Information on EC 1.8.3.3 - glutathione oxidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

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
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
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AlCl3
-
activates slightly
CaCl2
-
activates slightly
FeCl2
-
activates slightly
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
-
activates slightly
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
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
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
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
-