Succinate-CoA ligase (ADP-forming)

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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 $\rightleftharpoons$ 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: citrate cycle (tca cycle), propanoate metabolism, c5-branched dibasic acid metabolism, and reductive carboxylate cycle (co2 fixation).

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

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.

[edit] References

IUBMB entry for 6.2.1.5
BRENDA references for 6.2.1.5 (Recommended.)
PubMed references for 6.2.1.5
PubMed Central references for 6.2.1.5
Google Scholar references for 6.2.1.5
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: 153–164.
Kaufman S and Alivasatos SGA (1955). "Purification and properties of the phosphorylating enzyme from spinach". J. Biol. Chem. 216: 141–152.