Succinate—CoA ligase (ADP-forming)
| succinate-CoA ligase (ADP-forming) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifiers | |||||||||
| EC no. | 6.2.1.5 | ||||||||
| CAS no. | 9080-33-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a succinate-CoA ligase (ADP-forming) (EC 6.2.1.5) is an enzyme that catalyzes the chemical reaction
- ATP + succinate + CoA ADP + phosphate + succinyl-CoA
The 3 substrates of this enzyme are ATP, succinate, and CoA, whereas its 3 products are ADP, phosphate, and succinyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is succinate:CoA ligase (ADP-forming). Other names in common use include succinyl-CoA synthetase (ADP-forming), succinic thiokinase, succinate thiokinase, succinyl-CoA synthetase, succinyl coenzyme A synthetase (adenosine diphosphate-forming), succinyl coenzyme A synthetase, A-STK (adenin nucleotide-linked succinate thiokinase), STK, and A-SCS. This enzyme participates in 4 metabolic pathways: Citric acid cycle, propanoate metabolism, c5-branched dibasic acid metabolism, and reductive carboxylate cycle (CO2 fixation).
Structural studies
[edit]As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1CQI, 1CQJ, 1JKJ, 1JLL, 1OI7, 1SCU, 2NU6, 2NU7, 2NU8, 2NU9, 2NUA, and 2SCU.
References
[edit]- ^ Fraser, M. E.; James, M. N. G.; Bridger, W. A.; Wolodko, W. T. (1999). "A detailed structural description of Escherichia coli succinyl-CoA synthetase1". Journal of Molecular Biology. 285 (4): 1633–1653. doi:10.1006/jmbi.1998.2324. PMID 9917402.
- Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 6, Academic Press, New York, 1962, p. 387-399.
- Kaufman S (1955). "Studies on the mechanism of the reaction catalyzed by the phosphorylating enzyme". J. Biol. Chem. 216 (1): 153–164. doi:10.1016/S0021-9258(19)52292-X. PMID 13252015.
- Kaufman S; Alivasatos SGA (1955). "Purification and properties of the phosphorylating enzyme from spinach". J. Biol. Chem. 216 (1): 141–152. doi:10.1016/S0021-9258(19)52291-8. PMID 13252014.
