| EC |
1.8.1.14 |
| Accepted name: |
CoA-disulfide reductase |
| Reaction: |
2 CoA + NADP+ = CoA-disulfide + NADPH + H+ |
| Other name(s): |
CoA-disulfide reductase (NADH2); NADH2:CoA-disulfide oxidoreductase; CoA:NAD+ oxidoreductase (misleading); CoADR; coenzyme A disulfide reductase |
| Systematic name: |
CoA:NADP+ oxidoreductase |
| Comments: |
A flavoprotein. Not identical with EC 1.8.1.6 (cystine reductase), EC 1.8.1.7 (glutathione-disulfide reductase) or EC 1.8.1.13 (bis-γ-glutamylcystine reductase). The enzyme from the bacterium Staphylococcus aureus has a strong preference for NADPH [3], while the bacterium Bacillus megaterium contains both NADH and NADPH-dependent enzymes [1]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 206770-55-0 |
| References: |
| 1. |
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] |
| 2. |
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] |
| 3. |
Luba, J., Charrier, V. and Claiborne, A. Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction with pyridine nucleotides. Biochemistry 38 (1999) 2725–2737. [DOI] [PMID: 10052943] |
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| [EC 1.8.1.14 created 1992 as EC 1.6.4.10, transferred 2002 to EC 1.8.1.14, modified 2005, modified 2013] |
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