EC number:1.8.5.7

Enzyme

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EC Tree
     1. Oxidoreductases
        1.8 Acting on a sulfur group of donors
            1.8.5 With a quinone or similar compound as acceptor
ID:1.8.5.7
Description:Glutathionyl-hydroquinone reductase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.8.5.7
BRENDA Enzyme Link: BRENDA 1.8.5.7
KEGG Enzyme Link: KEGG1.8.5.7
BioCyc Enzyme Link: BioCyc 1.8.5.7
ExPASy Enzyme Link: ExPASy1.8.5.7
EC2PDB Enzyme Link: EC2PDB 1.8.5.7
ExplorEnz Enzyme Link: ExplorEnz 1.8.5.7
PRIAM enzyme-specific profiles Link: PRIAM 1.8.5.7
IntEnz Enzyme Link: IntEnz 1.8.5.7
MEDLINE Enzyme Link: MEDLINE 1.8.5.7

EC number:1.8.5.7

MSA:

1.8.5.7;
Phylogenetic Tree:

1.8.5.7;
Uniprot:
M-CSA:
RHEA:51936 2-(glutathione-S-yl)-hydroquinone + glutathione = glutathione disulfide + hydroquinone
RULE(radius=1) [*:1]-[S;H0;+0:2]-[c;H0;+0:3](:[*:4]):[*:5].[*:6]-[SH;+0:7]>>[*:1]-[S;H0;+0:2]-[S;H0;+0:7]-[*:6].[*:4]:[cH;+0:3]:[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural understanding of the glutathione-dependent reduction mechanism of glutathionyl-hydroquinone reductases.Green AR, Hayes RP, Xun L, Kang C2012 Oct 1922955277
Reduction of benzoquinones to hydroquinones via spontaneous reaction with glutathione and enzymatic reaction by S-glutathionyl-hydroquinone reductases.Lam LK, Zhang Z, Board PG, Xun L2012 Jun 2622686328
S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of glutathione transferases.Xun L, Belchik SM, Xun R, Huang Y, Zhou H, Sanchez E, Kang C, Board PG2010 May 2720388120
Maintenance role of a glutathionyl-hydroquinone lyase (PcpF) in pentachlorophenol degradation by Sphingobium chlorophenolicum ATCC 39723.Huang Y, Xun R, Chen G, Xun L2008 Dec18820023