- CoA-disulfide reductase
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CoA-disulfide reductase Identifiers EC number 1.8.1.14 CAS number 206770-55-0 Databases IntEnz IntEnz view BRENDA BRENDA entry ExPASy NiceZyme view KEGG KEGG entry MetaCyc metabolic pathway PRIAM profile PDB structures RCSB PDB PDBe PDBsum Gene Ontology AmiGO / EGO Search PMC articles PubMed articles In enzymology, a CoA-disulfide reductase (EC 1.8.1.14) is an enzyme that catalyzes the chemical reaction
- 2 CoA + NAD(P)+
CoA-disulfide + NAD(P)H + H+
The 3 substrates of this enzyme are CoA, NAD+, and NADP+, whereas its 4 products are CoA-disulfide, NADH, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is CoA:NAD(P)+ oxidoreductase. Other names in common use include CoA-disulfide reductase (NADH2), NADH2:CoA-disulfide oxidoreductase, CoA:NAD+ oxidoreductase, CoADR, and coenzyme A disulfide reductase.
References
- Setlow B, Setlow P (1977). "Levels of acetyl coenzyme A, reduced and oxidized coenzyme A, and coenzyme A in disulfide linkage to protein in dormant and germinated spores and growing and sporulating cells of Bacillus megaterium". J. Bacteriol. 132 (2): 444–52. PMC 221883. PMID 410791. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=221883.
- delCardayre SB, Stock KP, Newton GL, Fahey RC, Davies JE (1998). "Coenzyme A disulfide reductase, the primary low molecular weight disulfide reductase from Staphylococcus aureus. Purification and characterization of the native enzyme". J. Biol. Chem. 273 (10): 5744–51. doi:10.1074/jbc.273.10.5744. PMID 9488707.
- Luba J, Charrier V, Claiborne A (1999). "Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction with pyridine nucleotides". Biochemistry. 38 (9): 2725–37. doi:10.1021/bi9825899. PMID 10052943.
- Crane EJ 3rd; Ward, DE; Feasel, JM; Lancaster, KM; Murphy, RD; Mallet, TC; Crane Ej, 3rd (2005). "Discovery and characterization of a Coenzyme A disulfide reductase from Pyrococcus horikoshii. Implications for this disulfide metabolism of anaerobic hyperthermophiles". Febs. J. 272 (5): 1189–200. doi:10.1111/j.1742-4658.2005.04555.x. PMID 15720393.
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