Homocitrate synthase

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In enzymology, a homocitrate synthase (EC 2.3.3.14) is an enzyme that catalyzes the chemical reaction

acetyl-CoA + H₂O + 2-oxoglutarate $\rightleftharpoons$ (R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA

The 3 substrates of this enzyme are acetyl-CoA, H₂O, and 2-oxoglutarate, whereas its two products are (R)-2-hydroxybutane-1,2,4-tricarboxylate and CoA.

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.

[edit] References

IUBMB entry for 2.3.3.14
BRENDA references for 2.3.3.14 (Recommended.)
PubMed references for 2.3.3.14
PubMed Central references for 2.3.3.14
Google Scholar references for 2.3.3.14
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H (2002). "Characterization of bacterial homocitrate synthase involved in lysine biosynthesis". FEBS. Lett. 522: 35–40. doi:10.1016/S0014-5793(02)02877-6. PMID 12095615.
Andi B, West AH, Cook PF (2004). "Kinetic mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae". Biochemistry. 43: 11790–5. doi:10.1021/bi048766p. PMID 15362863.