| Revision as of 14:33, 21 November 2011 editBeetstra (talk | contribs)Edit filter managers, Administrators172,031 edits Saving copy of the {{chembox}} taken from revid 455922307 of page Homoserine for the Chem/Drugbox validation project (updated: 'ChEMBL'). |
Latest revision as of 06:10, 8 June 2024 edit Teaktl17 (talk | contribs)Extended confirmed users18,034 editsm →Biosynthesis: +wl |
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{{ambox | text = This page contains a copy of the infobox ({{tl|chembox}}) taken from revid of page ] with values updated to verified values.}} |
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{{chembox |
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{{chembox |
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| verifiedrevid = 402148997 |
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| verifiedrevid = 461770636 |
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| Name = <small>L</small>-Homoserine |
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| Name = {{sm|l}}-Homoserine |
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| ImageFile_Ref = {{chemboximage|correct|??}} |
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| ImageFile_Ref = {{chemboximage|correct|??}} |
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| ImageFile = L-Homoserin.svg |
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| ImageFile = L-Homoserin.svg |
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| ImageName1 = Ball-and-stick model of the zwitterion |
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| ImageName1 = Ball-and-stick model of the zwitterion |
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| IUPACName = (''S'')-2-Amino-4-hydroxybutanoic acid |
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| IUPACName = (''S'')-2-Amino-4-hydroxybutanoic acid |
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| Section1 = {{Chembox Identifiers |
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|Section1={{Chembox Identifiers |
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| InChI = 1/C4H9NO3/c5-3(1-2-6)4(7)8/h3,6H,1-2,5H2,(H,7,8) |
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| InChI = 1/C4H9NO3/c5-3(1-2-6)4(7)8/h3,6H,1-2,5H2,(H,7,8) |
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| ChEBI_Ref = {{ebicite|changed|EBI}} |
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| ChEBI_Ref = {{ebicite|correct|EBI}} |
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| ChEBI = 30653 |
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| ChEBI = 30653 |
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| SMILES = O=C(O)C(N)CCO |
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| SMILES = O=C(O)C(N)CCO |
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| StdInChIKey = UKAUYVFTDYCKQA-UHFFFAOYSA-N |
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| StdInChIKey = UKAUYVFTDYCKQA-UHFFFAOYSA-N |
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| CASNo = 672-15-1 |
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| CASNo = 672-15-1 |
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| CASNo_Ref = {{cascite|correct|CAS}} |
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| CASNo_Ref = {{cascite|correct|CAS}} |
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| UNII_Ref = {{fdacite|correct|FDA}} |
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| EC-number = 211-590-6 |
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| UNII = 6KA95X0IVO |
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| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}} |
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| EC_number = 211-590-6 |
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| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}} |
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| ChemSpiderID = 758 |
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| ChemSpiderID = 758 |
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| PubChem = 779 |
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| PubChem = 779 |
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| ChEMBL_Ref = {{ebicite|changed|EBI}} |
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| ChEMBL_Ref = {{ebicite|changed|EBI}} |
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| ChEMBL = <!-- blanked - oldvalue: 11722 --> |
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| ChEMBL = 11722 |
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}} |
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| Section2 = {{Chembox Properties |
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|Section2={{Chembox Properties |
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| Formula = C<sub>4</sub>H<sub>9</sub>NO<sub>3</sub> |
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| Formula = C<sub>4</sub>H<sub>9</sub>NO<sub>3</sub> |
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| MolarMass = 119.12 g/mol |
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| MolarMass = 119.12 g/mol |
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| MeltingPt = 203 °C (decomposes) |
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'''Homoserine''' (also called isothreonine) is an α-] with the ] HO<sub>2</sub>CCH(NH<sub>2</sub>)CH<sub>2</sub>CH<sub>2</sub>OH. <small>L</small>-Homoserine is not one of the common amino acids encoded by DNA. It differs from the ] ] by insertion of an additional ] into the backbone. Homoserine, or its ] form, is the product of a ] cleavage of a ] by degradation of ]. |
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<!-- ] This image shows the wrong enantiomers! --> |
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Homoserine is an intermediate in the ] of three ]s: ], ] (an ] of homoserine), and ].<ref>{{Cite journal| vauthors = Tanaka M, Kishi T, Kinoshita S |date=September 1961|title=Studies on the Synthesis of l -Amino Acids: Part III. A Synthesis of l -Homoserine from l -Aspartic Acid|url=https://academic.oup.com/bbb/article/25/9/678-679/5976039|journal=Agricultural and Biological Chemistry|language=en|volume=25|issue=9|pages=678–679|doi=10.1080/00021369.1961.10857862|issn=0002-1369}}</ref> Its complete biosynthetic pathway includes ], the ] (TCA) or ] (Krebs cycle), and the aspartate metabolic pathway. It forms by two reductions of ] via the intermediacy of aspartate semialdehyde.<ref>Berg, J. M.; Stryer, L. et al. (2002), ''Biochemistry''. W.H. Freeman. {{ISBN|0-7167-4684-0}}</ref> Specifically, the enzyme ], in association with ], catalyzes a reversible reaction that interconverts ] to <small>L</small>-homoserine. Then, two other enzymes, ] and ] use homoserine as a substrate and produce phosphohomoserine and ''O''-succinyl homoserine respectively.<ref name=":03">{{cite journal | vauthors = Liu P, Zhang B, Yao ZH, Liu ZQ, Zheng YG | title = Multiplex Design of the Metabolic Network for Production of l-Homoserine in Escherichia coli | journal = Applied and Environmental Microbiology | volume = 86 | issue = 20 | date = October 2020 | pmid = 32801175 | doi = 10.1128/AEM.01477-20 | pmc = 7531971 | bibcode = 2020ApEnM..86E1477L | veditors = Zhou NY }}</ref> |
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==Applications== |
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Commercially, homoserine can serve as precursor to the synthesis of ] and ].<ref name=":1">{{cite journal | vauthors = Huang JF, Zhang B, Shen ZY, Liu ZQ, Zheng YG | title = Metabolic engineering of ''E. coli'' for the production of ''O''-succinyl-l-homoserine with high yield | journal = 3 Biotech | volume = 8 | issue = 7 | pages = 310 | date = July 2018 | pmid = 30002999 | pmc = 6037649 | doi = 10.1007/s13205-018-1332-x }}</ref> Purified homoserine is used in enzyme structural studies.<ref>{{cite journal | vauthors = Akai S, Ikushiro H, Sawai T, Yano T, Kamiya N, Miyahara I | title = The crystal structure of homoserine dehydrogenase complexed with l-homoserine and NADPH in a closed form | journal = Journal of Biochemistry | volume = 165 | issue = 2 | pages = 185–195 | date = February 2019 | pmid = 30423116 | doi = 10.1093/jb/mvy094 }}</ref> Also, homoserine has played important roles in studies to elucidate peptide synthesis and synthesis of ] glycopeptides.<ref>{{cite journal | vauthors = Yang W, Ramadan S, Yang B, Yoshida K, Huang X | title = Homoserine as an Aspartic Acid Precursor for Synthesis of Proteoglycan Glycopeptide Containing Aspartic Acid and a Sulfated Glycan Chain | journal = The Journal of Organic Chemistry | volume = 81 | issue = 23 | pages = 12052–12059 | date = December 2016 | pmid = 27809505 | doi = 10.1021/acs.joc.6b02441 | pmc = 5215661 }}</ref> Bacterial cell lines can make copious amounts of this amino acid.<ref name=":03"/><ref name=":1" /> |
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==Biosynthesis== |
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Homoserine is produced from aspartate via aspartate-4-semialdehyde, which is produced from β-phosphoaspartate. By the action of ]s, the semialdehyde is converted to homoserine.<ref>{{cite journal |doi=10.1021/ar000057q|title=The Central Enzymes of the Aspartate Family of Amino Acid Biosynthesis |year=2001 |last1=Viola |first1=Ronald E. |journal=Accounts of Chemical Research |volume=34 |issue=5 |pages=339–349 |pmid=11352712 }}</ref> |
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<small>L</small>-Homoserine is substrate for ], yielding phosphohomoserine (homoserine-phosphate), which is converted to by ] to yield <small>L</small>-threonine. |
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Homoserine is converted to ''O''-succinyl homoserine by ], a precursor to <small>L</small>-methionine.<ref name=":2">{{cite journal | vauthors = Petit C, Kim Y, Lee SK, Brown J, Larsen E, Ronning DR, Suh JW, Kang CM | display-authors = 6 | title = Reduction of Feedback Inhibition in Homoserine Kinase (ThrB) of ''Corynebacterium glutamicum'' Enhances l-Threonine Biosynthesis | journal = ACS Omega | volume = 3 | issue = 1 | pages = 1178–1186 | date = January 2018 | pmid = 30023797 | doi = 10.1021/acsomega.7b01597 | pmc = 6045374 }}</ref> |
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Homoserine allosterically inhibits aspartate kinase and ].<ref name=":03"/> Glutamate dehydrogenase reversibly converts ] to ] and α-ketoglutarate coverts to ] through the citric cycle. Threonine acts as another ] of aspartate kinase and homoserine dehydrogenase, but it is a ] of homoserine kinase.<ref name=":2" /> |
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== References == |
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{{reflist}} |
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{{biochem-stub}} |