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Information on EC 1.8.4.7 - enzyme-thiol transhydrogenase (glutathione-disulfide) for references in articles please use BRENDA:EC1.8.4.7
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IUBMB Comments Converts EC 1.17.1.4 xanthine dehydrogenase into EC 1.17.3.2 xanthine oxidase in the presence of glutathione disulfide; also reduces the disulfide bond of ricin. Not inhibited by Cu2+ or thiol reagents.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
DnaJ, enzyme-thiol transhydrogenase (oxidized glutathione), glutathione-dependent thiol:disulfide oxidoreductase, thiol-disulfide oxidoreductase, thiol:disulfide oxidoreductase, thiol:disulphide oxidoreductase, YkuV, [xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase,
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enzyme-thiol transhydrogenase (oxidized glutathione)
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glutathione-dependent thiol:disulfide oxidoreductase
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thiol-disulfide oxidoreductase
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thiol:disulfide oxidoreductase
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thiol:disulphide oxidoreductase
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[xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase
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[xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] + 2 glutathione
[xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] + 2 glutathione
converts EC 1.1.1.204 xanthine dehydrogenase into EC 1.1.3.22 xanthine oxidase in presence of oxidized glutathione. Also reduces the disulfide bond of ricin. Not inhibited by Cu2+ or thiol reagents
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[xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] + 2 glutathione
thioltransferase, GSH:insulin transhydrogenase and ricin-disulphide-bond reductase activity
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[xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] + 2 glutathione
thioltransferase activity with cysteine as substrate. Mainly D-form of enzyme exists
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[xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] + 2 glutathione
thioltransferase activity with cysteine as substrate. Mainly D-form of enzyme exists
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[xanthine-dehydrogenase]:glutathione-disulfide S-oxidoreductase
Converts EC 1.17.1.4 xanthine dehydrogenase into EC 1.17.3.2 xanthine oxidase in the presence of glutathione disulfide; also reduces the disulfide bond of ricin. Not inhibited by Cu2+ or thiol reagents.
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85030-79-1
formerly 12345-67-8
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[xanthine dehydrogenase] + oxidized glutathione
[xanthine oxidase] + glutathione
additional information
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other disulfide compounds are either inactive or far less active than oxidized glutathione, reduction of disulfide bonds in ricin, thioltransferase activity, GSH:insulin transhydrogenase activity
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[xanthine dehydrogenase] + oxidized glutathione
[xanthine oxidase] + glutathione
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reverse conversion possible by dithioerythritol, not obtained in presence of GSH
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[xanthine dehydrogenase] + oxidized glutathione
[xanthine oxidase] + glutathione
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conversion into oxidase by treatment with proteolytic enzymes, storage at -20°C/-25°C or preincubation with either thiol reagents or whole liver homogenate. Can act in the opposite direction in the reduction of the disulfide bond of insulin and ricin
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[xanthine dehydrogenase] + oxidized glutathione
[xanthine oxidase] + glutathione
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reverse conversion possible by dithioerythritol, not obtained in presence of GSH
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additional information
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insensitive against 1 mM CuSO4 and 1 mM N-ethylmaleimide at 37°C for 30 min
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additional information
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372 U/mg, other definition of units
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3750 U/mg, 1 unit is defined as the amount of the enzyme producing a 1% reduction of the ration NADH formed/uric acid formed, corrected for non-enzymic conversion
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Wistar
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newborn and adults
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Wistar
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highest amount of activity
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Q5L7K1
Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343)
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40000
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1 * 40000, SDS-PAGE
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monomer
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1 * 40000, SDS-PAGE
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C161H/C183H
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exhibiting severe defect in the activity
C161S/C164S
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displaying full disulfide reductase activity of wild-type enzyme
C164H/183H
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exhibiting severe defect in the activity
C183H
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displaying full disulfide reductase activity of wild-type enzyme
C186H
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displaying full disulfide reductase activity of wild-type enzyme
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ammonium sulfate precipitation, gel filtration, ion-exchange
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anion-exchange chromatography (DEAE) and gel filtration (Superdex 75)
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ion-exchange, gel filtration
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expressed in Escherichia coli strain BL21(DE3)
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Battelli, M.G.; Lorenzoni, E.
Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver
Biochem. J.
207
133-138
1982
Rattus norvegicus
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Battelli, M.G.
Enzymic conversion of rat liver xanthine oxidase from dehydrogenase (D form) to oxidase (O form)
FEBS Lett.
113
47-51
1980
Rattus norvegicus, Rattus norvegicus Wistar
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Shi, Y.; Tang, W.; Hao, S.; Wang, C.
Contributions of cysteine residues in Zn2 to zinc fingers and thiol-disulfide oxidoreductase activities of chaperone DnaJ
Biochemistry
44
1683-1689
2005
Escherichia coli
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Zhang, X.; Hu, Y.; Guo, X.; Lescop, E.; Li, Y.; Xia, B.; Jin, C.
The Bacillus subtilis YkuV is a thiol:disulfide oxidoreductase revealed by its redox structures and activity
J. Biol. Chem.
281
8296-8304
2006
Bacillus subtilis
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