Information on EC 1.20.4.2 - methylarsonate reductase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.20.4.2
-
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RECOMMENDED NAME
GeneOntology No.
methylarsonate reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O
show the reaction diagram
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
arsenate detoxification I (glutaredoxin)
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-
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SYSTEMATIC NAME
IUBMB Comments
gluthathione:methylarsonate oxidoreductase
The product, methylarsonite, is biologically methylated by EC 2.1.1.137, arsenite methyltransferase, to form cacodylic acid.
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CAS REGISTRY NUMBER
COMMENTARY hide
254889-62-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arsenate + glutathione
arsenite + reduced glutathione
show the reaction diagram
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-
-
-
?
dimethylarsonate + glutathione
dimethylarsonous acid
show the reaction diagram
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-
-
-
?
methylarsonate + glutathione
methylarsonite + glutathione disulfide
show the reaction diagram
methylarsonate + glutathione
methylarsonite + oxidized glutathione
show the reaction diagram
-
rate-limiting enzyme in biotransformation of inorganic arsenite in rabbit liver
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-
?
monomethylarsonate + glutathione
monomethylarsonous acid + oxidized glutathione
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
methylarsonate + glutathione
methylarsonite + glutathione disulfide
show the reaction diagram
methylarsonate + glutathione
methylarsonite + oxidized glutathione
show the reaction diagram
-
rate-limiting enzyme in biotransformation of inorganic arsenite in rabbit liver
-
-
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sodium deoxycholate
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-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
stimulates
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
109
arsenate
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-
20.9
dimethylarsonate
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-
2.1
monomethylarsonate
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-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.27
GSTO1 mutant A140D, 30°C, pH 5.5
0.33
wild-type GSTO1, 30°C, pH 5.5
0.39
GSTO1 mutant E208K, 30°C, pH 5.5
0.42
wild-type GSTO1, 30°C, pH 5.5
0.44
GSTO2 mutant N142D, 30°C, pH 5.5
0.65
GSTO1 mutant DELTAE155, 30°C, pH 5.5
0.67
GSTO1 mutant DELTAE155/E208K, 30°C, pH 5.5
additional information
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-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.2
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-
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
SDS-PAGE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
wild-type, 30 min, 60% residual activity. GSTO1 mutant E208K, 30 min, 80% residual activity, GSTO1 mutant DELTAE155/E208K, 30 min, no residual activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A140D
isoform GSTO2, natural polymorphism, no significant alteration in monomethylarsonate reductase activity
DELTAE155
isoform GSTO2, natural polymorphism, 90% increase in monomethylarsonate reductase activity
DELTAE155/E208K
isoform GSTO2, natural polymorphism, 100% increase in monomethylarsonate reductase activity, decrease in heat stability
E208K
isoform GSTO2, natural polymorphism, slight increase in monomethylarsonate reductase activity, decrease in heat stability
N142D
isoform GSTO2, natural polymorphism, no significant alteration in monomethylarsonate reductase activity
additional information
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naturally occurring mutations S86C, A140D, E155del, A236V, and E208K significantly decrease enzyme activity
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LINKS TO OTHER DATABASES (specific for EC-Number 1.20.4.2)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)