|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 188.8.131.52
Supersedes EC number: 184.108.40.206
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: CoA-disulfide reductase
Enzyme Commission Synonyms: CoA-disulfide reductase (NADH2), NADH2:CoA-disulfide oxidoreductase, CoA:NAD+ oxidoreductase (misleading), CoADR, coenzyme A disulfide reductase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -11.002319 [Latendresse13]
Enzyme Commission Summary:
A flavoprotein. Not identical with EC 220.127.116.11, cystine reductase, EC 18.104.22.168, glutathione-disulfide reductase or EC 22.214.171.124, bis-γ-glutamylcystine reductase. The enzyme from the bacterium Staphylococcus aureus has a strong preference for NADPH [Luba99], while the bacterium Bacillus megaterium contains both NADH and NADPH-dependent enzymes [Setlow77].
Unification Links: KEGG:R07175
delCardayre98: 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. PMID: 9488707
Luba99: 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. PMID: 10052943
Setlow77: 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. PMID: 410791
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