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).
Substrate-level phosphorylation is a metabolism reaction that results in the production of ATP or GTP supported by the energy released from another high-energy bond that leads to phosphorylation of ADP or GDP to ATP or GTP (note that the reaction catalyzed by creatine kinase is not considered as "substrate-level phosphorylation"). This process uses some of the released chemical energy, the Gibbs free energy, to transfer a phosphoryl (PO3) group to ADP or GDP. Occurs in glycolysis and in the citric acid cycle.
Succinyl coenzyme A synthetase is an enzyme that catalyzes the reversible reaction of succinyl-CoA to succinate. The enzyme facilitates the coupling of this reaction to the formation of a nucleoside triphosphate molecule from an inorganic phosphate molecule and a nucleoside diphosphate molecule. It plays a key role as one of the catalysts involved in the citric acid cycle, a central pathway in cellular metabolism, and it is located within the mitochondrial matrix of a cell.
The long chain fatty acyl-CoA ligase is an enzyme of the ligase family that activates the oxidation of complex fatty acids. Long chain fatty acyl-CoA synthetase catalyzes the formation of fatty acyl-CoA by a two-step process proceeding through an adenylated intermediate. The enzyme catalyzes the following reaction,
In enzymology, a 3-oxoacid CoA-transferase is an enzyme that catalyzes the chemical reaction
In enzymology, an acetate—CoA ligase (ADP-forming) is an enzyme that catalyzes the chemical reaction
Butyrate—CoA ligase, also known as xenobiotic/medium-chain fatty acid-ligase (XM-ligase), is an enzyme that catalyzes the chemical reaction:
In enzymology, a D-alanine—D-alanine ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a dethiobiotin synthase (EC 6.3.3.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a dihydrofolate synthase is an enzyme that catalyzes the chemical reaction
In enzymology, a formate—tetrahydrofolate ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a glutarate—CoA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a malate—CoA ligase is an enzyme that catalyzes the chemical reaction
In molecular biology, the protein domain SAICAR synthase is an enzyme which catalyses a reaction to create SAICAR. In enzymology, this enzyme is also known as phosphoribosylaminoimidazolesuccinocarboxamide synthase. It is an enzyme that catalyzes the chemical reaction
In enzymology, a phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a succinate—CoA ligase (GDP-forming) is an enzyme that catalyzes the chemical reaction
In enzymology, a tetrahydrofolate synthase is an enzyme that catalyzes the chemical reaction
In enzymology, a UDP-N-acetylmuramate—L-alanine ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a UDP-N-acetylmuramoyl-L-alanine—D-glutamate ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a dephospho-CoA kinase is an enzyme that catalyzes the chemical reaction
Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial is an enzyme that in humans is encoded by the SUCLG1 gene.
References
↑ 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. PMID9917402.
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 6, Academic Press, New York, 1962, p.387-399.
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