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MetaCyc Reaction: 1.8.1.14

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 1.8.1.14

Supersedes EC number: 1.6.4.10

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. 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

Taxonomic Range: Archaea , Bacteria

Standard Gibbs Free Energy (ΔrG in kcal/mol): -20.025146 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
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 [Luba99], while the bacterium Bacillus megaterium contains both NADH and NADPH-dependent enzymes [Setlow77].

Citations: [delCardayre98]

Unification Links: KEGG:R07175

Relationship Links: BRENDA:EC:1.8.1.14 , ENZYME:EC:1.8.1.14 , IUBMB-ExplorEnz:EC:1.8.1.14 , Rhea:RELATED-TO:14704 , Rhea:RELATED-TO:14708


References

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

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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