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Succinate—CoA ligase (ADP-forming)

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succinate-CoA ligase (ADP-forming)
Succinyl-COA synthetase from Escherichia coli. PDB 2scu [1]
Identifiers
EC no.6.2.1.5
CAS no.9080-33-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

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

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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

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  1. ^ 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.