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Information on EC 1.8.3.3 - glutathione oxidase
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1.8.3.3 glutathione oxidaseIUBMB Comments
A flavoprotein (FAD). Also acts, more slowly, on L-cysteine and several other thiols.
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Word Map
- 1.8.3.3
- fad
- oxidases
- transpeptidase
-
gamma-glutamyl
- gamma-glutamyltransferase
- analysis
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
glutathione oxidase, flavin-linked sulfhydryl oxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glutathione sulfhydryl oxidase
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GSH oxidase >
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GSH sulfhydryl oxidase
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oxidase, glutathione
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Sox1
sulfhydryl oxidase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 glutathione + O2 = glutathione disulfide + H2O2
a FAD flavoprotein, acts, more slowly, also on L-cysteine and several other thiols
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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-
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reduction
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
glutathione:oxygen oxidoreductase
A flavoprotein (FAD). Also acts, more slowly, on L-cysteine and several other thiols.
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CAS REGISTRY NUMBER
COMMENTARY
55467-56-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dithiothreitol + cytochrome c
dithiothreitol disulfide + reduced cytochrome c
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-
-
-
?
S-methylglutathione + O2
?
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enzyme immobilized on microelectrode sensor, low activity
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?
2-mercaptoethanol + O2
mercaptoethanol disulfide
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19% of the activity with glutathione
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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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?
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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Penicillium sp. K-6-5
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no other amio acids but D- and L-cysteine serve as substrate
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.7
glutathione
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immobilized enzyme on sensor surface out of cellulose acetate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.8 - 11
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enzyme immobilized on microsensor surface out of cellulose acetate
5 - 10
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q2UA33_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
384
0
42498
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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