis01_a-ketoglutarate_family.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/4/42/Amino_acid_synthesis01_a-ketoglutarate_family.png/440px-Amino_acid_synthesis01_a-ketoglutarate_family.png 2x" data-file-width="3700" data-file-height="2832" /></a><figcaption>This diagram shows the biosynthesis (anabolism) of amino acids glutamate, glutamine, proline, and arginine from the precursor alpha-ketoglutarate.</figcaption></figure> <p><br /> The regulation of proline biosynthesis can depend on the initial controlling step through <a href="/wiki/Negative_feedback" title="Negative feedback">negative feedback</a> inhibition.<sup id="cite_ref-clara_4-0" class="reference"><a href="#cite_note-clara-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> In <i>E. coli</i>, proline allosterically inhibits Glutamate 5-kinase which catalyzes the reaction from L-glutamate to an unstable intermediate L-γ-Glutamyl phosphate.<sup id="cite_ref-clara_4-1" class="reference"><a href="#cite_note-clara-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> </p><p><a href="/wiki/Arginine" title="Arginine">Arginine</a> synthesis also utilizes negative feedback as well as repression through a repressor encoded by the <a href="/wiki/Gene" title="Gene">gene</a> <i>argR</i>. The gene product of <i>argR</i>, ArgR an <a href="/wiki/Aporepressor" class="mw-redirect" title="Aporepressor">aporepressor</a>, and arginine as a <a href="/wiki/Corepressor" title="Corepressor">corepressor</a> affect the operon of arginine biosynthesis. The degree of repression is determined by the concentrations of the repressor protein and corepressor level.<sup id="cite_ref-pmid1874410_5-0" class="reference"><a href="#cite_note-pmid1874410-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Erythrose_4-phosphate_and_phosphoenolpyruvate:_phenylalanine,_tyrosine,_and_tryptophan"><span id="Erythrose_4-phosphate_and_phosphoenolpyruvate:_phenylalanine.2C_tyrosine.2C_and_tryptophan"></span>Erythrose 4-phosphate and phosphoenolpyruvate: phenylalanine, tyrosine, and tryptophan</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=2" title="Edit section: Erythrose 4-phosphate and phosphoenolpyruvate: phenylalanine, tyrosine, and tryptophan"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Phenylalanine" title="Phenylalanine">Phenylalanine</a>, <a href="/wiki/Tyrosine" title="Tyrosine">tyrosine</a>, and <a href="/wiki/Tryptophan" title="Tryptophan">tryptophan</a>, the <a href="/wiki/Aromatic_amino_acids" class="mw-redirect" title="Aromatic amino acids">aromatic amino acids</a>, arise from <a href="/wiki/Chorismate" class="mw-redirect" title="Chorismate">chorismate</a>. The first step, condensation of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate (DAHP) from PEP/E4P, uses three isoenzymes AroF, AroG, and AroH. Each one of these has its synthesis regulated from tyrosine, phenylalanine, and tryptophan, respectively. The rest of the enzymes in the common pathway (conversion of DAHP to chorismate) appear to be synthesized constitutively, except for <a href="/wiki/Shikimate_kinase" title="Shikimate kinase">shikimate kinase</a>, which can be inhibited by shikimate through linear mixed-type inhibition. </p> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Amino_acid_synthesis02_erythrose-4-P_family.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/f/fc/Amino_acid_synthesis02_erythrose-4-P_family.png/220px-Amino_acid_synthesis02_erythrose-4-P_family.png" decoding="async" width="220" height="137" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/f/fc/Amino_acid_synthesis02_erythrose-4-P_family.png/330px-Amino_acid_synthesis02_erythrose-4-P_family.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/f/fc/Amino_acid_synthesis02_erythrose-4-P_family.png/440px-Amino_acid_synthesis02_erythrose-4-P_family.png 2x" data-file-width="4000" data-file-height="2487" /></a><figcaption>This diagram shows the biosynthesis (anabolism) of amino acids tryptophan, tyrosine, and phenylalanine from the precursor erythrose 4-phosphate.</figcaption></figure> <p>Tyrosine and phenylalanine are biosynthesized from <a href="/wiki/Prephenate" class="mw-redirect" title="Prephenate">prephenate</a>, which is converted to an amino acid-specific intermediate. This process is mediated by a <a href="/wiki/Phenylalanine" title="Phenylalanine">phenylalanine</a> (PheA) or <a href="/wiki/Tyrosine" title="Tyrosine">tyrosine</a> (TyrA) specific chorismate mutase-prephenate dehydrogenase. PheA uses a simple <a href="/wiki/Dehydrogenase" title="Dehydrogenase">dehydrogenase</a> to convert prephenate to <a href="/wiki/Phenylpyruvate" class="mw-redirect" title="Phenylpyruvate">phenylpyruvate</a>, while TyrA uses a NAD-dependent dehydrogenase to make 4-hydroxylphenylpyruvate. Both PheA and TyrA are feedback inhibited by their respective amino acids. Tyrosine can also be inhibited at the transcriptional level by the TyrR repressor. TyrR binds to the TyrR boxes on the operon near the promoter of the gene that it wants to repress. </p><p>Tryptophan biosynthesis involves conversion of chorismate to anthranilate using <a href="/wiki/Anthranilate_synthase" title="Anthranilate synthase">anthranilate synthase</a>. This enzyme requires either glutamine as the amino group donor or ammonia itself. <a href="/wiki/Anthranilate_synthase" title="Anthranilate synthase">Anthranilate synthase</a> is regulated by the gene products of trpE and trpG. trpE encodes the first subunit, which binds to <a href="/wiki/Chorismate" class="mw-redirect" title="Chorismate">chorismate</a> and moves the amino group from the donor to chorismate. trpG encodes the second subunit, which facilitates the transfer of the amino group from glutamine. Anthranilate synthase is also regulated by feedback inhibition: tryptophan is a co-repressor to the TrpR repressor. </p> <div class="mw-heading mw-heading2"><h2 id="Oxaloacetate/aspartate:_lysine,_asparagine,_methionine,_threonine,_and_isoleucine"><span id="Oxaloacetate.2Faspartate:_lysine.2C_asparagine.2C_methionine.2C_threonine.2C_and_isoleucine"></span>Oxaloacetate/aspartate: lysine, asparagine, methionine, threonine, and isoleucine</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=3" title="Edit section: Oxaloacetate/aspartate: lysine, asparagine, methionine, threonine, and isoleucine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The oxaloacetate/aspartate family of amino acids is composed of <a href="/wiki/Lysine" title="Lysine">lysine</a>, <a href="/wiki/Asparagine" title="Asparagine">asparagine</a>, <a href="/wiki/Methionine" title="Methionine">methionine</a>, <a href="/wiki/Threonine" title="Threonine">threonine</a>, and <a href="/wiki/Isoleucine" title="Isoleucine">isoleucine</a>. <a href="/wiki/Aspartate" class="mw-redirect" title="Aspartate">Aspartate</a> can be converted into lysine, asparagine, methionine and threonine. <a href="/wiki/Threonine" title="Threonine">Threonine</a> also gives rise to <a href="/wiki/Isoleucine" title="Isoleucine">isoleucine</a>. </p> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Amino_acid_synthesis03_oxaloacetate_family.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/f/fa/Amino_acid_synthesis03_oxaloacetate_family.png/220px-Amino_acid_synthesis03_oxaloacetate_family.png" decoding="async" width="220" height="213" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/f/fa/Amino_acid_synthesis03_oxaloacetate_family.png/330px-Amino_acid_synthesis03_oxaloacetate_family.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/f/fa/Amino_acid_synthesis03_oxaloacetate_family.png/440px-Amino_acid_synthesis03_oxaloacetate_family.png 2x" data-file-width="3860" data-file-height="3736" /></a><figcaption>This diagram shows the biosynthesis (anabolism) of amino acids aspartate, asparagine, threonine, methionine, lysine from the precursor oxaloacetate.</figcaption></figure> <p>The associated <a href="/wiki/Enzyme" title="Enzyme">enzymes</a> are subject to regulation via feedback inhibition and/or repression at the genetic level. As is typical in highly branched metabolic pathways, additional regulation at each branch point of the pathway. This type of regulatory scheme allows control over the total flux of the aspartate pathway in addition to the total flux of individual amino acids. The aspartate pathway uses L-aspartic acid as the precursor for the biosynthesis of one-fourth of the building block amino acids. </p> <div class="mw-heading mw-heading3"><h3 id="Aspartate">Aspartate</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=4" title="Edit section: Aspartate"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The biosynthesis of aspartate frequently involves the transamination of oxaloacetate. </p><p>The enzyme <a href="/wiki/Aspartokinase" class="mw-redirect" title="Aspartokinase">aspartokinase</a>, which catalyzes the <a href="/wiki/Phosphorylation" title="Phosphorylation">phosphorylation</a> of <a href="/wiki/Aspartate" class="mw-redirect" title="Aspartate">aspartate</a> and initiates its conversion into other amino acids, can be broken up into 3 isozymes, AK-I, II and III. AK-I is feed-back inhibited by <a href="/wiki/Threonine" title="Threonine">threonine</a>, while AK-II and III are inhibited by <a href="/wiki/Lysine" title="Lysine">lysine</a>. As a sidenote, AK-III catalyzes the <a href="/wiki/Phosphorylation" title="Phosphorylation">phosphorylation</a> of <a href="/wiki/Aspartic_acid" title="Aspartic acid">aspartic acid</a> that is the committed step in this biosynthetic pathway. Aspartate kinase becomes downregulated by the presence of <a href="/wiki/Threonine" title="Threonine">threonine</a> or <a href="/wiki/Lysine" title="Lysine">lysine</a>. </p> <div class="mw-heading mw-heading3"><h3 id="Lysine">Lysine</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=5" title="Edit section: Lysine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Lysine" title="Lysine">Lysine</a> is synthesized from aspartate via the diaminopimelate (DAP) pathway. The initial two stages of the DAP pathway are catalyzed by <a href="/wiki/Aspartokinase" class="mw-redirect" title="Aspartokinase">aspartokinase</a> and aspartate semialdehyde dehydrogenase. These enzymes play a key role in the biosynthesis of <a href="/wiki/Lysine" title="Lysine">lysine</a>, <a href="/wiki/Threonine" title="Threonine">threonine</a>, and <a href="/wiki/Methionine" title="Methionine">methionine</a>. There are two bifunctional aspartokinase/homoserine dehydrogenases, ThrA and MetL, in addition to a monofunctional aspartokinase, <a href="/wiki/LysC" title="LysC">LysC</a>. Transcription of aspartokinase genes is regulated by concentrations of the subsequently produced amino acids, lysine, threonine, and methionine. The higher these amino acids concentrations, the less the gene is transcribed. ThrA and LysC are also feed-back inhibited by threonine and lysine. Finally, DAP decarboxylase LysA mediates the last step of the lysine synthesis and is common for all studied bacterial species. The formation of aspartate kinase (AK), which catalyzes the <a href="/wiki/Phosphorylation" title="Phosphorylation">phosphorylation</a> of aspartate and initiates its conversion into other amino acids, is also inhibited by both <a href="/wiki/Lysine" title="Lysine">lysine</a> and <a href="/wiki/Threonine" title="Threonine">threonine</a>, which prevents the formation of the amino acids derived from aspartate. Additionally, high lysine concentrations inhibit the activity of <a href="/wiki/Dihydrodipicolinate_synthase" title="Dihydrodipicolinate synthase">dihydrodipicolinate synthase</a> (DHPS). So, in addition to inhibiting the first enzyme of the aspartate families biosynthetic pathway, lysine also inhibits the activity of the first enzyme after the branch point, i.e. the enzyme that is specific for lysine's own synthesis. </p> <div class="mw-heading mw-heading3"><h3 id="Asparagine">Asparagine</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=6" title="Edit section: Asparagine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The biosynthesis of asparagine originates with <a href="/wiki/Aspartate" class="mw-redirect" title="Aspartate">aspartate</a> using a <a href="/wiki/Transaminase" title="Transaminase">transaminase</a> enzyme. The enzyme <a href="/wiki/Asparagine_synthetase" title="Asparagine synthetase">asparagine synthetase</a> produces asparagine, <a href="/wiki/Adenosine_monophosphate" title="Adenosine monophosphate">AMP</a>, glutamate, and <a href="/wiki/Pyrophosphate" title="Pyrophosphate">pyrophosphate</a> from aspartate, <a href="/wiki/Glutamine" title="Glutamine">glutamine</a>, and <a href="/wiki/Adenosine_triphosphate" title="Adenosine triphosphate">ATP</a>. In the asparagine synthetase reaction, ATP is used to activate aspartate, forming β-aspartyl-AMP. <a href="/wiki/Glutamine" title="Glutamine">Glutamine</a> donates an ammonium group, which reacts with β-aspartyl-AMP to form asparagine and free AMP. </p> <figure class="mw-halign-center" typeof="mw:File/Frame"><a href="/wiki/File:Asn_biosynthesis.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/f/f3/Asn_biosynthesis.svg/512px-Asn_biosynthesis.svg.png" decoding="async" width="512" height="140" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/f/f3/Asn_biosynthesis.svg/768px-Asn_biosynthesis.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/f/f3/Asn_biosynthesis.svg/1024px-Asn_biosynthesis.svg.png 2x" data-file-width="512" data-file-height="140" /></a><figcaption>The biosynthesis of aspartate and asparagine from oxaloacetate.</figcaption></figure> <p>Two <a href="/wiki/Asparagine" title="Asparagine">asparagine</a> synthetases are found in <a href="/wiki/Bacteria" title="Bacteria">bacteria</a>. Both are referred to as the AsnC <a href="/wiki/Protein" title="Protein">protein</a>. They are coded for by the genes AsnA and AsnB. AsnC is autogenously regulated, which is where the product of a structural gene regulates the expression of the <a href="/wiki/Operon" title="Operon">operon</a> in which the genes reside. The stimulating effect of AsnC on AsnA transcription is downregulated by asparagine. However, the autoregulation of AsnC is not affected by asparagine. </p> <div class="mw-heading mw-heading3"><h3 id="Methionine">Methionine</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=7" title="Edit section: Methionine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Biosynthesis by the <a href="/wiki/Transsulfuration_pathway" title="Transsulfuration pathway">transsulfuration pathway</a> starts with aspartic acid. Relevant enzymes include <a href="/wiki/Aspartokinase" class="mw-redirect" title="Aspartokinase">aspartokinase</a>, <a href="/wiki/Aspartate-semialdehyde_dehydrogenase" title="Aspartate-semialdehyde dehydrogenase">aspartate-semialdehyde dehydrogenase</a>, <a href="/wiki/Homoserine_dehydrogenase" title="Homoserine dehydrogenase">homoserine dehydrogenase</a>, <a href="/wiki/Homoserine_O-transsuccinylase" class="mw-redirect" title="Homoserine O-transsuccinylase">homoserine O-transsuccinylase</a>, <a href="/wiki/Cystathionine-%CE%B3-synthase" class="mw-redirect" title="Cystathionine-γ-synthase">cystathionine-γ-synthase</a>, <a href="/wiki/Cystathionine-%CE%B2-lyase" class="mw-redirect" title="Cystathionine-β-lyase">Cystathionine-β-lyase</a> (in mammals, this step is performed by <a href="/wiki/Homocysteine_methyltransferase" class="mw-redirect" title="Homocysteine methyltransferase">homocysteine methyltransferase</a> or <a href="/wiki/Betaine%E2%80%94homocysteine_S-methyltransferase" title="Betaine—homocysteine S-methyltransferase">betaine—homocysteine S-methyltransferase</a>.) </p><p><a href="/wiki/Methionine" title="Methionine">Methionine</a> biosynthesis is subject to tight regulation. The repressor protein MetJ, in cooperation with the corepressor protein S-adenosyl-methionine, mediates the repression of methionine's biosynthesis. The regulator MetR is required for MetE and MetH gene expression and functions as a transactivator of transcription for these <a href="/wiki/Gene" title="Gene">genes</a>. MetR transcriptional activity is regulated by homocystein, which is the metabolic precursor of <a href="/wiki/Methionine" title="Methionine">methionine</a>. It is also known that <a href="/wiki/Vitamin_B12" title="Vitamin B12">vitamin B12</a> can repress MetE gene expression, which is mediated by the MetH holoenzyme. </p> <div class="mw-heading mw-heading3"><h3 id="Threonine">Threonine</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=8" title="Edit section: Threonine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>In plants and microorganisms, threonine is synthesized from <a href="/wiki/Aspartic_acid" title="Aspartic acid">aspartic acid</a> via α-aspartyl-semialdehyde and <a href="/wiki/Homoserine" title="Homoserine">homoserine</a>. Homoserine undergoes <i>O</i>-phosphorylation; this phosphate <a href="/wiki/Ester" title="Ester">ester</a> undergoes hydrolysis concomitant with relocation of the OH group.<sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> Enzymes involved in a typical biosynthesis of threonine include <a href="/wiki/Aspartokinase" class="mw-redirect" title="Aspartokinase">aspartokinase</a>, <a href="/wiki/Aspartate-semialdehyde_dehydrogenase" title="Aspartate-semialdehyde dehydrogenase">β-aspartate semialdehyde dehydrogenase</a>, <a href="/wiki/Homoserine_dehydrogenase" title="Homoserine dehydrogenase">homoserine dehydrogenase</a>, <a href="/wiki/Homoserine_kinase" title="Homoserine kinase">homoserine kinase</a>, <a href="/wiki/Threonine_synthase" title="Threonine synthase">threonine synthase</a>. </p><p>The biosynthesis of <a href="/wiki/Threonine" title="Threonine">threonine</a> is regulated via allosteric regulation of its precursor, <a href="/wiki/Homoserine" title="Homoserine">homoserine</a>, by structurally altering the enzyme homoserine dehydrogenase. This reaction occurs at a key branch point in the pathway, with the substrate homoserine serving as the precursor for the biosynthesis of lysine, methionine, threonin and isoleucine. High levels of <a href="/wiki/Threonine" title="Threonine">threonine</a> result in low levels of homoserine synthesis. The synthesis of <a href="/wiki/Aspartate_kinase" title="Aspartate kinase">aspartate kinase</a> (AK), which catalyzes the phosphorylation of aspartate and initiates its conversion into other amino acids, is feed-back inhibited by <a href="/wiki/Lysine" title="Lysine">lysine</a>, <a href="/wiki/Isoleucine" title="Isoleucine">isoleucine</a>, and <a href="/wiki/Threonine" title="Threonine">threonine</a>, which prevents the synthesis of the amino acids derived from aspartate. So, in addition to inhibiting the first enzyme of the aspartate families biosynthetic pathway, threonine also inhibits the activity of the first enzyme after the branch point, i.e. the enzyme that is specific for threonine's own synthesis. </p> <div class="mw-heading mw-heading3"><h3 id="Isoleucine">Isoleucine</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=9" title="Edit section: Isoleucine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>In plants and microorganisms, isoleucine is biosynthesized from <a href="/wiki/Pyruvic_acid" title="Pyruvic acid">pyruvic acid</a> and <a href="/wiki/Alpha-ketoglutarate" class="mw-redirect" title="Alpha-ketoglutarate">alpha-ketoglutarate</a>. Enzymes involved in this biosynthesis include <a href="/wiki/Acetolactate_synthase" title="Acetolactate synthase">acetolactate synthase</a> (also known as acetohydroxy acid synthase), <a href="/w/index.php?title=Acetohydroxy_acid_isomeroreductase&action=edit&redlink=1" class="new" title="Acetohydroxy acid isomeroreductase (page does not exist)">acetohydroxy acid isomeroreductase</a>, <a href="/wiki/Dihydroxyacid_dehydratase" class="mw-redirect" title="Dihydroxyacid dehydratase">dihydroxyacid dehydratase</a>, and <a href="/wiki/Valine-3-methyl-2-oxovalerate_transaminase" class="mw-redirect" title="Valine-3-methyl-2-oxovalerate transaminase">valine aminotransferase</a>.<sup id="cite_ref-7" class="reference"><a href="#cite_note-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> </p><p>In terms of regulation, the enzymes threonine deaminase, dihydroxy acid dehydrase, and transaminase are controlled by end-product regulation. i.e. the presence of isoleucine will downregulate threonine biosynthesis. High concentrations of isoleucine also result in the downregulation of aspartate's conversion into the aspartyl-phosphate intermediate, hence halting further biosynthesis of <a href="/wiki/Lysine" title="Lysine">lysine</a>, <a href="/wiki/Methionine" title="Methionine">methionine</a>, <a href="/wiki/Threonine" title="Threonine">threonine</a>, and <a href="/wiki/Isoleucine" title="Isoleucine">isoleucine</a>. </p> <div class="mw-heading mw-heading2"><h2 id="Ribose_5-phosphates:_histidine">Ribose 5-phosphates: histidine</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=10" title="Edit section: Ribose 5-phosphates: histidine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>In <i>E. coli</i>, the biosynthesis begins with phosphorylation of 5-phosphoribosyl-pyrophosphate (PRPP), catalyzed by <a href="/wiki/ATP_phosphoribosyltransferase" title="ATP phosphoribosyltransferase">ATP-phosphoribosyl transferase</a>. Phosphoribosyl-ATP converts to phosphoribosyl-AMP (PRAMP). His4 then catalyzes the formation of phosphoribosylformiminoAICAR-phosphate, which is then converted to phosphoribulosylformimino-AICAR-P by the His6 gene product.<sup id="cite_ref-:2_8-0" class="reference"><a href="#cite_note-:2-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> His7 splits phosphoribulosylformimino-AICAR-P to form <small>D</small>-erythro-imidazole-glycerol-phosphate. After, His3 forms imidazole acetol-phosphate releasing water. His5 then makes <small>L</small>-histidinol-phosphate, which is then hydrolyzed by His2 making <a href="/w/index.php?title=Histidinol&action=edit&redlink=1" class="new" title="Histidinol (page does not exist)">histidinol</a>. <a href="/wiki/Histidinol_dehydrogenase" title="Histidinol dehydrogenase">His4</a> catalyzes the oxidation of <small>L</small>-histidinol to form <small>L</small>-histidinal, an amino aldehyde. In the last step, <small>L</small>-histidinal is converted to <small>L</small>-histidine.<sup id="cite_ref-:2_8-1" class="reference"><a href="#cite_note-:2-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-9" class="reference"><a href="#cite_note-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> </p> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Amino_acid_synthesis04_ribose-5-phosphate_family.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/3/37/Amino_acid_synthesis04_ribose-5-phosphate_family.png/220px-Amino_acid_synthesis04_ribose-5-phosphate_family.png" decoding="async" width="220" height="133" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/3/37/Amino_acid_synthesis04_ribose-5-phosphate_family.png/330px-Amino_acid_synthesis04_ribose-5-phosphate_family.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/3/37/Amino_acid_synthesis04_ribose-5-phosphate_family.png/440px-Amino_acid_synthesis04_ribose-5-phosphate_family.png 2x" data-file-width="3860" data-file-height="2328" /></a><figcaption>This diagram shows the biosynthesis (anabolism) of amino acid histidine from the precursor ribose-5-phosphate.</figcaption></figure> <p>In general, the histidine biosynthesis is very similar in plants and microorganisms.<sup id="cite_ref-10" class="reference"><a href="#cite_note-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-cohen_11-0" class="reference"><a href="#cite_note-cohen-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> </p><p>HisG → HisE/HisI → HisA → HisH → HisF → HisB → HisC → HisB → HisD (HisE/I and HisB are both bifunctional enzymes) </p><p>The enzymes are coded for on the His operon. This operon has a distinct block of the leader sequence, called block 1: </p><p>Met-Thr-Arg-Val-Gln-Phe-Lys-His-His-His-His-His-His-His-Pro-Asp </p><p>This leader sequence is important for the regulation of histidine in <i>E. coli</i>. The <i>His</i> operon operates under a system of coordinated regulation where all the gene products will be repressed or depressed equally. The main factor in the repression or derepression of histidine synthesis is the concentration of histidine charged tRNAs. The regulation of histidine is actually quite simple considering the complexity of its biosynthesis pathway and, it closely resembles regulation of <a href="/wiki/Tryptophan" title="Tryptophan">tryptophan</a>. In this system the full leader sequence has 4 blocks of complementary strands that can form hairpin loops structures.<sup id="cite_ref-cohen_11-1" class="reference"><a href="#cite_note-cohen-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> Block one, shown above, is the key to regulation. When <a href="/wiki/Histidine" title="Histidine">histidine</a> charged <a href="/wiki/TRNA" class="mw-redirect" title="TRNA">tRNA</a> levels are low in the cell the ribosome will stall at the string of His residues in block 1. This stalling of the <a href="/wiki/Ribosome" title="Ribosome">ribosome</a> will allow complementary strands 2 and 3 to form a hairpin loop. The loop formed by strands 2 and 3 forms an anti-terminator and translation of the <i>his</i> genes will continue and histidine will be produced. However, when histidine charged tRNA levels are high the <a href="/wiki/Ribosome" title="Ribosome">ribosome</a> will not stall at block 1, this will not allow strands 2 and 3 to form a hairpin. Instead strands 3 and 4 will form a hairpin loop further downstream of the ribosome. The hairpin loop formed by strands 3 and 4 is a terminating loop, when the ribosome comes into contact with the loop, it will be “knocked off” the transcript. When the ribosome is removed the <i>His</i> genes will not be translated and histidine will not be produced by the cell.<sup id="cite_ref-12" class="reference"><a href="#cite_note-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="3-Phosphoglycerates:_serine,_glycine,_cysteine"><span id="3-Phosphoglycerates:_serine.2C_glycine.2C_cysteine"></span>3-Phosphoglycerates: serine, glycine, cysteine</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=11" title="Edit section: 3-Phosphoglycerates: serine, glycine, cysteine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The 3-Phosphoglycerate family of amino acids includes serine, glycine, and cysteine. </p> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Amino_acid_synthesis05_3-phosphoglycerate_family.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/8/8f/Amino_acid_synthesis05_3-phosphoglycerate_family.png/220px-Amino_acid_synthesis05_3-phosphoglycerate_family.png" decoding="async" width="220" height="75" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/8/8f/Amino_acid_synthesis05_3-phosphoglycerate_family.png/330px-Amino_acid_synthesis05_3-phosphoglycerate_family.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/8/8f/Amino_acid_synthesis05_3-phosphoglycerate_family.png/440px-Amino_acid_synthesis05_3-phosphoglycerate_family.png 2x" data-file-width="3860" data-file-height="1322" /></a><figcaption>This diagram shows the biosynthesis (anabolism) of amino acids serine, glycine, and cysteine from the precursor 3-phosphoglycerate.</figcaption></figure> <div class="mw-heading mw-heading3"><h3 id="Serine">Serine</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=12" title="Edit section: Serine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Serine" title="Serine">Serine</a> is the first amino acid in this family to be produced; it is then modified to produce both <a href="/wiki/Glycine" title="Glycine">glycine</a> and <a href="/wiki/Cysteine" title="Cysteine">cysteine</a> (and many other biologically important molecules). Serine is formed from 3-phosphoglycerate in the following pathway: </p><p>3-phosphoglycerate → phosphohydroxyl-pyruvate → phosphoserine → serine </p><p>The conversion from 3-phosphoglycerate to phosphohydroxyl-pyruvate is achieved by the enzyme <a href="/wiki/Phosphoglycerate_dehydrogenase" title="Phosphoglycerate dehydrogenase">phosphoglycerate dehydrogenase</a>. This enzyme is the key regulatory step in this pathway. Phosphoglycerate dehydrogenase is regulated by the concentration of serine in the <a href="/wiki/Cell_(biology)" title="Cell (biology)">cell</a>. At high concentrations this enzyme will be inactive and serine will not be produced. At low concentrations of serine the enzyme will be fully active and serine will be produced by the <a href="/wiki/Bacterium" class="mw-redirect" title="Bacterium">bacterium</a>.<sup id="cite_ref-13" class="reference"><a href="#cite_note-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup> Since serine is the first amino acid produced in this family both glycine and cysteine will be regulated by the available concentration of serine in the cell.<sup id="cite_ref-pmid14086727_14-0" class="reference"><a href="#cite_note-pmid14086727-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Glycine">Glycine</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=13" title="Edit section: Glycine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Glycine" title="Glycine">Glycine</a> is biosynthesized from serine, catalyzed by serine hydroxymethyltransferase (SHMT). The enzyme effectively replaces a hydroxymethyl group with a hydrogen atom. </p><p>SHMT is coded by the gene <i>glyA</i>. The regulation of <i>glyA</i> is complex and is known to incorporate serine, glycine, methionine, purines, thymine, and folates, The full mechanism has yet to be elucidated.<sup id="cite_ref-Steiert_1990_15-0" class="reference"><a href="#cite_note-Steiert_1990-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup> The methionine gene product MetR and the methionine intermediate homocysteine are known to positively regulate glyA. Homocysteine is a coactivator of <i>glyA</i> and must act in concert with MetR.<sup id="cite_ref-Steiert_1990_15-1" class="reference"><a href="#cite_note-Steiert_1990-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-pmid2670901_16-0" class="reference"><a href="#cite_note-pmid2670901-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup> On the other hand, PurR, a protein which plays a role in purine synthesis and S-adeno-sylmethionine are known to down regulate <i>glyA</i>. PurR binds directly to the control region of <i>glyA</i> and effectively turns the gene off so that glycine will not be produced by the bacterium. </p> <div class="mw-heading mw-heading3"><h3 id="Cysteine">Cysteine</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=14" title="Edit section: Cysteine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The genes required for the synthesis of <a href="/wiki/Cysteine" title="Cysteine">cysteine</a> are coded for on the <i>cys</i> regulon. The integration of sulfur is positively regulated by CysB. Effective inducers of this regulon are N-acetyl-serine (NAS) and very small amounts of reduced sulfur. CysB functions by binding to DNA half sites on the <i>cys</i> regulon. These half sites differ in quantity and arrangement depending on the promoter of interest. There is however one half site that is conserved. It lies just upstream of the -35 site of the promoter. There are also multiple accessory sites depending on the promoter. In the absence of the inducer, NAS, CysB will bind the <a href="/wiki/DNA" title="DNA">DNA</a> and cover many of the accessory half sites. Without the accessory half sites the regulon cannot be transcribed and cysteine will not be produced. It is believed that the presence of NAS causes CysB to undergo a conformational change. This conformational change allows CysB to bind properly to all the half sites and causes the recruitment of the RNA polymerase. The RNA polymerase will then transcribe the <i>cys</i> regulon and cysteine will be produced. </p><p>Further regulation is required for this pathway, however. CysB can down regulate its own transcription by binding to its own DNA sequence and blocking the RNA polymerase. In this case NAS will act to disallow the binding of CysB to its own DNA sequence. OAS is a precursor of NAS, cysteine itself can inhibit CysE which functions to create OAS. Without the necessary OAS, NAS will not be produced and cysteine will not be produced. There are two other negative regulators of cysteine. These are the molecules <a href="/wiki/Sulfide" title="Sulfide">sulfide</a> and <a href="/wiki/Thiosulfate" title="Thiosulfate">thiosulfate</a>, they act to bind to CysB and they compete with NAS for the binding of CysB.<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> </p> <div class="mw-heading mw-heading2"><h2 id="Pyruvate:_alanine,_valine,_and_leucine"><span id="Pyruvate:_alanine.2C_valine.2C_and_leucine"></span>Pyruvate: alanine, valine, and leucine</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=15" title="Edit section: Pyruvate: alanine, valine, and leucine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Pyruvate, the result of <a href="/wiki/Glycolysis" title="Glycolysis">glycolysis</a>, can feed into both the TCA cycle and <a href="/wiki/Fermentation" title="Fermentation">fermentation</a> processes. Reactions beginning with either one or two molecules of pyruvate lead to the synthesis of alanine, valine, and leucine. Feedback inhibition of final products is the main method of inhibition, and, in <i>E. coli</i>, the <i>ilvEDA</i> operon also plays a part in this regulation. </p> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Amino_acid_synthesis06_pyruvate_family.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/a/a4/Amino_acid_synthesis06_pyruvate_family.png/220px-Amino_acid_synthesis06_pyruvate_family.png" decoding="async" width="220" height="165" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/a/a4/Amino_acid_synthesis06_pyruvate_family.png/330px-Amino_acid_synthesis06_pyruvate_family.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/a/a4/Amino_acid_synthesis06_pyruvate_family.png/440px-Amino_acid_synthesis06_pyruvate_family.png 2x" data-file-width="3860" data-file-height="2898" /></a><figcaption>This diagram shows the biosynthesis (anabolism) of amino acids alanine, valine, isoleucine, and leucine from the precursor pyruvate.</figcaption></figure> <div class="mw-heading mw-heading3"><h3 id="Alanine">Alanine</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=16" title="Edit section: Alanine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Alanine" title="Alanine">Alanine</a> is produced by the transamination of one molecule of pyruvate using two alternate steps: 1) conversion of glutamate to α-ketoglutarate using a glutamate-alanine transaminase, and 2) conversion of valine to α-ketoisovalerate via Transaminase C. </p><p>Not much is known about the regulation of alanine synthesis. The only definite method is the bacterium's ability to repress Transaminase C activity by either valine or leucine (see <b><i>ilvEDA</i> operon</b>). Other than that, alanine biosynthesis does not seem to be regulated.<sup id="cite_ref-umbarger_18-0" class="reference"><a href="#cite_note-umbarger-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Valine">Valine</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=17" title="Edit section: Valine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p><a href="/wiki/Valine" title="Valine">Valine</a> is produced by a four-enzyme pathway. It begins with the condensation of two equivalents of pyruvate catalyzed by acetohydroxy acid synthase yielding α-acetolactate. The second step involves the NADPH<sup>+</sup>-dependent reduction of α-acetolactate and migration of methyl groups to produce α, β-dihydroxyisovalerate. This is <a href="/wiki/Catalyzed" class="mw-redirect" title="Catalyzed">catalyzed</a> by acetohydroxy isomeroreductase. The third step is the dehydration of α, β-dihydroxyisovalerate catalyzed by dihydroxy acid dehydrase. In the fourth and final step, the resulting α-ketoisovalerate undergoes transamination catalyzed either by an alanine-valine transaminase or a glutamate-valine transaminase. Valine biosynthesis is subject to feedback inhibition in the production of acetohydroxy acid synthase.<sup id="cite_ref-umbarger_18-1" class="reference"><a href="#cite_note-umbarger-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Leucine">Leucine</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=18" title="Edit section: Leucine"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The <a href="/wiki/Leucine" title="Leucine">leucine</a> synthesis pathway diverges from the valine pathway beginning with α-ketoisovalerate. α-Isopropylmalate synthase catalyzes this condensation with <a href="/wiki/Acetyl_CoA" class="mw-redirect" title="Acetyl CoA">acetyl CoA</a> to produce α-isopropylmalate. An isomerase converts α-isopropylmalate to β-isopropylmalate. The third step is the NAD<sup>+</sup>-dependent oxidation of β-isopropylmalate catalyzed by a dehydrogenase. The final step is the transamination of the α-ketoisocaproate by the action of a glutamate-leucine transaminase. </p><p>Leucine, like valine, regulates the first step of its pathway by inhibiting the action of the α-Isopropylmalate synthase.<sup id="cite_ref-umbarger_18-2" class="reference"><a href="#cite_note-umbarger-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> Because leucine is synthesized by a diversion from the valine synthetic pathway, the feedback inhibition of valine on its pathway also can inhibit the synthesis of leucine. </p> <div class="mw-heading mw-heading4"><h4 id="ilvEDA_operon">ilvEDA operon</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=19" title="Edit section: ilvEDA operon"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The genes that encode both the dihydroxy acid dehydrase used in the creation of α-ketoisovalerate and Transaminase E, as well as other enzymes are encoded on the ilvEDA operon. This operon is bound and inactivated by <a href="/wiki/Valine" title="Valine">valine</a>, <a href="/wiki/Leucine" title="Leucine">leucine</a>, and <a href="/wiki/Isoleucine" title="Isoleucine">isoleucine</a>. (Isoleucine is not a direct derivative of pyruvate, but is produced by the use of many of the same enzymes used to produce valine and, indirectly, leucine.) When one of these amino acids is limited, the gene furthest from the amino-acid binding site of this operon can be transcribed. When a second of these amino acids is limited, the next-closest gene to the binding site can be transcribed, and so forth.<sup id="cite_ref-umbarger_18-3" class="reference"><a href="#cite_note-umbarger-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Commercial_syntheses_of_amino_acids">Commercial syntheses of amino acids</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=20" title="Edit section: Commercial syntheses of amino acids"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The commercial production of amino acids usually relies on mutant bacteria that overproduce individual amino acids using glucose as a carbon source. Some amino acids are produced by enzymatic conversions of synthetic intermediates. <a href="/wiki/2-Aminothiazoline-4-carboxylic_acid" title="2-Aminothiazoline-4-carboxylic acid">2-Aminothiazoline-4-carboxylic acid</a> is an intermediate in the industrial synthesis of L-<a href="/wiki/Cysteine" title="Cysteine">cysteine</a> for example. <a href="/wiki/Aspartic_acid" title="Aspartic acid">Aspartic acid</a> is produced by the addition of ammonia to <a href="/wiki/Fumarate" class="mw-redirect" title="Fumarate">fumarate</a> using a lyase.<sup id="cite_ref-Ullmann_19-0" class="reference"><a href="#cite_note-Ullmann-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="References">References</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=21" 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-1"><span class="mw-cite-backlink"><b><a href="#cite_ref-1">^</a></b></span> <span class="reference-text"><style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#d33)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}</style><cite id="CITEREFAnnigan" class="citation web cs1">Annigan, Jan. <a rel="nofollow" class="external text" href="http://healthyeating.sfgate.com/many-amino-acids-body-require-6412.html">"How Many Amino Acids Does the Body Require?"</a>. <i>SFGate</i>. 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href="https://pubmed.ncbi.nlm.nih.gov/17321544">17321544</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+Molecular+Biology&rft.atitle=A+Novel+Two-domain+Architecture+Within+the+Amino+Acid+Kinase+Enzyme+Family+Revealed+by+the+Crystal+Structure+of+Escherichia+coli+Glutamate+5-kinase&rft.volume=367&rft.issue=5&rft.pages=%3Cspan+class%3D%22nowrap%22%3E1431-%3C%2Fspan%3E1446&rft.date=2007&rft_id=info%3Ahdl%2F10261%2F111016&rft_id=info%3Apmid%2F17321544&rft_id=info%3Adoi%2F10.1016%2Fj.jmb.2007.01.073&rft.aulast=Marco-Mar%C3%ADn&rft.aufirst=C&rft.au=Gil-Ortiz%2C+F&rft.au=P%C3%A9rez-Arellano%2C+I&rft.au=Cervera%2C+J&rft.au=Fita%2C+I&rft.au=Rubio%2C+V&rft_id=http%3A%2F%2Fhdl.handle.net%2F10261%2F111016&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid+synthesis" class="Z3988"></span></span> </li> <li id="cite_note-pmid1874410-5"><span class="mw-cite-backlink"><b><a 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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/1874410">1874410</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Genetics&rft.atitle=The+regulation+of+arginine+biosynthesis%3A+its+contribution+to+understanding+the+control+of+gene+expression&rft.volume=128&rft.issue=3&rft.pages=%3Cspan+class%3D%22nowrap%22%3E489-%3C%2Fspan%3E94&rft.date=1991&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC1204522%23id-name%3DPMC&rft_id=info%3Apmid%2F1874410&rft_id=info%3Adoi%2F10.1093%2Fgenetics%2F128.3.489&rft.au=Maas+WK&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC1204522&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid+synthesis" class="Z3988"></span></span> </li> <li id="cite_note-6"><span class="mw-cite-backlink"><b><a href="#cite_ref-6">^</a></b></span> <span 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New York: Worth Publishing. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/1-57259-153-6" title="Special:BookSources/1-57259-153-6"><bdi>1-57259-153-6</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Lehninger%2C+Principles+of+Biochemistry&rft.place=New+York&rft.edition=3rd&rft.pub=Worth+Publishing&rft.date=2000&rft.isbn=1-57259-153-6&rft.aulast=Nelson&rft.aufirst=DL&rft.au=Cox%2C+MM&rft_id=https%3A%2F%2Farchive.org%2Fdetails%2Flehningerprincip01lehn&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid+synthesis" class="Z3988"></span></span> </li> <li id="cite_note-:2-8"><span class="mw-cite-backlink">^ <a href="#cite_ref-:2_8-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-:2_8-1"><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="CITEREFKulis-HornPersickeKalinowski2014" class="citation journal cs1">Kulis-Horn, Robert K; Persicke, Marcus; Kalinowski, Jörn (2014-01-01). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3896937">"Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum"</a>. <i>Microbial Biotechnology</i>. <b>7</b> (1): <span class="nowrap">5–</span>25. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1111%2F1751-7915.12055">10.1111/1751-7915.12055</a>. <a href="/wiki/ISSN_(identifier)" class="mw-redirect" title="ISSN (identifier)">ISSN</a> <a rel="nofollow" class="external text" href="https://search.worldcat.org/issn/1751-7915">1751-7915</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/PMC3896937">3896937</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/23617600">23617600</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Microbial+Biotechnology&rft.atitle=Histidine+biosynthesis%2C+its+regulation+and+biotechnological+application+in+Corynebacterium+glutamicum&rft.volume=7&rft.issue=1&rft.pages=%3Cspan+class%3D%22nowrap%22%3E5-%3C%2Fspan%3E25&rft.date=2014-01-01&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3896937%23id-name%3DPMC&rft.issn=1751-7915&rft_id=info%3Apmid%2F23617600&rft_id=info%3Adoi%2F10.1111%2F1751-7915.12055&rft.aulast=Kulis-Horn&rft.aufirst=Robert+K&rft.au=Persicke%2C+Marcus&rft.au=Kalinowski%2C+J%C3%B6rn&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3896937&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid+synthesis" class="Z3988"></span></span> </li> <li id="cite_note-9"><span class="mw-cite-backlink"><b><a href="#cite_ref-9">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFAdams1955" class="citation journal cs1">Adams, E. 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"Methionine biosynthesis". In Wendisch VF (ed.). <i>Amino acid biosynthesis: pathways, regulation, and metabolic engineering</i>. Berlin: Springer. pp. <span class="nowrap">206–</span>208. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-3540485957" title="Special:BookSources/978-3540485957"><bdi>978-3540485957</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Methionine+biosynthesis&rft.btitle=Amino+acid+biosynthesis%3A+pathways%2C+regulation%2C+and+metabolic+engineering&rft.place=Berlin&rft.pages=%3Cspan+class%3D%22nowrap%22%3E206-%3C%2Fspan%3E208&rft.pub=Springer&rft.date=2007&rft.isbn=978-3540485957&rft.au=Figge+RM&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid+synthesis" class="Z3988"></span></span> </li> <li id="cite_note-umbarger-18"><span class="mw-cite-backlink">^ <a href="#cite_ref-umbarger_18-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-umbarger_18-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-umbarger_18-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-umbarger_18-3"><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="CITEREFUmbarger_HE1978" class="citation journal cs1">Umbarger HE (1978). "Amino Acid Biosynthesis and its Regulation". <i>Annual Review of Biochemistry</i>. <b>47</b>: <span class="nowrap">533–</span>606. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1146%2Fannurev.bi.47.070178.002533">10.1146/annurev.bi.47.070178.002533</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/354503">354503</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Annual+Review+of+Biochemistry&rft.atitle=Amino+Acid+Biosynthesis+and+its+Regulation&rft.volume=47&rft.pages=%3Cspan+class%3D%22nowrap%22%3E533-%3C%2Fspan%3E606&rft.date=1978&rft_id=info%3Adoi%2F10.1146%2Fannurev.bi.47.070178.002533&rft_id=info%3Apmid%2F354503&rft.au=Umbarger+HE&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid+synthesis" class="Z3988"></span></span> </li> <li id="cite_note-Ullmann-19"><span class="mw-cite-backlink"><b><a href="#cite_ref-Ullmann_19-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFDrauzGraysonKleemannKrimmer2006" class="citation encyclopaedia cs1">Drauz, Karlheinz; Grayson, Ian; Kleemann, Axel; Krimmer, Hans-Peter; Leuchtenberger, Wolfgang; Weckbecker, Christoph (2006). <i><a href="/wiki/Ullmann%27s_Encyclopedia_of_Industrial_Chemistry" title="Ullmann's Encyclopedia of Industrial Chemistry">Ullmann's Encyclopedia of Industrial Chemistry</a></i>. Weinheim: Wiley-VCH. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2F14356007.a02_057.pub2">10.1002/14356007.a02_057.pub2</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-3-527-30673-2" title="Special:BookSources/978-3-527-30673-2"><bdi>978-3-527-30673-2</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Ullmann%27s+Encyclopedia+of+Industrial+Chemistry&rft.place=Weinheim&rft.pub=Wiley-VCH&rft.date=2006&rft_id=info%3Adoi%2F10.1002%2F14356007.a02_057.pub2&rft.isbn=978-3-527-30673-2&rft.aulast=Drauz&rft.aufirst=Karlheinz&rft.au=Grayson%2C+Ian&rft.au=Kleemann%2C+Axel&rft.au=Krimmer%2C+Hans-Peter&rft.au=Leuchtenberger%2C+Wolfgang&rft.au=Weckbecker%2C+Christoph&rfr_id=info%3Asid%2Fen.wikipedia.org%3AAmino+acid+synthesis" class="Z3988"></span></span> </li> </ol></div></div> <div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Amino_acid_synthesis&action=edit&section=22" title="Edit section: External links"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/books/bv.fcgi?rid=stryer.TOC&depth=2">NCBI Bookshelf Free Textbook Access</a></li></ul> <div class="navbox-styles"><style data-mw-deduplicate="TemplateStyles:r1129693374">.mw-parser-output .hlist dl,.mw-parser-output .hlist ol,.mw-parser-output .hlist ul{margin:0;padding:0}.mw-parser-output .hlist dd,.mw-parser-output .hlist dt,.mw-parser-output .hlist li{margin:0;display:inline}.mw-parser-output .hlist.inline,.mw-parser-output .hlist.inline dl,.mw-parser-output .hlist.inline ol,.mw-parser-output .hlist.inline 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biology">Central dogma</a> <ul><li><a href="/wiki/DNA" title="DNA">DNA</a> → <a href="/wiki/Messenger_RNA" title="Messenger RNA">RNA</a> → <a href="/wiki/Protein" title="Protein">Protein</a></li></ul></li> <li><a href="/wiki/Central_dogma_of_molecular_biology#Special_transfers_of_biological_sequential_information" title="Central dogma of molecular biology">Special transfers</a> <ul><li><a href="/wiki/RNA-dependent_RNA_polymerase" title="RNA-dependent RNA polymerase">RNA→RNA</a></li> <li><a href="/wiki/Reverse_transcription" class="mw-redirect" title="Reverse transcription">RNA→DNA</a></li> <li><a href="/wiki/Prion" title="Prion">Protein→Protein</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Transcription_(biology)" title="Transcription (biology)">Transcription</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:8.0em;font-weight: normal;">Types</th><td class="navbox-list-with-group navbox-list navbox-even" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Bacterial_transcription" title="Bacterial transcription">Bacterial</a></li> <li><a href="/wiki/Archaeal_transcription" title="Archaeal transcription">Archaeal</a></li> <li><a href="/wiki/Eukaryotic_transcription" title="Eukaryotic transcription">Eukaryotic</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:8.0em;font-weight: normal;">Key elements</th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Transcription_factor" title="Transcription factor">Transcription factor</a></li> <li><a href="/wiki/RNA_polymerase" title="RNA polymerase">RNA polymerase</a></li> <li><a href="/wiki/Promoter_(genetics)" title="Promoter (genetics)">Promoter</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:8.0em;font-weight: normal;"><a href="/wiki/Post-transcriptional_modification" title="Post-transcriptional modification">Post-transcription</a></th><td class="navbox-list-with-group navbox-list navbox-even" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Primary_transcript" title="Primary transcript">Precursor mRNA (pre-mRNA / hnRNA)</a></li> <li><a href="/wiki/Five-prime_cap" title="Five-prime cap">5' capping</a></li> <li><a href="/wiki/RNA_splicing" title="RNA splicing">Splicing</a></li> <li><a href="/wiki/Polyadenylation" title="Polyadenylation">Polyadenylation</a></li> <li><a href="/wiki/Histone_acetylation_and_deacetylation" title="Histone acetylation and deacetylation">Histone acetylation and deacetylation</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Translation_(biology)" title="Translation (biology)">Translation</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:8.0em;font-weight: normal;">Types</th><td class="navbox-list-with-group navbox-list navbox-odd" style="padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Bacterial_translation" title="Bacterial translation">Bacterial</a></li> <li><a href="/wiki/Archaeal_translation" title="Archaeal translation">Archaeal</a></li> <li><a href="/wiki/Eukaryotic_translation" title="Eukaryotic translation">Eukaryotic</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:8.0em;font-weight: normal;">Key elements</th><td class="navbox-list-with-group navbox-list navbox-even" style="padding:0;white-space:nowrap;"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Ribosome" title="Ribosome">Ribosome</a></li> <li><a href="/wiki/Transfer_RNA" title="Transfer RNA">Transfer RNA (tRNA)</a></li> <li><a href="/wiki/Ribosome-nascent_chain_complex" title="Ribosome-nascent chain complex">Ribosome-nascent chain complex (RNC)</a></li> <li><a href="/wiki/Post-translational_modification" title="Post-translational modification">Post-translational modification</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Regulation_of_gene_expression" title="Regulation of gene expression">Regulation</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/Epigenetics" title="Epigenetics">Epigenetic</a> <ul><li><a href="/wiki/Genomic_imprinting" title="Genomic imprinting">imprinting</a></li></ul></li> <li><a href="/wiki/Transcriptional_regulation" title="Transcriptional regulation">Transcriptional</a> <ul><li><a href="/wiki/Gene_regulatory_network" title="Gene regulatory network">Gene regulatory network</a></li> <li><a href="/wiki/Cis-regulatory_element" title="Cis-regulatory element">cis-regulatory element</a></li></ul></li> <li><a href="/wiki/Lac_operon" title="Lac operon">lac operon</a></li> <li><a href="/wiki/Post-transcriptional_regulation" title="Post-transcriptional regulation">Post-transcriptional</a> <ul><li><a href="/wiki/P-bodies" title="P-bodies">sequestration (P-bodies)</a></li> <li><a href="/wiki/Alternative_splicing" title="Alternative splicing">alternative splicing</a></li> <li><a href="/wiki/MicroRNA" title="MicroRNA">microRNA</a></li></ul></li> <li><a href="/wiki/Translational_regulation" title="Translational regulation">Translational</a></li> <li><a href="/wiki/Post-translational_regulation" title="Post-translational regulation">Post-translational</a> <ul><li><a href="/wiki/Phosphorylation" title="Phosphorylation">reversible</a></li> <li><a href="/wiki/Proteolysis" title="Proteolysis">irreversible</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Influential people</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/Fran%C3%A7ois_Jacob" title="François Jacob">François Jacob</a></li> <li><a href="/wiki/Jacques_Monod" title="Jacques Monod">Jacques Monod</a></li></ul> </div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235"></div><div role="navigation" class="navbox" aria-labelledby="Metabolism,_catabolism,_anabolism113" 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:Metabolism" title="Template:Metabolism"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Metabolism" title="Template talk:Metabolism"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Metabolism" title="Special:EditPage/Template:Metabolism"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Metabolism,_catabolism,_anabolism113" style="font-size:114%;margin:0 4em"><a href="/wiki/Metabolism" title="Metabolism">Metabolism</a>, <a href="/wiki/Catabolism" title="Catabolism">catabolism</a>, <a href="/wiki/Anabolism" title="Anabolism">anabolism</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">General</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Metabolic_pathway" title="Metabolic pathway">Metabolic pathway</a></li> <li><a href="/wiki/Metabolic_network" title="Metabolic network">Metabolic network</a></li> <li><a href="/wiki/Primary_nutritional_groups" title="Primary nutritional groups">Primary nutritional groups</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Bioenergetics" title="Bioenergetics">Energy<br /> metabolism</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Aerobic_respiration" class="mw-redirect" title="Aerobic respiration">Aerobic respiration</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/Glycolysis" title="Glycolysis">Glycolysis</a> → <a href="/wiki/Pyruvate_dehydrogenase" title="Pyruvate dehydrogenase">Pyruvate decarboxylation</a> → <a href="/wiki/Citric_acid_cycle" title="Citric acid cycle">Citric acid cycle</a> → <a href="/wiki/Oxidative_phosphorylation" title="Oxidative phosphorylation">Oxidative phosphorylation</a> (<span style="font-size:85%;"><a href="/wiki/Electron_transport_chain" title="Electron transport chain">electron transport chain</a> + <a href="/wiki/ATP_synthase" title="ATP synthase">ATP synthase</a></span>)</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Anaerobic_respiration" title="Anaerobic respiration">Anaerobic respiration</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>Electron acceptors other than oxygen</li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Fermentation" title="Fermentation">Fermentation</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/Glycolysis" title="Glycolysis">Glycolysis</a> → <a href="/wiki/Substrate-level_phosphorylation" title="Substrate-level phosphorylation">Substrate-level phosphorylation</a> <ul><li><a href="/wiki/Acetone%E2%80%93butanol%E2%80%93ethanol_fermentation" title="Acetone–butanol–ethanol fermentation">ABE</a></li> <li><a href="/wiki/Ethanol_fermentation" title="Ethanol fermentation">Ethanol</a></li> <li><a href="/wiki/Lactic_acid_fermentation" title="Lactic acid fermentation">Lactic acid</a></li></ul></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Specific<br /> paths</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Protein_metabolism" title="Protein metabolism">Protein metabolism</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/Protein_biosynthesis" title="Protein biosynthesis">Protein synthesis</a></li> <li><a href="/wiki/Protein_catabolism" title="Protein catabolism">Catabolism</a> (protein→peptide→amino acid)</li></ul> </div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Amino_acid" title="Amino acid">Amino acid</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 class="mw-selflink selflink">Amino acid synthesis</a></li> <li><a href="/wiki/Protein_catabolism#Amino_acid_degradation" title="Protein catabolism">Amino acid degradation</a> (amino acid→pyruvate, acetyl CoA, or TCA intermediate)</li> <li><a href="/wiki/Urea_cycle" title="Urea cycle">Urea cycle</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Nucleic_acid_metabolism" title="Nucleic acid metabolism">Nucleotide<br /> metabolism</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/Purine_metabolism" title="Purine metabolism">Purine metabolism</a></li> <li><a href="/wiki/Nucleotide_salvage" title="Nucleotide salvage">Nucleotide salvage</a></li> <li><a href="/wiki/Pyrimidine_metabolism" title="Pyrimidine metabolism">Pyrimidine metabolism</a></li> <li><a href="/wiki/Purine_nucleotide_cycle" title="Purine nucleotide cycle">Purine nucleotide cycle</a></li></ul> </div></td></tr></tbody></table><div> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Carbohydrate_metabolism" title="Carbohydrate metabolism">Carbohydrate metabolism</a><br />(<a href="/wiki/Carbohydrate_catabolism" title="Carbohydrate catabolism">carbohydrate catabolism</a><br />and <a href="/wiki/Anabolism" title="Anabolism">anabolism</a>)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%">Human</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><td colspan="2" class="navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Glycolysis" title="Glycolysis">Glycolysis</a> ⇄ <a href="/wiki/Gluconeogenesis" title="Gluconeogenesis">Gluconeogenesis</a></li></ul> </div></td></tr><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Glycogenolysis" title="Glycogenolysis">Glycogenolysis</a> ⇄ <a href="/wiki/Glycogenesis" title="Glycogenesis">Glycogenesis</a></li></ul> </div></td></tr><tr><td colspan="2" class="navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Pentose_phosphate_pathway" title="Pentose phosphate pathway">Pentose phosphate pathway</a></li> <li><a href="/wiki/Fructolysis" title="Fructolysis">Fructolysis</a> <ul><li><a href="/wiki/Polyol_pathway" title="Polyol pathway">Polyol pathway</a></li></ul></li> <li><a href="/wiki/Galactolysis" title="Galactolysis">Galactolysis</a> <ul><li><a href="/wiki/Leloir_pathway" title="Leloir pathway">Leloir pathway</a></li></ul></li></ul> </div></td></tr><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Glycosylation" title="Glycosylation">Glycosylation</a> <ul><li><a href="/wiki/N-linked_glycosylation" title="N-linked glycosylation">N-linked</a></li> <li><a href="/wiki/O-linked_glycosylation" title="O-linked glycosylation">O-linked</a></li></ul></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Nonhuman</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><td colspan="2" class="navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Photosynthesis" title="Photosynthesis">Photosynthesis</a></li> <li><a href="/wiki/Anoxygenic_photosynthesis" title="Anoxygenic photosynthesis">Anoxygenic photosynthesis</a></li> <li><a href="/wiki/Chemosynthesis" title="Chemosynthesis">Chemosynthesis</a></li> <li><a href="/wiki/Carbon_fixation" class="mw-redirect" title="Carbon fixation">Carbon fixation</a></li> <li><a href="/w/index.php?title=DeLey-Doudoroff_pathway&action=edit&redlink=1" class="new" title="DeLey-Doudoroff pathway (page does not exist)">DeLey-Doudoroff pathway</a></li> <li><a href="/wiki/Entner-Doudoroff_pathway" class="mw-redirect" title="Entner-Doudoroff pathway">Entner-Doudoroff pathway</a></li></ul> </div></td></tr><tr><td colspan="2" class="navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Xylose_metabolism" title="Xylose metabolism">Xylose metabolism</a></li> <li><a href="/wiki/Radiotrophic_fungus" title="Radiotrophic fungus">Radiotrophism</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Lipid_metabolism" title="Lipid metabolism">Lipid metabolism</a> <br />(<a href="/wiki/Lipolysis" title="Lipolysis">lipolysis</a>, <a href="/wiki/Lipogenesis" title="Lipogenesis">lipogenesis</a>)</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Fatty_acid_metabolism" title="Fatty acid metabolism">Fatty acid metabolism</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/Fatty_acid_degradation" title="Fatty acid degradation">Fatty acid degradation</a> (<a href="/wiki/Beta_oxidation" title="Beta oxidation">Beta oxidation</a>)</li> <li><a href="/wiki/Fatty_acid_synthesis" title="Fatty acid synthesis">Fatty acid synthesis</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Steroid" title="Steroid">Steroid metabolism</a></li> <li><a href="/wiki/Sphingolipid_metabolism" class="mw-redirect" title="Sphingolipid metabolism">Sphingolipid metabolism</a></li> <li><a href="/wiki/Eicosanoid_metabolism" class="mw-redirect" title="Eicosanoid metabolism">Eicosanoid metabolism</a></li> <li><a href="/wiki/Ketosis" title="Ketosis">Ketosis</a></li> <li><a href="/wiki/Reverse_cholesterol_transport" title="Reverse cholesterol transport">Reverse cholesterol transport</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Bioinorganic_chemistry" title="Bioinorganic chemistry">Metal metabolism</a> <ul><li><a href="/wiki/Human_iron_metabolism" title="Human iron metabolism">Iron metabolism</a></li></ul></li> <li><a href="/wiki/Ethanol_metabolism" class="mw-redirect" title="Ethanol metabolism">Ethanol metabolism</a></li> <li><a href="/wiki/Phosphagen" title="Phosphagen">Phospagen system (ATP-PCr)</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235"></div><div role="navigation" class="navbox" aria-labelledby="Metabolism:_Protein_metabolism,_synthesis_and_catabolism_enzymes216" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239400231"><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Amino_acid_metabolism_enzymes" title="Template:Amino acid metabolism enzymes"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Amino_acid_metabolism_enzymes" title="Template talk:Amino acid metabolism enzymes"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Amino_acid_metabolism_enzymes" title="Special:EditPage/Template:Amino acid metabolism enzymes"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Metabolism:_Protein_metabolism,_synthesis_and_catabolism_enzymes216" style="font-size:114%;margin:0 4em"><a href="/wiki/Metabolism" title="Metabolism">Metabolism</a>: <a href="/wiki/Protein_metabolism" title="Protein metabolism">Protein metabolism</a>, <a class="mw-selflink selflink">synthesis</a> and catabolism <a href="/wiki/Enzyme" title="Enzyme">enzymes</a></div></th></tr><tr><td class="navbox-abovebelow" colspan="2"><div><i><a href="/wiki/Essential_amino_acid" title="Essential amino acid">Essential amino acids</a> are in Capitals</i></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Ketogenic_amino_acid" title="Ketogenic amino acid">K</a>→<a href="/wiki/Acetyl-CoA" title="Acetyl-CoA">acetyl-CoA</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Lysine" title="Lysine">LYSINE</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Saccharopine_dehydrogenase" title="Saccharopine dehydrogenase">Saccharopine dehydrogenase</a></li> <li><a href="/wiki/Glutaryl-CoA_dehydrogenase" title="Glutaryl-CoA dehydrogenase">Glutaryl-CoA dehydrogenase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Leucine" title="Leucine">LEUCINE</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/3-Hydroxybutyryl-CoA_dehydrogenase" title="3-Hydroxybutyryl-CoA dehydrogenase">3-Hydroxybutyryl-CoA dehydrogenase</a></li> <li><a href="/wiki/Branched-chain_amino_acid_aminotransferase" title="Branched-chain amino acid aminotransferase">Branched-chain amino acid aminotransferase</a></li> <li><a href="/wiki/Branched-chain_alpha-keto_acid_dehydrogenase_complex" title="Branched-chain alpha-keto acid dehydrogenase complex">Branched-chain alpha-keto acid dehydrogenase complex</a></li> <li><a href="/wiki/Enoyl-CoA_hydratase" title="Enoyl-CoA hydratase">Enoyl-CoA hydratase</a></li> <li><a href="/wiki/3-hydroxy-3-methylglutaryl-CoA_lyase" class="mw-redirect" title="3-hydroxy-3-methylglutaryl-CoA lyase">HMG-CoA lyase</a></li> <li><a href="/wiki/HMG-CoA_reductase" title="HMG-CoA reductase">HMG-CoA reductase</a></li> <li><a href="/wiki/Isovaleryl_coenzyme_A_dehydrogenase" class="mw-redirect" title="Isovaleryl coenzyme A dehydrogenase">Isovaleryl coenzyme A dehydrogenase</a></li> <li><a href="/wiki/%CE%91-ketoisocaproate_dioxygenase" class="mw-redirect" title="Α-ketoisocaproate dioxygenase">α-Ketoisocaproate dioxygenase</a></li> <li><a href="/wiki/Leucine_2,3-aminomutase" title="Leucine 2,3-aminomutase">Leucine 2,3-aminomutase</a></li> <li><a href="/wiki/Methylcrotonyl-CoA_carboxylase" title="Methylcrotonyl-CoA carboxylase">Methylcrotonyl-CoA carboxylase</a></li> <li><a href="/wiki/Methylglutaconyl-CoA_hydratase" title="Methylglutaconyl-CoA hydratase">Methylglutaconyl-CoA hydratase</a></li></ul> <p>(See <a href="/wiki/Template:Leucine_metabolism_in_humans" title="Template:Leucine metabolism in humans">Template:Leucine metabolism in humans</a> – this diagram does not include the pathway for β-leucine synthesis via leucine 2,3-aminomutase) </p> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Tryptophan" title="Tryptophan">TRYPTOPHAN</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Indoleamine_2,3-dioxygenase" title="Indoleamine 2,3-dioxygenase">Indoleamine 2,3-dioxygenase</a>/<a href="/wiki/Tryptophan_2,3-dioxygenase" title="Tryptophan 2,3-dioxygenase">Tryptophan 2,3-dioxygenase</a></li> <li><a href="/wiki/Arylformamidase" title="Arylformamidase">Arylformamidase</a></li> <li><a href="/wiki/Kynureninase" title="Kynureninase">Kynureninase</a></li> <li><a href="/wiki/3-hydroxyanthranilate_oxidase" title="3-hydroxyanthranilate oxidase">3-hydroxyanthranilate oxidase</a></li> <li><a href="/wiki/Aminocarboxymuconate-semialdehyde_decarboxylase" title="Aminocarboxymuconate-semialdehyde decarboxylase">Aminocarboxymuconate-semialdehyde decarboxylase</a></li> <li><a href="/wiki/Aminomuconate-semialdehyde_dehydrogenase" title="Aminomuconate-semialdehyde dehydrogenase">Aminomuconate-semialdehyde dehydrogenase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Phenylalanine" title="Phenylalanine">PHENYLALANINE</a>→<a href="/wiki/Tyrosine" title="Tyrosine">tyrosine</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li>(see below)</li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Glucogenic_amino_acid" title="Glucogenic amino acid">G</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th id="G→pyruvate→citrate205" scope="row" class="navbox-group" style="width:1%">G→<a href="/wiki/Pyruvate" class="mw-redirect" title="Pyruvate">pyruvate</a><br />→<a href="/wiki/Citrate" class="mw-redirect" title="Citrate">citrate</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Glycine" title="Glycine">glycine</a>→<a href="/wiki/Serine" title="Serine">serine</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Serine_hydroxymethyltransferase" title="Serine hydroxymethyltransferase">Serine hydroxymethyltransferase</a></li> <li><a href="/wiki/Serine_dehydratase" title="Serine dehydratase">Serine dehydratase</a></li></ul> <ul><li><a href="/wiki/Glycine" title="Glycine">glycine</a>→<a href="/wiki/Creatine" title="Creatine">creatine</a>: <a href="/wiki/Guanidinoacetate_N-methyltransferase" title="Guanidinoacetate N-methyltransferase">Guanidinoacetate N-methyltransferase</a></li> <li><a href="/wiki/Creatine_kinase" title="Creatine kinase">Creatine kinase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Alanine" title="Alanine">alanine</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Alanine_transaminase" title="Alanine transaminase">Alanine transaminase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Cysteine" title="Cysteine">cysteine</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/D-cysteine_desulfhydrase" title="D-cysteine desulfhydrase">D-cysteine desulfhydrase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Threonine" title="Threonine">threonine</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/L-threonine_dehydrogenase" class="mw-redirect" title="L-threonine dehydrogenase">L-threonine dehydrogenase</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">G→<a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a>→<br /><a href="/wiki/Alpha-Ketoglutaric_acid" class="mw-redirect" title="Alpha-Ketoglutaric acid">α-ketoglutarate</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Histidine" title="Histidine">HISTIDINE</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Histidine_ammonia-lyase" title="Histidine ammonia-lyase">Histidine ammonia-lyase</a></li> <li><a href="/wiki/Urocanase" title="Urocanase">Urocanate hydratase</a></li> <li><a href="/wiki/Formiminotransferase_cyclodeaminase" class="mw-redirect" title="Formiminotransferase cyclodeaminase">Formiminotransferase cyclodeaminase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Proline" title="Proline">proline</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Proline_oxidase" title="Proline oxidase">Proline oxidase</a></li> <li><a href="/wiki/Pyrroline-5-carboxylate_reductase" title="Pyrroline-5-carboxylate reductase">Pyrroline-5-carboxylate reductase</a></li> <li><a href="/wiki/1-Pyrroline-5-carboxylate_dehydrogenase" title="1-Pyrroline-5-carboxylate dehydrogenase">1-Pyrroline-5-carboxylate dehydrogenase</a>/<a href="/wiki/Aldehyde_dehydrogenase_4_family,_member_A1" title="Aldehyde dehydrogenase 4 family, member A1">ALDH4A1</a></li> <li><a href="/wiki/PYCR1" title="PYCR1">PYCR1</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Arginine" title="Arginine">arginine</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Ornithine_aminotransferase" title="Ornithine aminotransferase">Ornithine aminotransferase</a></li> <li><a href="/wiki/Ornithine_decarboxylase" title="Ornithine decarboxylase">Ornithine decarboxylase</a></li> <li><a href="/wiki/Agmatinase" title="Agmatinase">Agmatinase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">→<a href="/wiki/Alpha-ketoglutarate" class="mw-redirect" title="Alpha-ketoglutarate">alpha-ketoglutarate</a>→TCA</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Glutamate_dehydrogenase" title="Glutamate dehydrogenase">Glutamate dehydrogenase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Other</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Cysteine" title="Cysteine">cysteine</a>+<a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a>→<a href="/wiki/Glutathione" title="Glutathione">glutathione</a>: <a href="/wiki/Gamma-glutamylcysteine_synthetase" class="mw-redirect" title="Gamma-glutamylcysteine synthetase">Gamma-glutamylcysteine synthetase</a></li> <li><a href="/wiki/Glutathione_synthetase" title="Glutathione synthetase">Glutathione synthetase</a></li> <li><a href="/wiki/Gamma-glutamyl_transpeptidase" class="mw-redirect" title="Gamma-glutamyl transpeptidase">Gamma-glutamyl transpeptidase</a></li></ul> <ul><li><a href="/wiki/Glutamate" class="mw-redirect" title="Glutamate">glutamate</a>→<a href="/wiki/Glutamine" title="Glutamine">glutamine</a>: <a href="/wiki/Glutamine_synthetase" title="Glutamine synthetase">Glutamine synthetase</a></li> <li><a href="/wiki/Glutaminase" title="Glutaminase">Glutaminase</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">G→<a href="/wiki/Propionyl-CoA" title="Propionyl-CoA">propionyl-CoA</a>→<br /><a href="/wiki/Succinyl-CoA" title="Succinyl-CoA">succinyl-CoA</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Valine" title="Valine">VALINE</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Branched-chain_amino_acid_aminotransferase" title="Branched-chain amino acid aminotransferase">Branched-chain amino acid aminotransferase</a></li> <li><a href="/wiki/Branched-chain_alpha-keto_acid_dehydrogenase_complex" title="Branched-chain alpha-keto acid dehydrogenase complex">Branched-chain alpha-keto acid dehydrogenase complex</a></li> <li><a href="/wiki/Enoyl-CoA_hydratase" title="Enoyl-CoA hydratase">Enoyl-CoA hydratase</a></li> <li><a href="/wiki/3-hydroxyisobutyryl-CoA_hydrolase" title="3-hydroxyisobutyryl-CoA hydrolase">3-hydroxyisobutyryl-CoA hydrolase</a></li> <li><a href="/wiki/3-hydroxyisobutyrate_dehydrogenase" title="3-hydroxyisobutyrate dehydrogenase">3-hydroxyisobutyrate dehydrogenase</a></li> <li><a href="/wiki/Methylmalonate-semialdehyde_dehydrogenase_(acylating)" title="Methylmalonate-semialdehyde dehydrogenase (acylating)">Methylmalonate semialdehyde dehydrogenase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Isoleucine" title="Isoleucine">ISOLEUCINE</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Branched-chain_amino_acid_aminotransferase" title="Branched-chain amino acid aminotransferase">Branched-chain amino acid aminotransferase</a></li> <li><a href="/wiki/Branched-chain_alpha-keto_acid_dehydrogenase_complex" title="Branched-chain alpha-keto acid dehydrogenase complex">Branched-chain alpha-keto acid dehydrogenase complex</a></li> <li><a href="/wiki/3-hydroxy-2-methylbutyryl-CoA_dehydrogenase" title="3-hydroxy-2-methylbutyryl-CoA dehydrogenase">3-hydroxy-2-methylbutyryl-CoA dehydrogenase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Methionine" title="Methionine">METHIONINE</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><i><a href="/wiki/Methionine#Generation_of_homocysteine" title="Methionine">generation of homocysteine</a>:</i> <a href="/wiki/Methionine_adenosyltransferase" class="mw-redirect" title="Methionine adenosyltransferase">Methionine adenosyltransferase</a></li> <li><a href="/wiki/Adenosylhomocysteinase" title="Adenosylhomocysteinase">Adenosylhomocysteinase</a></li></ul> <ul><li><i><a href="/wiki/Methionine#Regeneration_of_methionine" title="Methionine">regeneration of methionine</a>:</i> <a href="/wiki/Methionine_synthase" title="Methionine synthase">Methionine synthase</a>/<a href="/wiki/Methionine_synthase" title="Methionine synthase">Homocysteine methyltransferase</a></li> <li><a href="/wiki/Betaine-homocysteine_S-methyltransferase" class="mw-redirect" title="Betaine-homocysteine S-methyltransferase">Betaine-homocysteine methyltransferase</a></li></ul> <ul><li><i><a href="/wiki/Methionine#Conversion_to_cysteine" title="Methionine">conversion to cysteine</a>:</i> <a href="/wiki/Cystathionine_beta_synthase" title="Cystathionine beta synthase">Cystathionine beta synthase</a></li> <li><a href="/wiki/Cystathionine_gamma-lyase" title="Cystathionine gamma-lyase">Cystathionine gamma-lyase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Threonine" title="Threonine">THREONINE</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Threonine_aldolase" title="Threonine aldolase">Threonine aldolase</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">→<a href="/wiki/Succinyl-CoA" title="Succinyl-CoA">succinyl-CoA</a>→TCA</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Propionyl-CoA_carboxylase" title="Propionyl-CoA carboxylase">Propionyl-CoA carboxylase</a></li> <li><a href="/wiki/Methylmalonyl_CoA_epimerase" title="Methylmalonyl CoA epimerase">Methylmalonyl CoA epimerase</a></li> <li><a href="/wiki/Methylmalonyl-CoA_mutase" title="Methylmalonyl-CoA mutase">Methylmalonyl-CoA mutase</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">G→<a href="/wiki/Fumarate" class="mw-redirect" title="Fumarate">fumarate</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Phenylalanine" title="Phenylalanine">PHENYLALANINE</a>→<a href="/wiki/Tyrosine" title="Tyrosine">tyrosine</a>→</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Phenylalanine_hydroxylase" title="Phenylalanine hydroxylase">Phenylalanine hydroxylase</a></li> <li><a href="/wiki/Tyrosine_aminotransferase" title="Tyrosine aminotransferase">Tyrosine aminotransferase</a></li> <li><a href="/wiki/4-Hydroxyphenylpyruvate_dioxygenase" title="4-Hydroxyphenylpyruvate dioxygenase">4-Hydroxyphenylpyruvate dioxygenase</a></li> <li><a href="/wiki/Homogentisate_1,2-dioxygenase" title="Homogentisate 1,2-dioxygenase">Homogentisate 1,2-dioxygenase</a></li> <li><a href="/wiki/Fumarylacetoacetate_hydrolase" title="Fumarylacetoacetate hydrolase">Fumarylacetoacetate hydrolase</a></li></ul> <ul><li><a href="/wiki/Tyrosine" title="Tyrosine">tyrosine</a>→<a href="/wiki/Melanin" title="Melanin">melanin</a>: <a href="/wiki/Tyrosinase" title="Tyrosinase">Tyrosinase</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">G→<a href="/wiki/Oxaloacetic_acid" title="Oxaloacetic acid">oxaloacetate</a></th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Asparagine" title="Asparagine">asparagine</a>→<a href="/wiki/Aspartate" class="mw-redirect" title="Aspartate">aspartate</a>→</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Asparaginase" title="Asparaginase">Asparaginase</a>/<a href="/wiki/Asparagine_synthetase" title="Asparagine synthetase">Asparagine synthetase</a></li> <li><a href="/wiki/Aspartate_transaminase" title="Aspartate transaminase">Aspartate transaminase</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr></tbody></table><div></div></td></tr></tbody></table></div>    </div><noscript><img src="https://login.wikimedia.org/wiki/Special:CentralAutoLogin/start?useformat=desktop&type=1x1&usesul3=0" alt="" width="1" height="1" style="border: none; position: absolute;"></noscript> <div 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