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Enzyme Nomenclature
Information on EC 1.8.4.7 - enzyme-thiol transhydrogenase (glutathione-disulfide)
for references in articles please use BRENDA:EC1.8.4.7
Word Map on EC 1.8.4.7
- 1.8.4.7
- thioredoxins
-
dsbas
-
thioredoxin-like
- glutaredoxins
-
thioltransferase
-
cys-x-x-cys
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.8.4.7
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RECOMMENDED NAME
GeneOntology No.
enzyme-thiol transhydrogenase (glutathione-disulfide)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[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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-
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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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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
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redox reaction
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-
-
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reduction
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-
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
[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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CAS REGISTRY NUMBER
COMMENTARY
85030-79-1
formerly 12345-67-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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r
[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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r
[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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r
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C161S/C164S
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displaying full disulfide reductase activity of wild-type enzyme
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.4.7)
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