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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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
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 hide
ORGANISM
UNIPROT
LITERATURE
[xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] + 2 glutathione
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glutathione metabolism
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-
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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 hide
85030-79-1
formerly 12345-67-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Wistar
-
-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[xanthine dehydrogenase] + oxidized glutathione
[xanthine oxidase] + glutathione
show the reaction diagram
additional information
?
-
-
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
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 hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Q5L7K1
Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
1 * 40000, SDS-PAGE
43000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
-
monomer
-
1 * 40000, SDS-PAGE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, gel filtration, ion-exchange
-
anion-exchange chromatography (DEAE) and gel filtration (Superdex 75)
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ion-exchange, gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21(DE3)
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C161H/C183H
-
exhibiting severe defect in the activity
C161S/C164S
-
displaying full disulfide reductase activity of wild-type enzyme
C164H/183H
-
exhibiting severe defect in the activity
C183H
-
displaying full disulfide reductase activity of wild-type enzyme
C186H
-
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)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)