Homocitrate synthase

{{Short description|Enzyme}}

{{infobox enzyme

| Name = homocitrate synthase

| EC_number = 2.3.3.14

| CAS_number = 9075-60-9

| GO_code = 0004410

| image = 3mi3.jpg

| width = 270

| caption = Homocitrate synthase homodimer, Schizosaccharomyces pombe

}}

In enzymology, a homocitrate synthase ({{EC number|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.

References

{{reflist|1}}

  • {{cite journal |vauthors=Strassman M, Ceci LN | date = 1964 | title = Enzymatic formation of homocitric acid, an intermediate in lysine biosynthesis | journal = Biochem. Biophys. Res. Commun. | volume = 14 | pages = 262–7 | pmid = 5836514 | doi = 10.1016/0006-291X(64)90446-2 | issue = 3 }}
  • {{cite journal | author = H | date = 2002 | title = Characterization of bacterial homocitrate synthase involved in lysine biosynthesis | journal = FEBS Lett. | volume = 522 | pages = 35–40 | pmid = 12095615 | doi = 10.1016/S0014-5793(02)02877-6 | last2 = Miyazaki | first2 = J | last3 = Kobashi | first3 = N | last4 = Nishiyama | first4 = M | last5 = Hoshino | first5 = T | last6 = Yamane | first6 = H | issue = 1–3 | doi-access = }}
  • {{cite journal |vauthors=Andi B, West AH, Cook PF | date = 2004 | title = Kinetic mechanism of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae | journal = Biochemistry | volume = 43 | pages = 11790–5 | pmid = 15362863 | doi = 10.1021/bi048766p | issue = 37 }}

{{Acyltransferases}}

{{Enzymes}}

{{Portal bar|Biology|border=no}}

Category:EC 2.3.3

Category:Enzymes of unknown structure

{{2.3-enzyme-stub}}