We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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,
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
enzyme-thiol transhydrogenase (oxidized glutathione)
-
-
-
glutathione-dependent thiol:disulfide oxidoreductase
-
-
-
thiol-disulfide oxidoreductase
-
-
thiol:disulfide oxidoreductase
-
-
thiol:disulphide oxidoreductase
-
-
-
[xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
[xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] + 2 glutathione
[xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] + 2 glutathione
thioltransferase, GSH:insulin transhydrogenase and ricin-disulphide-bond reductase activity
-
[xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] + 2 glutathione
thioltransferase activity with cysteine as substrate. Mainly D-form of enzyme exists
-
[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
-
-
[xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] + 2 glutathione
thioltransferase activity with cysteine as substrate. Mainly D-form of enzyme exists
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
[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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
85030-79-1
formerly 12345-67-8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
[xanthine dehydrogenase] + oxidized glutathione
[xanthine oxidase] + glutathione
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
-
-
?
[xanthine dehydrogenase] + oxidized glutathione
[xanthine oxidase] + glutathione
-
reverse conversion possible by dithioerythritol, not obtained in presence of GSH
-
r
[xanthine dehydrogenase] + oxidized glutathione
[xanthine oxidase] + glutathione
-
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
-
r
[xanthine dehydrogenase] + oxidized glutathione
[xanthine oxidase] + glutathione
-
reverse conversion possible by dithioerythritol, not obtained in presence of GSH
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
insensitive against 1 mM CuSO4 and 1 mM N-ethylmaleimide at 37°C for 30 min
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Breast Neoplasms
Thioltransferase overexpression increases resistance of MCF-7 cells to adriamycin.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
372 U/mg, other definition of units
additional information
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
Wistar
-
-
brenda
newborn and adults
-
-
brenda
Wistar
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
highest amount of activity
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
A1K1L5_AZOSB
Azoarcus sp. (strain BH72)
175
0
19379
TrEMBL
-
Q5L7K1_BACFN
Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343)
356
0
40356
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
40000
-
1 * 40000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
monomer
-
1 * 40000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ammonium sulfate precipitation, gel filtration, ion-exchange
-
anion-exchange chromatography (DEAE) and gel filtration (Superdex 75)
-
ion-exchange, gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Escherichia coli strain BL21(DE3)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
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
brenda
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
brenda
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
brenda
Select items on the left to see more content.
html completed
HOME
login
history
all enzymes
BRENDA home
History
1.8.4.7 enzyme-thiol transhydrogenase (glutathione-disulfide)
more
top
Information
