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Information on EC 1.20.4.2 - methylarsonate reductase and Organism(s) Homo sapiens and UniProt Accession P78417

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EC Tree
IUBMB Comments
The product, methylarsonite, is biologically methylated by EC 2.1.1.137, arsenite methyltransferase, to form cacodylic acid.
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This record set is specific for:
Homo sapiens
UNIPROT: P78417
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
gsto1, gsto2, mma(v) reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomethylarsonic acid (MMA V) reductase/hGSTO1
-
MMA(V) reductase
-
-
-
-
reductase, methylarsonate
-
-
-
-
additional information
identical to omega class glutathione-S-transferase (hGSTO1-1)
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
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reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
glutathione:methylarsonate oxidoreductase
The product, methylarsonite, is biologically methylated by EC 2.1.1.137, arsenite methyltransferase, to form cacodylic acid.
CAS REGISTRY NUMBER
COMMENTARY hide
254889-62-8
-
SUBSTRATE
PRODUCT                       
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
monomethylarsonate + glutathione
monomethylarsonous acid + oxidized glutathione
show the reaction diagram
-
-
-
?
monomethylarsonate + glutathione
monomethylarsonous acid + oxidized glutathione
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sodium deoxycholate
-
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GSTO1_HUMAN
241
0
27566
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
SDS-PAGE
PROTEIN VARIANTS
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zakharyan, R.A.; Aposhian, H.V.
Enzymatic reduction of arsenic compounds in mammalian systems: the rate-limiting enzyme of rabbit liver arsenic biotransformation is MMA(V) reductase
Chem. Res. Toxicol.
12
1278-1283
1999
Homo sapiens, Oryctolagus cuniculus
Manually annotated by BRENDA team
Zakharyan, R.A.; Sampayo-Reyes, A.; Healy, S.M.; Tsaprailis, G.; Board, P.G.; Liebler, D.C.; Aposhian, H.V.
Human monomethylarsonic acid (MMA(V)) reductase is a member of the glutathione-S-transferase superfamily
Chem. Res. Toxicol.
14
1051-1057
2001
Homo sapiens (P78417), Homo sapiens
Manually annotated by BRENDA team
Marnell, L.L.; Garcia-Vargas, G.G.; Chowdhury, U.K.; Zakharyan, R.A.; Walsh, B.; Avram, M.D.; Kopplin, M.J.; Cebrian, M.E.; Silbergeld, E.K.; Aposhian, H.V.
Polymorphisms in the human monomethylarsonic acid (MMA V) reductase/hGSTO1 gene and changes in urinary arsenic profiles
Chem. Res. Toxicol.
16
1507-1513
2003
Homo sapiens (P78417), Homo sapiens
Manually annotated by BRENDA team
Schmuck, E.M.; Board, P.G.; Whitbread, A.K.; Tetlow, N.; Cavanaugh, J.A.; Blackburn, A.C.; Masoumi, A.
Characterization of the monomethylarsonate reductase and dehydroascorbate reductase activities of Omega class glutathione transferase variants: implications for arsenic metabolism and the age-at-onset of Alzheimers and Parkinsons diseases
Pharmacogenet. Genomics
15
493-501
2005
Homo sapiens (P78417), Homo sapiens
Manually annotated by BRENDA team