ATP citrate synthase

In enzymology, an ATP citrate synthase (EC 2.3.3.8) is an enzyme that catalyzes the chemical reaction

The 4 substrates of this enzyme are ADP, phosphate, acetyl-CoA, and oxaloacetate, whereas its 3 products are ATP, citrate, 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:oxaloacetate C-acetyltransferase [(pro-S)-carboxymethyl-forming, ADP-phosphorylating]. Other names in common use include ATP-citric lyase, ATP:citrate oxaloacetate-lyase [(pro-S)-CH2COO-->acetyl-CoA], (ATP-dephosphorylating), acetyl-CoA:oxaloacetate acetyltransferase (isomerizing, ADP-phosphorylating), adenosine triphosphate citrate lyase, citrate cleavage enzyme, citrate-ATP lyase, citric cleavage enzyme, and ATP citrate (pro-S)-lyase. This enzyme participates in citrate cycle (tca cycle) and reductive carboxylate cycle (co2 fixation).