| EC |
2.3.3.8 |
| Accepted name: |
ATP citrate synthase |
| Reaction: |
ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA |
| Other name(s): |
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; ATP citrate (pro-S)-lyase |
| Systematic name: |
acetyl-CoA:oxaloacetate C-acetyltransferase [(pro-S)-carboxymethyl-forming, ADP-phosphorylating] |
| Comments: |
The enzyme can be dissociated into components, two of which are identical with EC 4.1.3.34 (citryl-CoA lyase) and EC 6.2.1.18 (citrate—CoA ligase). |
| Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-95-6 |
| References: |
| 1. |
Lill, U., Schreil, A. and Eggerer, H. Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase. Eur. J. Biochem. 125 (1982) 645–650. [DOI] [PMID: 6749502] |
| 2. |
Srere, P.A. and Lipmann, F. An enzymatic reaction between citrate, adenosine triphosphate and coenzyme A. J. Am. Chem. Soc. 75 (1953) 4874. |
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| [EC 2.3.3.8 created 1965 as EC 4.1.3.8, modified 1986, transferred 2002 to EC 2.3.3.8] |
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