A flavoprotein. Not identical with EC 22.214.171.124 (cystine reductase), EC 126.96.36.199 (glutathione-disulfide reductase) or EC 188.8.131.52 (bis-γ-glutamylcystine reductase). The enzyme from the bacterium Staphylococcus aureus has a strong preference for NADPH , while the bacterium Bacillus megaterium contains both NADH and NADPH-dependent enzymes .
Setlow, B. and Setlow, P. 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 (1977) 444–452. [PMID: 410791]
delCardayré, S.B., Stock, K.P., Newton, G.L., Fahey, R.C. and Davies, J.E. 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 (1998) 5744–5751. [DOI] [PMID: 9488707]
Luba, J., Charrier, V. and Claiborne, A. Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction with pyridine nucleotides. Biochemistry38 (1999) 2725–2737. [DOI] [PMID: 10052943]
[EC 184.108.40.206 created 1992 as EC 220.127.116.11, transferred 2002 to EC 18.104.22.168, modified 2005, modified 2013]