| EC |
2.3.3.14 |
| Accepted name: |
homocitrate synthase |
| Reaction: |
acetyl-CoA + H2O + 2-oxoglutarate = (2R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA |
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For diagram of L-Lysine synthesis, click here |
| Glossary: |
(R)-homocitrate = (2R)-2-hydroxybutane-1,2,4-tricarboxylate |
| Other name(s): |
2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acetylating); acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase; homocitrate synthetase; HCS |
| Systematic name: |
acetyl-CoA:2-oxoglutarate C-acetyltransferase (thioester-hydrolysing, carboxymethyl-forming) |
| Comments: |
Belongs in the α-aminoadipate pathway of lysine synthesis, along with EC 4.2.1.36, homoaconitate hydratase. The enzyme also acts with oxaloacetate as substrate, but more slowly [2,3]. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9075-60-9 |
| References: |
| 1. |
Strassman, M. and Ceci, L.N. Enzymatic formation of homocitric acid, an intermediate in lysine biosynthesis. Biochem. Biophys. Res. Commun. 14 (1964) 262–267. [DOI] [PMID: 5836514] |
| 2. |
Wulandari, A.P., Miyazaki, J., Kobashi, N., Nishiyama, M., Hoshino, T. and Yamane, H. Characterization of bacterial homocitrate synthase involved in lysine biosynthesis. FEBS Lett. 522 (2002) 35–40. [DOI] [PMID: 12095615] |
| 3. |
Andi, B., West, A.H. and Cook, P.F. Kinetic mechanism of histidine-tagged homocitrate synthase from
Saccharomyces cerevisiae. Biochemistry 43 (2004) 11790–11795. [DOI] [PMID: 15362863] |
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| [EC 2.3.3.14 created 1972 as EC 4.1.3.21, transferred 2002 to EC 2.3.3.14] |
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