Information on EC 1.8.3.3 - glutathione oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
1.8.3.3
-
RECOMMENDED NAME
GeneOntology No.
glutathione oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 glutathione + O2 = glutathione disulfide + H2O2
show the reaction diagram
a FAD flavoprotein, acts, more slowly, also on L-cysteine and several other thiols
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Glutathione metabolism
-
SYSTEMATIC NAME
IUBMB Comments
glutathione:oxygen oxidoreductase
A flavoprotein (FAD). Also acts, more slowly, on L-cysteine and several other thiols.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
flavin adenine dinucleotide-linked sulfhydryl oxidase
-
-
flavin-dependent sulfhydryl oxidase
-
-
flavin-linked sulfhydryl oxidase
-
-
glutathione sulfhydryl oxidase
-
-
-
-
GSH oxidase >
-
-
-
-
GSH sulfhydryl oxidase
-
-
-
-
oxidase, glutathione
-
-
-
-
protein pB119L
-
-
Sox1
Q2UA33
-
Sox1
Aspergillus oryzae ATCC 42149
Q2UA33
-
-
sulfhydryl oxidase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
55467-56-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Aspergillus oryzae ATCC 42149
-
UniProt
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
no activity in Mucor sp.
not: molds belonging to Rhizopus and Mucor
-
-
Manually annotated by BRENDA team
no activity in Rhizopus sp.
not: molds belonging to Rhizopus and Mucor
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
Penicillium sp. K-6-5
K-6-5
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 2-mercaptoethanol + O2
(ethyldisulfanyl)ethane + H2O2
show the reaction diagram
Q2UA33
-
-
-
?
2 D-Cys + O2
D-cystine + H2O2
show the reaction diagram
Q2UA33
-
-
-
-
2 dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
Q2UA33
-
-
-
?
2 glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
Q2UA33
-
-
-
?
2 L-Cys + O2
L-cystine + H2O2
show the reaction diagram
Q2UA33
-
-
-
-
2-mercaptoethanol + O2
mercaptoethanol disulfide
show the reaction diagram
-
-
-
-
-
2-mercaptoethanol + O2
mercaptoethanol disulfide
show the reaction diagram
-
slowly
-
-
r
2-mercaptoethanol + O2
mercaptoethanol disulfide
show the reaction diagram
-
19% of the activity with glutathione
-
-
?
cysteamine + O2
?
show the reaction diagram
-
slowly
-
-
?
cysteine-glycine + O2
?
show the reaction diagram
-
enzyme immobilized on microelectrode sensor
-
-
?
D-cysteine + O2
D-cystine
show the reaction diagram
-
slowly
-
-
?
D-cysteine + O2
D-cystine
show the reaction diagram
-
low activity
-
-
?
dithiothreitol + cytochrome c
dithiothreitol disulfide + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
?
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
?
show the reaction diagram
-
low activity
-
-
?
dithiothreitol + O2
?
show the reaction diagram
-
38% of the activity with glutathione
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
-
-
-
?
dithiothreitol + O2
dithiothreitol disulfide + H2O2
show the reaction diagram
-
-
-
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
-
-
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
-
-
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
-
-
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
-
-
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
enzyme immobilized on microsensor
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
enzyme immobilized on microsensor, measurement of H2O2 in vivo via microelectrodes with immobilized enzyme
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
measurement of glutathione in vivo via microelectrodes with immobilized enzyme
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
Penicillium sp. K-6-5
-
-
-
-
?
L-cysteine + O2
L-cystine
show the reaction diagram
-
-
-
-
?
L-cysteine + O2
L-cystine
show the reaction diagram
-
-
-
-
?
L-cysteine + O2
L-cystine
show the reaction diagram
-
low activity
-
-
?
L-cysteine + O2
L-cystine
show the reaction diagram
Penicillium sp. K-6-5
-
-
-
-
?
L-cysteine ethyl ester + O2
L-cystine diethyl ester
show the reaction diagram
-
low activity
-
-
?
N-acetyl-L-cysteine + O2
N,N'-diacetyl-L-cystine
show the reaction diagram
-
slowly
-
-
?
N-acetyl-L-cysteine + O2
N,N'-diacetyl-L-cystine
show the reaction diagram
-
low activity
-
-
?
N-acetyl-L-cysteine + O2
N,N'-diacetyl-L-cystine
show the reaction diagram
Penicillium sp. K-6-5
-
slowly
-
-
?
R-SH + O2
R-S-S-R + H2O2
show the reaction diagram
-
-
-
-
?
reduced RNase A + O2
?
show the reaction diagram
-
-
-
-
?
reduced RNase A + O2
?
show the reaction diagram
-
-
-
-
?
S-methylglutathione + O2
?
show the reaction diagram
-
enzyme immobilized on microelectrode sensor, low activity
-
-
?
thiophenol + O2
diphenyl sulfide
show the reaction diagram
-
slowly
-
-
?
L-cysteine methyl ester + O2
L-cystine dimethyl ester
show the reaction diagram
Penicillium sp., Penicillium sp. K-6-5
-
slowly
-
-
?
additional information
?
-
-
not: D,L-homocysteine
-
-
-
additional information
?
-
-
no other amio acids but D- and L-cysteine serve as substrate
-
-
-
additional information
?
-
-
D-penicilamine and coenzyme A are no substrates
-
-
-
additional information
?
-
-
ALT-2074, a catalytic mimic of glutathione oxidase, inhibits human cytochrome P450 3A isoforms in vitro
-
-
-
additional information
?
-
Penicillium sp. K-6-5
-
no other amio acids but D- and L-cysteine serve as substrate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
-
-
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
measurement of H2O2 in vivo via microelectrodes with immobilized enzyme
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
-
measurement of glutathione in vivo via microelectrodes with immobilized enzyme
-
?
glutathione + O2
glutathione disulfide + H2O2
show the reaction diagram
Penicillium sp. K-6-5
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
1 mol FAD per mol of enzyme; flavoprotein
FAD
-
contains 2 mol of FAD per mol of enzyme; flavoprotein
FAD
-
flavoprotein
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AlCl3
-
activates slightly
CaCl2
-
activates slightly
FeCl2
-
activates slightly
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
CuSO4
-
slight inhibition
KCl
-
slight inhibition
KI
-
slight inhibition
KI
Q2UA33
1 mM, 65% residual activity
MgSO4
Q2UA33
1 mM, 55% residual activity
Na2SO4
Q2UA33
1 mM, 61% residual activity
NiCl2
-
slight inhibition
sodium dodecylsulfate
Q2UA33
1 mM, 58% residual activity
thiols
-
at high concentrations above 20 mM
Urea
Q2UA33
1 mM, 80% residual activity
ZnSO4
-
complete inhibition at 1 mM
ZnSO4
Q2UA33
1 mM, complete inhibition
MnSO4
-
slight inhibition
additional information
-
EDTA has no effect on oxidation reaction
-
additional information
-
EDTA has no effect on oxidation reaction
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
-
activates slightly
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
9.73
-
2-mercaptoethanol
Q2UA33
pH 7.5, 20C
32
-
2-mercaptoethanol
-
-
0.01
-
cytochrome c
-
wild type enzyme
1.55
-
D-Cys
Q2UA33
pH 7.5, 20C
0.7
-
dithiothreitol
-
-
1.3
-
dithiothreitol
-
mutant enzyme C15A
1.7
-
dithiothreitol
-
mutant enzyme C15A/C74A/C85A/C124A
1.8
-
dithiothreitol
-
mutant enzyme C124A
2
-
dithiothreitol
-
mutant enzyme C15A/C124A; mutant enzyme C74A/C85A
2.1
-
dithiothreitol
-
wild type enzyme
2.41
-
dithiothreitol
Q2UA33
pH 7.5, 20C
6.7
-
dithiothreitol
-
-
0.69
-
glutathione
-
-
1.7
-
glutathione
-
immobilized enzyme on sensor surface out of cellulose acetate
2.78
-
glutathione
Q2UA33
pH 7.5, 20C
4.4
-
glutathione
-
-
6.11
-
L-Cys
Q2UA33
pH 7.5, 20C
3.6
-
L-cysteine
-
-
9.1
-
L-cysteine
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
50
100
2-mercaptoethanol
Q2UA33
pH 7.5, 20C
4.5
-
cytochrome c
-
wild type enzyme
5950
-
D-Cys
Q2UA33
pH 7.5, 20C
0.83
-
dithiothreitol
-
mutant enzyme C74A/C85A
0.867
-
dithiothreitol
-
mutant enzyme C15A
0.9
-
dithiothreitol
-
mutant enzyme C124A
0.95
-
dithiothreitol
-
mutant enzyme C15A/C124A
1.1
-
dithiothreitol
-
wild type enzyme
1.25
-
dithiothreitol
-
mutant enzyme C15A/C74A/C85A/C124A
309000
-
dithiothreitol
Q2UA33
pH 7.5, 20C
3600000
-
glutathione
Q2UA33
pH 7.5, 20C
52300
-
L-Cys
Q2UA33
pH 7.5, 20C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
515000
-
2-mercaptoethanol
Q2UA33
pH 7.5, 20C
2666
3840
-
D-Cys
Q2UA33
pH 7.5, 20C
9121
128000
-
dithiothreitol
Q2UA33
pH 7.5, 20C
9992
1290000
-
glutathione
Q2UA33
pH 7.5, 20C
10966
8560
-
L-Cys
Q2UA33
pH 7.5, 20C
12146
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
substrate dithioerythritol
8
-
Q2UA33
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.8
11
-
enzyme immobilized on microsensor surface out of cellulose acetate
5
10
-
minimal activity below pH 5.0, active at least up to pH 10.0
5
10
-
minimal activity below pH 5.0, active at least up to pH 10.0
6.2
8.8
-
sharp decline in activity below pH 6.2 and above pH 8.8
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
25
-
-
assay with immobilized enzyme on microsensor
30
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Penicillium sp. K-6-5
-
-
-
-
Manually annotated by BRENDA team
Penicillium sp. K-6-5
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
14000
-
-
SDS-PAGE
28000
-
-
SDS-PAGE
66000
-
-
gel filtration
95000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q2UA33
x * 45000, SDS-PAGE, x * 43959, mass spectrometry
?
Aspergillus oryzae ATCC 42149
-
x * 45000, SDS-PAGE, x * 43959, mass spectrometry
-
dimer
-
2 * 47000, SDS-PAGE
dimer
-
disulfide-bridged dimer (linked via C15-C124) with two free cysteine residues (C74 and 85) per monomer
dimer
-
2 * 14000, SDS-PAGE, after centrifugation of infected cell extracts in glycerol gradients
dimer
Penicillium sp. K-6-5
-
2 * 47000, SDS-PAGE
-
monomer
-
1 * 66000, SDS-PAGE
monomer
-
1 * 14000, SDS-PAGE, in the infected cell
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
Q2UA33
sequence contains six potential N-glycosylation site. Deglycosylation reduces the molecluar mass to 40000 Da
glycoprotein
Aspergillus oryzae ATCC 42149
-
sequence contains six potential N-glycosylation site. Deglycosylation reduces the molecluar mass to 40000 Da
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
8
Q2UA33
24 h, more than 80% of initial activity
5.2
8.6
-
45C, 30 min
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
Q2UA33
24 h, more than 70% of initial activity
50
-
Q2UA33
1 h, 40% of initial activity
55
-
-
30 min, no loss of activity
57
-
Q2UA33
melting temperature
60
-
-
3.5 min, 50% loss of activity
75
-
-
30 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
after 36 measurements with enzyme immobilized on microelectrode sensor loss of 30% activity
-
after 50 measurements with enzyme immobilized on microelectrode sensor loss of 50% activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 0.1 M, potassium phosphate buffer, pH 7.4, 6 months
-
4C, pH 6.5, phosphate buffer, immobilized enzyme on microelectrode sensor, loss of 20% activity, 60 days
-
4C, phosphate buffered saline, immobilized enzyme on microelectrode sensor, loss of 20% activity, 68 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glutathione-Sepharose 4B column chromatography
-
recombinant protein
Q2UA33
gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli strain XL-1
-
expression in Trichoderma reesei
Q2UA33
expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C124A
-
reduced activity compared to wild type enzyme
C15A
-
reduced activity compared to wild type enzyme
C15A/C124A
-
reduced activity compared to wild type enzyme
C15A/C74A/C85A/C124A
-
reduced activity compared to wild type enzyme
C74A/C85A
-
reduced activity compared to wild type enzyme
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in 8M urea
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
ALT-2074, a catalytic mimic of glutathione oxidase, inhibits human cytochrome P450 3A isoforms in vitro
analysis
-
development of a glutathione micro-enzyme sensor for amperometric detection in vivo, immobilization of enzyme on microelectrode tips
analysis
-
development of amperometric glutathione electrodes with immobilized enzyme for detection of H2O2
analysis
-
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 25C. 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