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IUBMB Comments A flavoprotein (FAD). Also acts, more slowly, on L-cysteine and several other thiols.
The enzyme appears in viruses and cellular organisms
Synonyms
glutathione oxidase, flavin-linked sulfhydryl oxidase,
more
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flavin adenine dinucleotide-linked sulfhydryl oxidase
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flavin-dependent sulfhydryl oxidase
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flavin-linked sulfhydryl oxidase
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glutathione sulfhydryl oxidase
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GSH sulfhydryl oxidase
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oxidase, glutathione
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sulfhydryl oxidase
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Sox1
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2 glutathione + O2 = glutathione disulfide + H2O2
a FAD flavoprotein, acts, more slowly, also on L-cysteine and several other thiols
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glutathione:oxygen oxidoreductase
A flavoprotein (FAD). Also acts, more slowly, on L-cysteine and several other thiols.
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2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
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-
-
?
2 D-Cys + O2
D-cystine + H2O2
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-
-
?
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
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-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
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-
-
?
2 L-Cys + O2
L-cystine + H2O2
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-
-
?
2-mercaptoethanol + O2
mercaptoethanol disulfide
cysteamine + O2
?
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slowly
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?
cysteine-glycine + O2
?
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enzyme immobilized on microelectrode sensor
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-
?
D-cysteine + O2
D-cystine
dithiothreitol + cytochrome c
dithiothreitol disulfide + reduced cytochrome c
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-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
glutathione + O2
glutathione disulfide + H2O2
L-cysteine + O2
L-cystine
L-cysteine ethyl ester + O2
L-cystine diethyl ester
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low activity
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-
?
L-cysteine methyl ester + O2
L-cystine dimethyl ester
N-acetyl-L-cysteine + O2
N,N'-diacetyl-L-cystine
R-SH + O2
R-S-S-R + H2O2
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-
-
-
?
S-methylglutathione + O2
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enzyme immobilized on microelectrode sensor, low activity
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?
thiophenol + O2
diphenyl sulfide
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slowly
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?
additional information
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2-mercaptoethanol + O2
mercaptoethanol disulfide
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slowly
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r
2-mercaptoethanol + O2
mercaptoethanol disulfide
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19% of the activity with glutathione
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?
2-mercaptoethanol + O2
mercaptoethanol disulfide
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?
D-cysteine + O2
D-cystine
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slowly
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?
D-cysteine + O2
D-cystine
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low activity
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?
dithiothreitol + O2
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low activity
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?
dithiothreitol + O2
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38% of the activity with glutathione
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?
dithiothreitol + O2
?
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?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
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?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
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?
glutathione + O2
glutathione disulfide + H2O2
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?
glutathione + O2
glutathione disulfide + H2O2
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?
glutathione + O2
glutathione disulfide + H2O2
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?
glutathione + O2
glutathione disulfide + H2O2
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enzyme immobilized on microsensor
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?
glutathione + O2
glutathione disulfide + H2O2
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enzyme immobilized on microsensor
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?
glutathione + O2
glutathione disulfide + H2O2
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measurement of H2O2 in vivo via microelectrodes with immobilized enzyme
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?
glutathione + O2
glutathione disulfide + H2O2
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measurement of glutathione in vivo via microelectrodes with immobilized enzyme
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?
glutathione + O2
glutathione disulfide + H2O2
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?
glutathione + O2
glutathione disulfide + H2O2
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?
L-cysteine + O2
L-cystine
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?
L-cysteine + O2
L-cystine
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low activity
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?
L-cysteine + O2
L-cystine
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?
L-cysteine + O2
L-cystine
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?
L-cysteine methyl ester + O2
L-cystine dimethyl ester
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slowly
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?
L-cysteine methyl ester + O2
L-cystine dimethyl ester
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slowly
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?
N-acetyl-L-cysteine + O2
N,N'-diacetyl-L-cystine
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slowly
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?
N-acetyl-L-cysteine + O2
N,N'-diacetyl-L-cystine
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low activity
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?
N-acetyl-L-cysteine + O2
N,N'-diacetyl-L-cystine
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slowly
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?
reduced RNase A + O2
?
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reduced RNase A + O2
?
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?
additional information
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ALT-2074, a catalytic mimic of glutathione oxidase, inhibits human cytochrome P450 3A isoforms in vitro
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?
additional information
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no other amio acids but D- and L-cysteine serve as substrate
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?
additional information
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D-penicilamine and coenzyme A are no substrates
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?
additional information
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no other amio acids but D- and L-cysteine serve as substrate
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?
additional information
?
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not: D,L-homocysteine
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?
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glutathione + O2
glutathione disulfide + H2O2
glutathione + O2
glutathione disulfide + H2O2
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?
glutathione + O2
glutathione disulfide + H2O2
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measurement of H2O2 in vivo via microelectrodes with immobilized enzyme
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?
glutathione + O2
glutathione disulfide + H2O2
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measurement of glutathione in vivo via microelectrodes with immobilized enzyme
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?
glutathione + O2
glutathione disulfide + H2O2
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?
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FAD
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flavoprotein
FAD
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1 mol FAD per mol of enzyme
FAD
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contains 2 mol of FAD per mol of enzyme
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AlCl3
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activates slightly
CaCl2
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activates slightly
FeCl2
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activates slightly
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CuSO4
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slight inhibition
MgSO4
1 mM, 55% residual activity
MnSO4
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slight inhibition
Na2SO4
1 mM, 61% residual activity
NiCl2
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slight inhibition
sodium dodecylsulfate
1 mM, 58% residual activity
thiols
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at high concentrations above 20 mM
Urea
1 mM, 80% residual activity
KI
1 mM, 65% residual activity
ZnSO4
1 mM, complete inhibition
ZnSO4
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complete inhibition at 1 mM
additional information
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EDTA has no effect on oxidation reaction
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additional information
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EDTA has no effect on oxidation reaction
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EDTA
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activates slightly
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Neoplasms
Biocompatible Ruthenium Single-Atom Catalyst for Cascade Enzyme-Mimicking Therapy.
Neoplasms
Self-Assembled Single-Site Nanozyme for Tumor-Specific Amplified Cascade Enzymatic Therapy.
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9.73 - 32
2-mercaptoethanol
0.01
cytochrome c
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wild type enzyme
9.73
2-mercaptoethanol
pH 7.5, 20°C
0.7
dithiothreitol
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1.3
dithiothreitol
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mutant enzyme C15A
1.7
dithiothreitol
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mutant enzyme C15A/C74A/C85A/C124A
1.8
dithiothreitol
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mutant enzyme C124A
2
dithiothreitol
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mutant enzyme C15A/C124A
2
dithiothreitol
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mutant enzyme C74A/C85A
2.1
dithiothreitol
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wild type enzyme
2.41
dithiothreitol
pH 7.5, 20°C
0.69
glutathione
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1.7
glutathione
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immobilized enzyme on sensor surface out of cellulose acetate
2.78
glutathione
pH 7.5, 20°C
3.6
L-cysteine
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50 - 100
2-mercaptoethanol
pH 7.5, 20°C
4.5
cytochrome c
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wild type enzyme
0.83 - 309000
dithiothreitol
3600000
glutathione
pH 7.5, 20°C
0.83
dithiothreitol
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mutant enzyme C74A/C85A
0.867
dithiothreitol
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mutant enzyme C15A
0.9
dithiothreitol
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mutant enzyme C124A
0.95
dithiothreitol
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mutant enzyme C15A/C124A
1.1
dithiothreitol
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wild type enzyme
1.25
dithiothreitol
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mutant enzyme C15A/C74A/C85A/C124A
309000
dithiothreitol
pH 7.5, 20°C
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515000
2-mercaptoethanol
pH 7.5, 20°C
128000
dithiothreitol
pH 7.5, 20°C
1290000
glutathione
pH 7.5, 20°C
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7
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substrate dithioerythritol
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3.8 - 11
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enzyme immobilized on microsensor surface out of cellulose acetate
6.2 - 8.8
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sharp decline in activity below pH 6.2 and above pH 8.8
5 - 10
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minimal activity below pH 5.0, active at least up to pH 10.0
5 - 10
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minimal activity below pH 5.0, active at least up to pH 10.0
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25
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assay with immobilized enzyme on microsensor
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brenda
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UniProt
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UniProt
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overview
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overview
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no activity in Mucor sp.
not: molds belonging to Rhizopus and Mucor
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no activity in Rhizopus sp.
not: molds belonging to Rhizopus and Mucor
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brenda
K-6-5
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brenda
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brenda
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brenda
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brenda
K-6-5
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brenda
overview
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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Q2UA33_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
384
0
42498
TrEMBL
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43959
x * 45000, SDS-PAGE, x * 43959, mass spectrometry
45000
x * 45000, SDS-PAGE, x * 43959, mass spectrometry
47000
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2 * 47000, SDS-PAGE
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?
x * 45000, SDS-PAGE, x * 43959, mass spectrometry
?
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x * 45000, SDS-PAGE, x * 43959, mass spectrometry
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dimer
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2 * 14000, SDS-PAGE, after centrifugation of infected cell extracts in glycerol gradients
dimer
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disulfide-bridged dimer (linked via C15-C124) with two free cysteine residues (C74 and 85) per monomer
dimer
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2 * 47000, SDS-PAGE
dimer
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2 * 47000, SDS-PAGE
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monomer
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1 * 14000, SDS-PAGE, in the infected cell
monomer
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1 * 66000, SDS-PAGE
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glycoprotein
sequence contains six potential N-glycosylation site. Deglycosylation reduces the molecluar mass to 40000 Da
glycoprotein
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sequence contains six potential N-glycosylation site. Deglycosylation reduces the molecluar mass to 40000 Da
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C124A
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reduced activity compared to wild type enzyme
C15A
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reduced activity compared to wild type enzyme
C15A/C124A
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reduced activity compared to wild type enzyme
C15A/C74A/C85A/C124A
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reduced activity compared to wild type enzyme
C74A/C85A
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reduced activity compared to wild type enzyme
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4 - 8
24 h, more than 80% of initial activity
724654
5.2 - 8.6
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45°C, 30 min
394886
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40
24 h, more than 70% of initial activity
50
1 h, 40% of initial activity
55
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30 min, no loss of activity
60
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3.5 min, 50% loss of activity
75
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30 min, complete loss of activity
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after 36 measurements with enzyme immobilized on microelectrode sensor loss of 30% activity
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after 50 measurements with enzyme immobilized on microelectrode sensor loss of 50% activity
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-20°C, 0.1 M, potassium phosphate buffer, pH 7.4, 6 months
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4°C, pH 6.5, phosphate buffer, immobilized enzyme on microelectrode sensor, loss of 20% activity, 60 days
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4°C, phosphate buffered saline, immobilized enzyme on microelectrode sensor, loss of 20% activity, 68 days
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glutathione-Sepharose 4B column chromatography
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expressed in Escherichia coli
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expressed in Escherichia coli strain XL-1
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expression in Trichoderma reesei
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medicine
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ALT-2074, a catalytic mimic of glutathione oxidase, inhibits human cytochrome P450 3A isoforms in vitro
analysis
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development of amperometric glutathione electrodes with immobilized enzyme for detection of H2O2
analysis
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development of a glutathione micro-enzyme sensor for amperometric detection in vivo, immobilization of enzyme on microelectrode tips
analysis
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development of an amperometric biosensor for determination of glutathione, by immobilizing covalently a glutathione oxidase onto the surface of gold coated magnetic nanoparticles modified Pt electrode. The electrode shows maximum response within 4 s, when polarizes at +0.4 V, pH 7.0 and 25°C. There is a linear relationship between electrode response and glutathione concentrations in the range 5.0-4000 microM with a detection limit of 0.1 microM. The biosensor shows 50% loss in its initial activity after its 150 uses over a period 4 months. Glutathione concentration in hemolysated erythrocytes as measured by the present biosensor is 2.8 mM in apparently healthy persons
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Kusakabe, H.; Midorikawa, Y.; Kuninaka, A.; Yoshino, H.
Distribution of extracellular oxygen related enzymes in molds
Agric. Biol. Chem.
47
1385-1387
1983
Aspergillus sp., Penicillium sp., Fusarium sp., no activity in Mucor sp., no activity in Rhizopus sp.
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brenda
Ostrowski, M.C.; Kistler, W.S.
Properties of a flavoprotein sulfhydryl oxidase from rat seminal vesicle secretion
Biochemistry
19
2639-2645
1980
Rattus norvegicus
brenda
Kusakaba, H.; Kuninaka, A.; Yoshino, H.
Purification and properties of a new enzyme, glutathione oxidase from Penicillium sp. K-6-5
Agric. Biol. Chem.
46
2057-2067
1982
Penicillium sp., Penicillium sp. K-6-5
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brenda
Huang, Z.; Villarta-Snow, R.L.; Lubrano, G.J.; Guilbault, G.G.
Glutathione amperometric enzyme microsensor
Anal. Lett.
27
263-271
1994
Penicillium sp.
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brenda
Compagnone, D.; Federici, G.; Scarciglia, L.; Palleschi, G.
Amperometric glutathione electrodes
Biosens. Bioelectron.
8
257-263
1993
Penicillium sp.
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brenda
Farrell, S.R.; Thorpe, C.
Augmenter of liver regeneration: a flavin-dependent sulfhydryl oxidase with cytochrome c reductase activity
Biochemistry
44
1532-1541
2005
Homo sapiens
brenda
Rodriguez, I.; Redrejo-Rodriguez, M.; Rodriguez, J.M.; Alejo, A.; Salas, J.; Salas, M.L.
African swine fever virus pB119L protein is a flavin adenine dinucleotide-linked sulfhydryl oxidase
J. Virol.
80
3157-3166
2006
African swine fever virus
brenda
Greenblatt, D.J.; Peters, D.E.; Oleson, L.E.; Harmatz, J.S.; MacNab, M.W.; Berkowitz, N.; Zinny, M.A.; Court, M.H.
Inhibition of oral midazolam clearance by boosting doses of ritonavir, and by 4,4-dimethyl-benziso-(2H)-selenazine (ALT-2074), an experimental catalytic mimic of glutathione oxidase
Br. J. Clin. Pharmacol.
68
920-927
2009
Homo sapiens
brenda
Faccio, G.; Kruus, K.; Buchert, J.; Saloheimo, M.
Secreted fungal sulfhydryl oxidases: Sequence analysis and characterisation of a representative flavin-dependent enzyme from Aspergillus oryzae
BMC Biochem.
11
31
2010
Aspergillus oryzae (Q2UA33), Aspergillus oryzae ATCC 42149 (Q2UA33)
brenda
Chauhan, N.; Narang, J.; Meena, J.; Pundir, C.S.
An amperometric glutathione biosensor based on chitosan-iron coated gold nanoparticles modified Pt electrode
Int. J. Biol. Macromol.
51
879-886
2012
unidentified
brenda
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