Succinate-CoA ligase (GDP-forming)

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In enzymology, a succinate-CoA ligase (GDP-forming) (EC 6.2.1.4) is an enzyme that catalyzes the chemical reaction

GTP + succinate + CoA $\rightleftharpoons$ GDP + phosphate + succinyl-CoA

The 3 substrates of this enzyme are GTP, succinate, and CoA, whereas its 3 products are GDP, 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 (GDP-forming). Other names in common use include succinyl-CoA synthetase (GDP-forming), succinyl coenzyme A synthetase (guanosine diphosphate-forming), succinate thiokinase, succinic thiokinase, succinyl coenzyme A synthetase, succinate-phosphorylating enzyme, P-enzyme, SCS, G-STK, succinyl coenzyme A synthetase (GDP-forming), succinyl CoA synthetase, and succinyl coenzyme A synthetase. This enzyme participates in citrate cycle (tca cycle) and propanoate metabolism.

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

[edit] Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1EUC, 1EUD, 2FP4, 2FPG, 2FPI, and 2FPP.

[edit] References

IUBMB entry for 6.2.1.4
BRENDA references for 6.2.1.4 (Recommended.)
PubMed references for 6.2.1.4
PubMed Central references for 6.2.1.4
Google Scholar references for 6.2.1.4
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, Gilvarg C, Cori O and Ochoa S (1953). "Enzymatic oxidation of alpha-ketoglutarate and coupled phosphorylation". J. Biol. Chem. 203: 869–888.
Mazumder R, Sanadi DR and Rodwell WV (1960). "Purification and properties of hog kidney succinic thiokinase". J. Biol. Chem. 235: 2546–2550.
SANADI DR, GIBSON M, AYENGAR P (1954). "Guanosine triphosphate, the primary product of phosphorylation coupled to the breakdown of succinyl coenzyme A". Biochim. Biophys. Acta. 14: 434–6. doi:10.1016/0006-3002(54)90205-X. PMID 13181903.