In enzymology, a succinate-CoA ligase (ADP-forming) (EC 6.2.1.5) is an enzyme that catalyzes the chemical reaction
| 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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- 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
editAs 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.
