Biology:Homocitrate synthase
| homocitrate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Homocitrate synthase homodimer, Schizosaccharomyces pombe | |||||||||
| Identifiers | |||||||||
| EC number | 2.3.3.14 | ||||||||
| CAS number | 9075-60-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a homocitrate synthase (EC 2.3.3.14) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are α-ketoglutaric acid, acetyl-CoA, and water. Its products are (-)-homoisocitric acid and coenzyme A.[1][2][3][4]
This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl-CoA:2-oxoglutarate C-acetyltransferase (thioester-hydrolysing, carboxymethyl forming). Other names in common use include 2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase, (CoA-acetylating), acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase, and homocitrate synthetase. This enzyme participates in lysine biosynthesis and pyruvate metabolism.
References
- ↑ Enzyme 2.3.3.14 at KEGG Pathway Database.
- ↑ "Enzymatic formation of homocitric acid, an intermediate in lysine biosynthesis". Biochem. Biophys. Res. Commun. 14 (3): 262–7. 1964. doi:10.1016/0006-291X(64)90446-2. PMID 5836514. Bibcode: 1964BBRC...14..262S.
- ↑ H; Miyazaki, J; Kobashi, N; Nishiyama, M; Hoshino, T; Yamane, H (2002). "Characterization of bacterial homocitrate synthase involved in lysine biosynthesis". FEBS Lett. 522 (1–3): 35–40. doi:10.1016/S0014-5793(02)02877-6. PMID 12095615. Bibcode: 2002FEBSL.522...35W.
- ↑ "Kinetic mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae". Biochemistry 43 (37): 11790–5. 2004. doi:10.1021/bi048766p. PMID 15362863.
 |  |
