KEGG   ENZYME: 1.8.1.10
Entry
EC 1.8.1.10                 Enzyme                                 
Name
CoA-glutathione reductase;
coenzyme A glutathione disulfide reductase;
NADPH-dependent coenzyme A-SS-glutathione reductase;
coenzyme A disulfide-glutathione reductase;
NADPH:CoA-glutathione oxidoreductase
Class
Oxidoreductases;
Acting on a sulfur group of donors;
With NAD+ or NADP+ as acceptor
Sysname
glutathione:NADP+ oxidoreductase (CoA-acylating)
Reaction(IUBMB)
CoA + glutathione + NADP+ = CoA-glutathione + NADPH + H+ [RN:R05714]
Reaction(KEGG)
R05714;
(other) R00900
Substrate
CoA [CPD:C00010];
glutathione [CPD:C00051];
NADP+ [CPD:C00006]
Product
CoA-glutathione [CPD:C00920];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
A flavoprotein. The substrate is a mixed disulfide. May be identical to EC 1.8.1.9, thioredoxin-disulfide reductase.
History
EC 1.8.1.10 created 1972 as EC 1.6.4.6, transferred 2002 to EC 1.8.1.10
Pathway
ec00270  Cysteine and methionine metabolism
ec01100  Metabolic pathways
Reference
1  [PMID:4390951]
  Authors
Ondarza RN, Abney R, Lopez-Colome AM.
  Title
Characterization of a NADPH-dependent coenzyme A-SS-glutathione reductase from yeast.
  Journal
Biochim Biophys Acta 191:239-48 (1969)
DOI:10.1016/0005-2744(69)90243-5
Reference
2  [PMID:4151341]
  Authors
Ondarza RN, Escamilla E, Gutierrez J, De la Chica G.
  Title
CoAS-Sglutathione and GSSG reductases from rat liver. Two disulfide oxidoreductase activities in one protein entity.
  Journal
Biochim Biophys Acta 341:162-71 (1974)
DOI:10.1016/0005-2744(74)90076-X
Reference
3  [PMID:334266]
  Authors
Carlberg I, Mannervik B.
  Title
Purification by affinity chromatography of yeast glutathione reductase, the enzyme responsible for the NADPH-dependent reduction of the mixed disulfide of coenzyme A and glutathione.
  Journal
Biochim Biophys Acta 484:268-74 (1977)
DOI:10.1016/0005-2744(77)90083-3
Other DBs
ExplorEnz - The Enzyme Database: 1.8.1.10
IUBMB Enzyme Nomenclature: 1.8.1.10
ExPASy - ENZYME nomenclature database: 1.8.1.10
BRENDA, the Enzyme Database: 1.8.1.10
CAS: 37256-33-0

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