Succinate—CoA ligase (GDP-forming)
In enzymology, a succinate-CoA ligase (GDP-forming) (EC 6.2.1.4) is an enzyme that catalyzes the chemical reaction
- GTP + succinate + CoA
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 the citric acid cycle and propanoate metabolism.
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.
References
- ↑ Fraser, M. E.; Hayakawa, K.; Hume, M. S.; Ryan, D. G.; Brownie, E. R. (2006). "Interactions of GTP with the ATP-grasp Domain of GTP-specific Succinyl-CoA Synthetase". Journal of Biological Chemistry 281 (16): 11058–11065. doi:10.1074/jbc.M511785200. PMID 16481318.
- 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. PMID 13084656.
- Mazumder R, Sanadi DR and Rodwell WV (1960). "Purification and properties of hog kidney succinic thiokinase". J. Biol. Chem. 235: 2546–2550. PMID 13768680.
- 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 (3): 434–6. doi:10.1016/0006-3002(54)90205-X. PMID 13181903.
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