| EC |
6.2.1.22 |
| Accepted name: |
[citrate (pro-3S)-lyase] ligase |
| Reaction: |
ATP + acetate + holo-[citrate (pro-3S)-lyase] = AMP + diphosphate + acetyl-[citrate (pro-3S)-lyase] |
| Glossary: |
citrate = 2-hydroxypropane-1,2,3-tricarboxylate |
| Other name(s): |
citrate lyase ligase; citrate lyase synthetase; acetate: SH-[acyl-carrier-protein] enzyme ligase (AMP); acetate:HS-citrate lyase ligase; acetate:citrate-(pro-3S)-lyase(thiol-form) ligase (AMP-forming); acetate:[citrate-(pro-3S)-lyase](thiol-form) ligase (AMP-forming) |
| Systematic name: |
acetate:holo-[citrate-(pro-3S)-lyase] ligase (AMP-forming) |
| Comments: |
Both this enzyme and EC 2.3.1.49,deacetyl-[citrate-(pro-3S)-lyase] S-acetyltransferase, acetylate and activate EC 4.1.3.6, citrate (pro-3S)-lyase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52660-22-7 |
| References: |
| 1. |
Antranikian, G. and Gottschalk, G. Copurification of citrate lyase and citrate lyase ligase from Rhodopseudomonas gelatinosa and subsequent separation of the two enzymes. Eur. J. Biochem. 126 (1982) 43–47. [DOI] [PMID: 7128585] |
| 2. |
Antranikian, G., Herzberg, C. and Gottschalk, G. Covalent modification of citrate lyase ligase from Clostridium sphenoides by phosphorylation/dephosphorylation. Eur. J. Biochem. 153 (1985) 413–420. [DOI] [PMID: 3935436] |
| 3. |
Quentmeier, A. and Antranikian, G. Characterization of citrate lyase from Clostridium sporosphaeroides. Arch. Microbiol. 141 (1985) 85–90. [PMID: 3994485] |
| 4. |
Schmellenkamp, H. and Eggerer, H. Mechanism of enzymic acetylation of des-acetyl citrate lyase. Proc. Natl. Acad. Sci. USA 71 (1974) 1987–1991. [DOI] [PMID: 4365579] |
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| [EC 6.2.1.22 created 1989] |
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