Homocitrate synthase

Enzyme From Wikipedia, the free encyclopedia

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

 
 
H2O
 
Reversible left-right reaction arrow with minor forward substrate(s) from top left and minor reverse product(s) to bottom left
H2O
 
 
 

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.

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