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α-Aminoadipate pathway
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<h2 id="pathway-overview">Pathway overview</h2> <p>This pathway is a part of the glutamate family of amino acid biosynthetic pathways.<a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> The reaction steps in the pathway are similar to the <a href="/facts/Citric_acid_cycle/EGJL9NXP">citric acid cycle</a>. </p><p>The first step in the pathway is condensation of <a href="/facts/Acetyl-CoA/XyxFfC84">acetyl-CoA</a> with <a href="/facts/%25CE%2591-ketoglutarate/t5gJPVzB">α-ketoglutarate</a>, which gives <a href="/facts/Homocitrate/LjDUNcu5">homocitrate</a>. This reaction is catalyzed by <a href="/facts/Homocitrate_synthase/uHmxpJec">homocitrate synthase</a>. Homocitrate is then converted to <a href="/facts/Homoaconitate/33ASjTDQ">homoaconitate</a> by <a href="/facts/Homoaconitate_hydratase/xzm3PdWb">homoaconitase</a> and then to <a href="/facts/Homoisocitrate/XspAE1D3">homoisocitrate</a>. This is then <a href="/facts/Decarboxylation/Uugc18fz">decarboxylated</a> by <a href="/facts/Homoisocitrate_dehydrogenase/t82cH44e">homoisocitrate dehydrogenase</a>, which results in <a href="/facts/2-ketoadipate/DS5JU7C8">α-ketoadipate</a>. A nitrogen atom is added from glutamate by <a href="/facts/Aminoadipate_aminotransferase/HThsg003">aminoadipate aminotransferase</a> to form the <a href="/facts/%25CE%2591-aminoadipate/yFKgJE1G">α-aminoadipate</a>, from which this pathway gets its name. This is then reduced by <a href="/facts/L-aminoadipate-semialdehyde_dehydrogenase/tJSWtKsB">aminoadipate reductase</a> via an acyl-enzyme intermediate to a semialdehyde. Reaction with <a href="/facts/Glutamate/7oXbNcvu">glutamate</a> by one class of <a href="/facts/Saccharopine_dehydrogenase/9W6WS4FH">saccharopine dehydrogenase</a> yields <a href="/facts/Saccharopine/3BaouPHT">saccharopine</a> which is then cleaved by a second saccharopine dehydrogenase to yield lysine and oxoglutarate.<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> </p><p>Conversion of lysine to α-ketoadipate during degradation of lysine proceeds via the same steps, but in reverse.<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> </p> <h2 id="see-also">See also</h2> <ul><li><a href="/facts/Adipic_acid/8l8ahlDC">Adipic acid</a></li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Zabriskie TM, Jackson MD (2000). "Lysine biosynthesis and metabolism in fungi". Natural Product Reports. 17 (1): 85–97. doi:10.1039/a801345d. PMID 10714900. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Xu H, Andi B, Qian J, West AH, Cook PF (2006). "The alpha-aminoadipate pathway for lysine biosynthesis in fungi". Cell Biochemistry and Biophysics. 46 (1): 43–64. doi:10.1385/CBB:46:1:43. PMID 16943623. S2CID 22370361. <a href="/wiki/Cell_Biochemistry_and_Biophysics" target="_blank">/wiki/Cell_Biochemistry_and_Biophysics</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>Andi B, West AH, Cook PF (September 2004). "Kinetic mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae". Biochemistry. 43 (37): 11790–11795. doi:10.1021/bi048766p. PMID 15362863. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>Bhattacharjee JK (1985). "alpha-Aminoadipate pathway for the biosynthesis of lysine in lower eukaryotes". Critical Reviews in Microbiology. 12 (2): 131–151. doi:10.3109/10408418509104427. PMID 3928261. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Bhattacharjee JK, Strassman M (May 1967). "Accumulation of tricarboxylic acids related to lysine biosynthesis in a yeast mutant". The Journal of Biological Chemistry. 242 (10): 2542–2546. doi:10.1016/S0021-9258(18)95997-1. PMID 6026248. <a href="https://doi.org/10.1016%2FS0021-9258%2818%2995997-1" target="_blank">https://doi.org/10.1016%2FS0021-9258%2818%2995997-1</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>Kosuge T, Hoshino T (1999). "The α-aminoadipate pathway for lysine biosynthesis is widely distributed among Thermus strains". Journal of Bioscience and Bioengineering. 88 (6): 672–5. doi:10.1016/S1389-1723(00)87099-1. PMID 16232683. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>Nishida, Hiromi; Nishiyama, Makoto; Kobashi, Nobuyuki; Kosuge, Takehide; Hoshino, Takayuki; Yamane, Hisakazu (1999-12-01). "A Prokaryotic Gene Cluster Involved in Synthesis of Lysine through the Amino Adipate Pathway: A Key to the Evolution of Amino Acid Biosynthesis". Genome Research. 9 (12): 1175–1183. doi:10.1101/gr.9.12.1175. ISSN 1088-9051. PMID 10613839. <a href="https://genome.cshlp.org/content/9/12/1175" target="_blank">https://genome.cshlp.org/content/9/12/1175</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>Andi B, West AH, Cook PF (September 2004). "Kinetic mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae". Biochemistry. 43 (37): 11790–11795. doi:10.1021/bi048766p. PMID 15362863. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>Xu H, Andi B, Qian J, West AH, Cook PF (2006). "The alpha-aminoadipate pathway for lysine biosynthesis in fungi". Cell Biochemistry and Biophysics. 46 (1): 43–64. doi:10.1385/CBB:46:1:43. PMID 16943623. S2CID 22370361. <a href="/wiki/Cell_Biochemistry_and_Biophysics" target="_blank">/wiki/Cell_Biochemistry_and_Biophysics</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>Xu H, Andi B, Qian J, West AH, Cook PF (2006). "The alpha-aminoadipate pathway for lysine biosynthesis in fungi". Cell Biochemistry and Biophysics. 46 (1): 43–64. doi:10.1385/CBB:46:1:43. PMID 16943623. S2CID 22370361. <a href="/wiki/Cell_Biochemistry_and_Biophysics" target="_blank">/wiki/Cell_Biochemistry_and_Biophysics</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> <li id="fn:11"><p>Voet, Donald; Voet, Judith G. (2011). Biochemistry (4. ed.). Hoboken, NJ: Wiley. ISBN 978-0-470-91745-9. <a href="978-0-470-91745-9" target="_blank">978-0-470-91745-9</a> <a href="#fnref:11" class="footnote-back-ref">↩</a></p></li> </ol>