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Information on EC 2.1.1.137 - arsenite methyltransferase
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2.1.1.137 arsenite methyltransferaseIUBMB Comments
An enzyme of the biotransformation pathway that forms dimethylarsinate from inorganic arsenite and arsenate. It methylates arsenite to form methylarsonate, Me-AsO3H2, which is reduced by EC 1.20.4.2, methylarsonate reductase, to methylarsonite, Me-As(OH)2. Methylarsonite is also a substrate for this enzyme (EC 2.1.1.137), which converts it into the much less toxic compound dimethylarsinate (cacodylate), Me2As(O)-OH.
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Word Map
- 2.1.1.137
-
dimethylarsinic
-
monomethylarsonic
-
trivalent
-
arsenic-induced
-
metalloid
-
arsenic-related
-
biomethylation
- trimethylarsine
- dimethylarsenate
-
dmasiii
-
gstos
-
organoarsenical
-
arsenic-contaminated
-
methylarsenicals
-
as-contaminated
-
hplc-icpms
- cyanidioschyzon
-
arsenic-exposed
-
methylarsonic
- medicine
- degradation
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
AdoMet:arsenic(III) methyltransferase, arsenic (+3 oxidation state) methyltransferase, arsenic (+3 oxidation state)-methyltransferase, arsenic (+3) methyltransferase, arsenic (III) methyltransferase, arsenic (III) S-adenosylmethionine methyltransferase, arsenic methyltransferase Cyt19, arsenic(III) methyltransferase, arsenite (+3 oxidation state) methyltransferase, arsenite methyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
arsenic (+3 oxidation state) methyltransferase
arsenic (+3) methyltransferase
arsenite (+3 oxidation state) methyltransferase
arsenite methyltransferase
arsenite S-adenosylmethionine methyltransferase
ArsM
ArsM protein
As(III) S-adenosylmethionine methyltransferase
AS3MT
EC 2.1.1.138
-
-
formerly
-
S-adenosyl-L-methionine:arsenic(III) methyltransferase
arsenic (+3 oxidation state) methyltransferase
-
-
arsenic (+3 oxidation state) methyltransferase
-
AS3MT
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + methylarsonite = S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
-
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
reaction mechanism, overview
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
reaction modelling, overview
-
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
reaction modelling, overview
-
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
reaction modelling, overview
-
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
reaction modelling, overview
-
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
reaction modelling, overview
-
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
reaction modelling, overview
-
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
reaction modelling, overview
-
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
reaction modelling, overview
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
reaction modelling, overview
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
reaction modelling, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
transfer of methyl group
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:arsenite As-methyltransferase
An enzyme of the biotransformation pathway that forms dimethylarsinate from inorganic arsenite and arsenate. It methylates arsenite to form methylarsonate, Me-AsO3H2, which is reduced by EC 1.20.4.2, methylarsonate reductase, to methylarsonite, Me-As(OH)2. Methylarsonite is also a substrate for this enzyme (EC 2.1.1.137), which converts it into the much less toxic compound dimethylarsinate (cacodylate), Me2As(O)-OH.
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CAS REGISTRY NUMBER
COMMENTARY
167140-41-2
-
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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
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsenate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsenate(III)
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsenite + dimethylarsenite + trimethylarsine
Cyanidioschyzon sp.
-
the first product, methylarsenite, undergoes a second round of methylation faster than it dissociates from the enzyme. The second product, dimethylarsenite, dissociates faster than it undergoes the third round of methylation to the third and final product, trimethylarsine
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate + dimethylarsinous acid + dimethylarsinic acid
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + monomethylarsenate + dimethylarsenate
-
maximal conversion of arsenite to monomethylarsenate occurs at about 0.1 mM arsenite. Higher substrate concentrations inhibit monomethylarsenate yields. The production of dimethylarsenate increases as arsenite concentration increases from 0.0005 to 0.0083 mM, and then quickly decreases to zero
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + monomethylarsonate + dimethylarsinic acid
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + monomethylarsonous acid + monomethylarsonic acid + dimethylarsinic acid
-
the enzyme methylates arsenite to dimethylarsinic acid as an end product and produces monomethylarsonous acid and monomethylarsonic acid as intermediates
-
-
?
S-adenosyl-L-methionine + methylarsinate
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
-
?
S-adenosyl-L-methionine + methylarsonate
S-adenosyl-L-homocysteine + dimethylarsinous acid
-
-
-
?
S-adenosyl-L-methionine + methylarsonate
S-adenosyl-L-homocysteine + dimethylarsinous acid + dimethylarsinic acid
-
-
-
-
?
S-adenosyl-L-methionine + phenylarsenite
S-adenosyl-L-homocysteine + phenylmethylarsenate(III)
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
Cyanidioschyzon sp.
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
AS3MT may contribute to variation in arsenic metabolism and, perhaps, arsenic-dependent carcinogenesis in humans
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
hAS3MT is the key enzyme in the pathway for methylation of iAs in human hepatic cells
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
As3MT enzyme is indispensable for conversion of the arsenic metabolites to their corresponding methylated products, metabolism of arsenic proceeds through sequential reduction and oxidative methylation involving several enzymes including the arsenic (+3) methyltransferase, overview
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
methylation of environmental arsenic by conversion to soluble and gaseous methylated species is a detoxifying process that may contribute to global cycling of arsenic
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
ArsM catalyzes the formation of a number of methylated intermediates from arsenite, with trimethylarsine as the end product
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
methylation of environmental arsenic by conversion to soluble and gaseous methylated species is a detoxifying process that may contribute to global cycling of arsenic
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
ArsM catalyzes the formation of a number of methylated intermediates from arsenite, with trimethylarsine as the end product
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
Cyanidioschyzon sp.
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
the enzyme also produces also produces dimethylarsine and trimethylarsine gases as by-products
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
the enzyme also produces also produces dimethylarsine and trimethylarsine gases as by-products
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
-
?
additional information
?
-
-
upon incubation with arsenite, dimethylarsinate and a small amount of methylarsinate are detected in the reaction system within 0.5 h
-
-
-
additional information
?
-
As3MT methylates inorganic arsenic and its metabolites
-
-
?
additional information
?
-
genetic susceptibility to arsenic toxicity in Asian is different from Africans and Caucasians, overview
-
-
?
additional information
?
-
-
genetic susceptibility to arsenic toxicity in Asian is different from Africans and Caucasians, overview
-
-
?
additional information
?
-
the enzyme does not methylate selenium and tellurium
-
-
?
additional information
?
-
-
the enzyme is responsible for the removal of arsenic as the volatile arsines from the bacteria producing trimethylarsine via successive methylation
-
-
?
additional information
?
-
-
enzyme evolutionary analysis
-
-
?
additional information
?
-
-
besides methylarsonate and dimethylarsinate, the enzyme also produces trimethylarsenite and dimethylarsine gases
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
Cyanidioschyzon sp.
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
AS3MT may contribute to variation in arsenic metabolism and, perhaps, arsenic-dependent carcinogenesis in humans
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
hAS3MT is the key enzyme in the pathway for methylation of iAs in human hepatic cells
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
As3MT enzyme is indispensable for conversion of the arsenic metabolites to their corresponding methylated products, metabolism of arsenic proceeds through sequential reduction and oxidative methylation involving several enzymes including the arsenic (+3) methyltransferase, overview
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
methylation of environmental arsenic by conversion to soluble and gaseous methylated species is a detoxifying process that may contribute to global cycling of arsenic
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
methylation of environmental arsenic by conversion to soluble and gaseous methylated species is a detoxifying process that may contribute to global cycling of arsenic
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
Cyanidioschyzon sp.
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
the enzyme also produces also produces dimethylarsine and trimethylarsine gases as by-products
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
the enzyme also produces also produces dimethylarsine and trimethylarsine gases as by-products
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
-
-
-
-
?
additional information
?
-
As3MT methylates inorganic arsenic and its metabolites
-
-
?
additional information
?
-
genetic susceptibility to arsenic toxicity in Asian is different from Africans and Caucasians, overview
-
-
?
additional information
?
-
-
genetic susceptibility to arsenic toxicity in Asian is different from Africans and Caucasians, overview
-
-
?
additional information
?
-
-
the enzyme is responsible for the removal of arsenic as the volatile arsines from the bacteria producing trimethylarsine via successive methylation
-
-
?
additional information
?
-
-
enzyme evolutionary analysis
-
-
?
additional information
?
-
-
besides methylarsonate and dimethylarsinate, the enzyme also produces trimethylarsenite and dimethylarsine gases
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
arsenite
-
the enzyme activity is completely inhibited by elevated concentrations of the substrate arsenite (0.2 mM)
trimethyl-selenonium iodide
-
weak activator of recombinant As(III)-methyltransferase, weak inhibitor of arsenite methylation in hepatocytes
trimethylselenonium iodide
-
weak activator of recombinant As(III)-methyltransferase, weak inhibitor of arsenite methylation in hepatocytes
dimethylselenoxide
-
weak activator of recombinant As(III)-methyltransferase, weak inhibitor of arsenite methylation in hepatocytes
dimethylselenoxide
-
weak activator of recombinant As(III)-methyltransferase, weak inhibitor of arsenite methylation in hepatocytes
GSH
addition of GSH stimulates the overall rate for As methylation, but inhibits formation of trimethylarsenite
GSH
suppression of formation of trimethylarsine oxide, stimulatory effect on the rate of methylarsonate and dimethylarsinate production from arsenite is concentration-dependent
GSH
addition of GSH stimulates the overall rate for As methylation, but inhibits formation of trimethylarsenite
Selenite
-
addition of selenite at 1:10 molar ratio with arsenite in the reaction mixture completely abolishes the arsenic methylation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
trimethyl-selenonium iodide
-
weak activator of recombinant As(III)-methyltransferase, weak inhibitor of arsenite methylation in hepatocytes
trimethylselenonium iodide
-
weak activator of recombinant As(III)-methyltransferase, weak inhibitor of arsenite methylation in hepatocytes
dimethylselenoxide
-
weak activator of recombinant As(III)-methyltransferase, weak inhibitor of arsenite methylation in hepatocytes
dimethylselenoxide
-
weak activator of recombinant As(III)-methyltransferase, weak inhibitor of arsenite methylation in hepatocytes
glutathione
ArsM is able to methylate As(III) in the presence of Cys without glutathione. In contrast, ArsM is not able to methylate As(III) in the presence of tris(2-carboxyethyl)phosphine without GSH
glutathione
-
a 4fold increase in glutathione concentration, 2 to 8 mM, leads to a 2fold increase in enzyme activity, reducing environment is required for enzyme activity
glutathione
Cyanidioschyzon sp.
-
As(III) SAM methyltransferase conducts three successive rounds of oxidative methylation, with the glutathione conjugates serving as metalloid donors to the enzyme
glutathione
-
1 mM GSH decreases Km and increases Vmax estimates for arsenite and methylarsonous acid
glutathione
-
GSH should combine with the enzyme after the methylation to reduce the disulfide bond formed during the catalytic cycle to resume the active form of the enzyme
GSH
-
nonenzymatic generation of arsenic triglutathione from arsenite when GSH is present at concentrations 2 mM or higher. Methylation of arsenic is catalyzed by Cyt19 only when arsenic triglutathione is present in the reaction mixture
GSH
addition of GSH stimulates the overall rate for As methylation, but inhibits formation of trimethylarsenite
GSH
stimulatory effect on the rate of methylarsonate and dimethylarsinate production from arsenite is concentration-dependent, suppression of formation of trimethylarsine oxide
GSH
addition of GSH stimulates the overall rate for As methylation, but inhibits formation of trimethylarsenite
thioredoxin
dependent on, activates formation of methyl arsenic, dimethyl arsenic, and trimethyl arsenic
thioredoxin
activates formation of methyl arsenic, dimethyl arsenic, and trimethyl arsenic
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Atherosclerosis
Effects of Inorganic Arsenic, Methylated Arsenicals, and Arsenobetaine on Atherosclerosis in the Mouse Model and the Role of As3mt-Mediated Methylation.
Atherosclerosis
Ethnic, Geographic, and Genetic Differences in Arsenic Metabolism at Low Arsenic Exposure: A Preliminary Analysis in the Multi-Ethnic Study of Atherosclerosis (MESA).
Atherosclerosis
Significantly increased risk of carotid atherosclerosis with arsenic exposure and polymorphisms in arsenic metabolism genes.
Carcinogenesis
Human arsenic methyltransferase (AS3MT) pharmacogenetics: gene resequencing and functional genomics studies.
Carcinogenesis
Inorganic arsenic-mediated upregulation of AS3MT promotes proliferation of nonsmall cell lung cancer cells by regulating cell cycle genes.
Carcinogenesis
Role of the Met(287)Thr polymorphism in the AS3MT gene on the metabolic arsenic profile.
Carcinoma
Genetic variation in arsenic (+3 oxidation state) methyltransferase (AS3MT), arsenic metabolism and risk of basal cell carcinoma in a European population.
Carcinoma, Basal Cell
Genetic variation in arsenic (+3 oxidation state) methyltransferase (AS3MT), arsenic metabolism and risk of basal cell carcinoma in a European population.
Carcinoma, Hepatocellular
Manipulation of expression of arsenic (+3 oxidation state) methyltransferase in cultured cells.
Carcinoma, Hepatocellular
shRNA silencing of AS3MT expression minimizes arsenic methylation capacity of HepG2 cells.
Carcinoma, Non-Small-Cell Lung
Inorganic arsenic-mediated upregulation of AS3MT promotes proliferation of nonsmall cell lung cancer cells by regulating cell cycle genes.
Cardiovascular Diseases
Low-level arsenic exposure, AS3MT gene polymorphism and cardiovascular diseases in rural Texas counties.
Carotid Artery Diseases
Significantly increased risk of carotid atherosclerosis with arsenic exposure and polymorphisms in arsenic metabolism genes.
Coronary Artery Disease
Association of N6AMT1 rs2254638 Polymorphism With Clopidogrel Response in Chinese Patients With Coronary Artery Disease.
Coronary Disease
Genomewide Association Study Identifies Novel Genetic Loci That Modify Antiplatelet Effects and Pharmacokinetics of Clopidogrel.
Heart Diseases
Low-level arsenic exposure, AS3MT gene polymorphism and cardiovascular diseases in rural Texas counties.
Hydronephrosis
Effect of Sodium Arsenite Dose Administered in the Drinking Water on the Urinary Bladder Epithelium of Female Arsenic (+3 oxidation state) Methyltransferase Knockout Mice.
Hyperlipidemias
Low-level arsenic exposure, AS3MT gene polymorphism and cardiovascular diseases in rural Texas counties.
Hypertension
Low-level arsenic exposure, AS3MT gene polymorphism and cardiovascular diseases in rural Texas counties.
Insulin Resistance
Knockout of arsenic (+3 oxidation state) methyltransferase is associated with adverse metabolic phenotype in mice: the role of sex and arsenic exposure.
Leukemia
Biotransformation of arsenic trioxide by AS3MT favors eradication of acute promyelocytic leukemia: revealing the hidden facts.
Leukemia
Role of arsenic (+3 oxidation state) methyltransferase in arsenic mediated APL treatment: an in vitro investigation.
Leukemia, Promyelocytic, Acute
Biotransformation of arsenic trioxide by AS3MT favors eradication of acute promyelocytic leukemia: revealing the hidden facts.
Leukemia, Promyelocytic, Acute
Role of arsenic (+3 oxidation state) methyltransferase in arsenic mediated APL treatment: an in vitro investigation.
Lung Neoplasms
Associations between arsenic (+3 oxidation state) methyltransferase (AS3MT) and N-6 adenine-specific DNA methyltransferase 1 (N6AMT1) polymorphisms, arsenic metabolism, and cancer risk in a chilean population.
Lung Neoplasms
Inorganic arsenic-mediated upregulation of AS3MT promotes proliferation of nonsmall cell lung cancer cells by regulating cell cycle genes.
Neoplasms
Associations between arsenic (+3 oxidation state) methyltransferase (AS3MT) and N-6 adenine-specific DNA methyltransferase 1 (N6AMT1) polymorphisms, arsenic metabolism, and cancer risk in a chilean population.
Neoplasms
Effects of Arsenic (+3 Oxidation State) Methyltransferase Gene Polymorphisms and Expression on Bladder Cancer: Evidence from a Systematic Review, Meta-analysis and TCGA Dataset.
Neoplasms
Inorganic arsenic-mediated upregulation of AS3MT promotes proliferation of nonsmall cell lung cancer cells by regulating cell cycle genes.
Neoplasms
Polymorphisms in arsenic metabolism genes, urinary arsenic methylation profile and cancer.
Neuroblastoma
Identification and characterisation of arsenite (+3 Oxidation State) methyltransferase (AS3MT) in mouse neuroblastoma cell line N1E-115.
Obesity
Knockout of arsenic (+3 oxidation state) methyltransferase is associated with adverse metabolic phenotype in mice: the role of sex and arsenic exposure.
Urinary Bladder Neoplasms
Effects of Arsenic (+3 Oxidation State) Methyltransferase Gene Polymorphisms and Expression on Bladder Cancer: Evidence from a Systematic Review, Meta-analysis and TCGA Dataset.
Urinary Bladder Neoplasms
Genetic variation in Glutathione S-Transferase Omega-1, Arsenic Methyltransferase and Methylene-tetrahydrofolate Reductase, arsenic exposure and bladder cancer: a case-control study.
Urinary Bladder Neoplasms
Polymorphisms of Arsenic (+3 Oxidation State) Methyltransferase and Arsenic Methylation Capacity Affect the Risk of Bladder Cancer.
Vaccinia
Progress in genome-wide association studies of schizophrenia in Han Chinese populations.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0016
arsenite
-
mutant enzyme M287T, in the presence of 1 mM glutathione, in 100 mM Tris-HCl buffer (pH 7.4), at 37°C
0.0016
arsenite
-
wild type enzyme, in the presence of 1 mM glutathione, in 100 mM Tris-HCl buffer (pH 7.4), at 37°C
0.002
arsenite
-
mutant enzyme M287T, in 100 mM Tris-HCl buffer (pH 7.4), at 37°C
0.0007
methylarsonate
-
wild type enzyme, in the presence of 1 mM glutathione, in 100 mM Tris-HCl buffer (pH 7.4), at 25°C
0.0009
methylarsonate
-
mutant enzyme M287T, in the presence of 1 mM glutathione, in 100 mM Tris-HCl buffer (pH 7.4), at 25°C
0.0015
methylarsonate
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 7.4), at 25°C
0.003
methylarsonate
-
mutant enzyme M287T, in 100 mM Tris-HCl buffer (pH 7.4), at 25°C
0.0478
S-adenosyl-L-methionine
-
wild type enzyme, in PBS (25 mM, pH 7.0), at 37°C
0.049
S-adenosyl-L-methionine
-
mutant enzyme C375S, in PBS (25 mM, pH 7.0), at 37°C
0.0495
S-adenosyl-L-methionine
-
mutant enzyme C360S, in PBS (25 mM, pH 7.0), at 37°C
0.0503
S-adenosyl-L-methionine
-
mutant enzyme C334S, in PBS (25 mM, pH 7.0), at 37°C
0.0512
S-adenosyl-L-methionine
-
mutant enzyme C271S, in PBS (25 mM, pH 7.0), at 37°C
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Ki VALUE [mM]
INHIBITOR
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
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 11
pH 7.5: about 40% of maximal activity, pH 11: about 35% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16 - 37
-
purified enzyme converts almost all arsenite to dimethylarsinate at temperatures of 16–37°C in pH 7.5 buffer, while at higher temperatures the rate of arsenite transformation is reduced
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Cyanidioschyzon sp.
no activity in Callithrix jacchus
no activity in Saguinus oedipus
-
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
mRNA is detected after 35 or 45 cycles of amplification
brenda
-
in a stable clonal HepG2/A cell line, AS3MT mRNA and protein levels are reduced by 83 and 88%, respectively. The capacity to methylate inorganic arsenic decreases by 70%
brenda
additional information
-
the enzyme is universally expressed in zebrafish tissues
brenda
additional information
not detected in UROtsa cells, an immortalized cell line derived from normal human urothelium, after 45 cycles of amplification
brenda
additional information
-
not detected in UROtsa cells, an immortalized cell line derived from normal human urothelium, after 45 cycles of amplification
brenda
additional information
the As3MT protein level is lower in cancer tissues in comparison to normal tissues
brenda
additional information
the As3MT protein level is lower in cancer tissues in comparison to normal tissues
brenda
additional information
-
the As3MT protein level is lower in cancer tissues in comparison to normal tissues
brenda
additional information
the level of N6AMT1 protein in most cancer tissues is comparable to the levels in normal tissues
brenda
additional information
the level of N6AMT1 protein in most cancer tissues is comparable to the levels in normal tissues
brenda
additional information
-
the level of N6AMT1 protein in most cancer tissues is comparable to the levels in normal tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
a gene disruption mutant loses arsenite methylation ability and becomes more sensitive to arsenite
malfunction
-
a gene disruption mutant loses arsenite methylation ability and becomes more sensitive to arsenite
-
metabolism
splicing of AS3MT pre-mRNA is disconcerted by oxidative stress and abnormal alternative splicing of AS3MT mRNA may affect arsenic methylation ability. Exposure of HepG2 cells to H2O2 results in increased levels of a spliced form skipping exon-3 to exon-10 in an H2O2-concentration-dependent manner
physiological function
-
the enzyme plays an important role in the detoxification of arsenicals
physiological function
the enzyme plays a role in arsenite methylation and detoxification of As3+
physiological function
Bacillus subtilis 168 expressing ArsM converts most of the inorganic As in the medium into dimethylarsenate and trimethylarsine oxide within 48 h and volatizes substantial amounts of dimethylarsine and trimethylarsine. The rate of As methylation and volatilization increases with temperature from 37 to 50°C. When inoculated into an As-contaminated organic manure composted at 50°C, the modified strain significantly enhances As volatilization
physiological function
expression of ArsM confers resistance to an As(III)-hypersensitive strain of Escherichia coli
physiological function
N6AMT1 converts monomethylarsonous acid(III) into the less toxic dimethylarsonic acid (V). The effects of N6AMT1 in arsenic metabolism are relatively minor and limited when compared with the action of As3MT
physiological function
-
the enzyme plays a role in arsenite methylation and detoxification of As3+
-
Show AA Sequence and Transmembrane Helices (195 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31100
-
x * 31100, truncated exon-4 and -5 skipping (DELTA4,5) mutant form, calculated from amino acid sequence
35400
-
x * 35400, His-tagged enzyme, calculated from amino acid sequence
41700
41700
-
x * 41700, full-lenth wild type form, calculated from amino acid sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 32000, calculated from sequence and SDS-PAGE, recombinant protein
?
-
x * 31100, truncated exon-4 and -5 skipping (DELTA4,5) mutant form, calculated from amino acid sequence
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure. The two conserved cysteine residues Cys145 and Cys195 are in close propinquity and form an As(III) binding site. GSH forms the third ligand with As with the sulfur atom of GSH orienting toward the bound As(III) at approximately 2.4 A distance
hanging drop vapor diffusion method, using 20% (w/v) polyethylene glycol 3000, 0.1 M Tris-HCl, pH 7.0, containing 0.2 M calcium acetate
Cyanidioschyzon sp.
structure with the bound aromatic arsenicals phenylarsenite at 1.80 A resolution and reduced roxarsone at 2.25 A resolution. Compounds are bound to conserved residues C174 and C224. A loop containing Cys44 and Cys72 shifts by nearly 6.5 A in the arsenic(III)-bound structures compared with the SAM-bound structure
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C72A
Cyanidioschyzon sp.
-
the mutation leads to loss of As(III) methylation, but still shows trivalent methylarsenate methylation
C44A
mutant is unable to methylate arsenic(III) but retains the ability to methylate methylarsenate
C44A/C72A
mutant is unable to methylate arsenic(III) but retains the ability to methylate methylarsenate
C334S
-
the mutation decreases the enzymatic turnover and changes the conformation of the enzyme
C360S
-
the mutation decreases the enzymatic turnover and changes the conformation of the enzyme
G134A
the mutant’s activity is seriously impaired compared with that of wild type
G82A
the mutant’s activity is seriously impaired compared with that of wild type
L77A
the mutant’s activity is seriously impaired compared with that of wild type
M287T
R57A
the mutant's activity is seriously impaired compared with that of wild type
R83A
the mutant’s activity is seriously impaired compared with that of wild type
S81A
the mutant’s activity is seriously impaired compared with that of wild type
T104A
the mutant’s activity is seriously impaired compared with that of wild type
V157A
the mutant’s activity is seriously impaired compared with that of wild type
V161A
the mutant’s activity is seriously impaired compared with that of wild type
Y135A
the mutant’s activity is seriously impaired compared with that of wild type
Y58A
the mutant’s activity is seriously impaired compared with that of wild type
additional information
-
an exon-4 and -5 skipping (DELTA4,5) truncated mutant form does not convert arsenite to monomethylarsonate or dimethylarsinic acid
M287T
a naturally occurring T/C polymorphism in AS3MT among Japanese, Koreans, Chinese, Mongolians, Uygurs, Tibetans, Tamangs, Tamils, Sinhalese, Turks, Ovambos, Ghanaians, and Xhosas. Xhosas have the highest 287T frequency
M287T
genotype distribution and allele frequencies of M287T in Ovambo, Turkish, Mongolian, Korean, and Japanese populations , the mutation frequencies in Asian populations are relatively lower than those of African and Caucasian populations, the frequencies of mutation in the Mongolian, Korean, and Japanese populations, overview
M287T
-
in the absence of glutathione, the mutant shows decreased Vmax and Km for arsenite and increased Vmax and Km for methylarsonate compared to the wild type enzyme
M287T
-
the mutation is associated with an increased percentage of monomethylated arsenic in urine
M287T
the substitution results in an increase in the capacity of the first step of methylation, leading to an increase in the percentage of urinary methylarsonate, but not the second step of methylation
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
the wild type enzyme exhibits about 40% residual activity after 120 min at 45°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE anion exchange chromatography, Sephadex G-200, High Q anion exchange chromatographie, 40fold purification
-
DEAE cellulose, ammonium sulfate precipitation, Sephadex G-200, Sephadex G-100, 2000fold purification
-
DEAE-cellulose, Sephadex G-200, Sephadex G-100, anion exchange chromatographie
-
native enzyme several thousandfold using pH-dependent fractionation, chromatofocusing, and S-adenosylhomocysteine-affinity chromatography, the purification of AS3MT from liver cytosol is dependent on the presence of 1 mM dithiothreitol and 5 mM GSH
Ni-NTA agarose column chromatography
Ni-NTA column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
after expression in COS-1 cells and correction for transfection efficiency, the Trp173 allozyme displays 31%, Thr287 350%, Ile306 4.8%, and Thr287/Ile306 6.2% of the activity of the wild type allozyme, with 20, 190, 4.4, and 7.9% of the level of wild-type immunoreactive protein, respectively
-
creation of a clonal human UROtsa cell line (UROtsa/F35) that expresses rat AS3MT and, unlike the parent UROtsa cell line, methylates inorganic arsenite and methylarsenite
-
DNA and amino acid sequence determination and analysis, genotyping with method development and optimization, overview
expressed in Escherichia coli BL21 (DE3) pLysS cells
expressed in Escherichia coli BL21(DE3) cells
expressed in the arsenite-sensitive Escherichia coli strain AW3110(DE3)
expression of a mutant lacking 31 residues from the N-terminus and 28 residues from the C-terminus
expression of rat AS3MT in a simian virus 40 (SV40)-transformed human urothelial cell line confers the capacity to methylate inorganic arsenic on cells that otherwise do not express AS3MT and that have a null phenotype for iAs methylation
gene arsM, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotype-phenotype correlations for arsenic methylation and AS3MT
gene arsM, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotype-phenotype correlations for arsenic methylation and AS3MT, recombinant expression
genes arsM and arsMC2, functional expression in enzyme-deficient Escherichia coli strain AW3110
-
genotyping
wild-type ArsM and the C281/282S ArsMC2 variant, both with a His6 tag, are expressed in Escherichia coli
-
gene arsM, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotype-phenotype correlations for arsenic methylation and AS3MT
-
gene arsM, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotype-phenotype correlations for arsenic methylation and AS3MT
-
gene arsM, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotype-phenotype correlations for arsenic methylation and AS3MT
-
gene arsM, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotype-phenotype correlations for arsenic methylation and AS3MT
-
gene arsM, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotype-phenotype correlations for arsenic methylation and AS3MT
-
gene arsM, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotype-phenotype correlations for arsenic methylation and AS3MT
-
gene arsM, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotype-phenotype correlations for arsenic methylation and AS3MT
-
gene arsM, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotype-phenotype correlations for arsenic methylation and AS3MT
gene arsM, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotype-phenotype correlations for arsenic methylation and AS3MT
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is expressed in the absence of As(3+), and the expression is further enhanced after 6 h by 0.04 mM As(3+) exposure
the enzyme is expressed in the absence of As(3+), and the expression is further enhanced after 6 h by 0.04 mM As(3+) exposure
the enzyme is expressed in the absence of As(3+), and the expression is further enhanced after 6 h by 0.04 mM As(3+) exposure
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
Bacillus subtilis 168 expressing ArsM converts most of the inorganic As in the medium into dimethylarsenate and trimethylarsine oxide within 48 h and volatizes substantial amounts of dimethylarsine and trimethylarsine. The rate of As methylation and volatilization increases with temperature from 37 to 50°C. When inoculated into an As-contaminated organic manure composted at 50°C, the modified strain significantly enhances As volatilization
medicine
the proliferation of NB4 cells is significantly inhibited in a transwell system cocultured with AS3MT-transfected HepG2 cells after exposure to arsenite. The therapeutic efficacy of As2O3 (i.e., iAsIII) in acute promyelocytic leukemia patients is probably associated with the production of methylated arsenic metabolites by AS3MT
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wildfang, E.; Zakharyan, R.A.; Aposhian, H.V.
Enzymatic methylation of arsenic compounds. VI. Characterization of hamster liver arsenite and methylarsonic acid methyltransferase activities in vitro
Toxicol. Appl. Pharmacol.
152
366-375
1998
Cricetinae
brenda
Healey, S.M.; Casarez, E.A.; Ayalo-Fierro, F.; Aposhian, H.V.
Enzymatic methylation of arsenic compoundes. Arsenite methyltransferase activity in tissues of mice
Toxicol. Appl. Pharmacol.
148
65-70
1998
Mus musculus
brenda
Healy S.M.; Zakharyan, R.A.; Aposhian, H.V.
Enzymatic methylation of arsenic compounds. VI. In vitro and in vivo deficiency of the methylation of arsenite and monomethylarsonic acid in the guinea pig
Mutat. Res.
386
229-239
1997
no activity in Cavia porcellus
brenda
Zakharyan, R.A.; Wildfang, E.; Aposhian, H.V.
Enzymatic methylation of arsenic compoundes. The marmoset and tamarin, but not the rhesus monkeys are deficient in methyltransferases that methylate inorganic compounds
Toxicol. Appl. Pharmacol.
140
77-84
1996
Oryctolagus cuniculus, Macaca mulatta, no activity in Callithrix jacchus, no activity in Saguinus oedipus
brenda
Zakharyan, R.; Wu, Y.; Bogdan, G.M.; Aposhian, H.V.
Enzymatic methylation of arsenic compounds: assay, partial purification, and properties of arsenite methyltransferase and monomethylarsonic acid methyltransferase of rabbit liver
Chem. Res. Toxicol.
8
1029-1038
1995
Oryctolagus cuniculus
brenda
Hayakawa, T.; Kobayashi, Y.; Cui, X.; Hirano, S.
A new metabolic pathway of arsenite: arsenic-glutathione complexes are substrates for human arsenic methyltransferase Cyt19
Arch. Toxicol.
79
183-191
2005
Homo sapiens
brenda
Walton, F.S.; Waters, S.B.; Jolley, S.L.; LeCluyse, E.L.; Thomas, D.J.; Styblo, M.
Selenium compounds modulate the activity of recombinant rat AsIII-methyltransferase and the methylation of arsenite by rat and human hepatocytes
Chem. Res. Toxicol.
16
261-265
2003
Homo sapiens, Rattus norvegicus
brenda
Waters, S.B.; Devesa, V.; Fricke, M.W.; Creed, J.T.; Styblo, M.; Thomas, D.J.
Glutathione modulates recombinant rat arsenic (+3 oxidation state) methyltransferase-catalyzed formation of trimethylarsine oxide and trimethylarsine
Chem. Res. Toxicol.
17
1621-1629
2004
Rattus norvegicus (Q8VHT6)
brenda
Lin, S.; Shi, Q.; Nix, F.B.; Styblo, M.; Beck, M.A.; Herbin-Davis, K.M.; Hall, L.L.; Simeonsson, J.B.; Thomas, D.J.
A novel S-adenosyl-L-methionine:arsenic(III) methyltransferase from rat liver cytosol
J. Biol. Chem.
277
10795-10803
2002
Rattus norvegicus (Q8VHT6), Homo sapiens (Q9HBK9), Homo sapiens
brenda
Wildfang, E.; Radabaugh, T.R.; Vasken Aposhian, H.
Enzymatic methylation of arsenic compounds. IX. Liver arsenite methyltransferase and arsenate reductase activities in primates
Toxicology
168
213-221
2001
Macaca fascicularis, Macaca mulatta, no activity in Callithrix jacchus, no activity in Saguinus oedipus, no activity in Papio cynocephalus, Saimiri sp., no activity in Aotus sp., no activity in Daubentonia madagascariensis, no activity in Galago senegalensis, no activity in Nycticebus coucang, no activity in Lemur catta, no activity in Propithecus verreauxi, no activity in Cheirogaleus medius, no activity in Gorilla gorilla, no activity in Pongo pygmaeus, no activity in Pan troglodytes, Macaca nemestrina
brenda
Drobna, Z.; Xing, W.; Thomas, D.J.; Styblo, M.
shRNA silencing of AS3MT expression minimizes arsenic methylation capacity of HepG2 cells
Chem. Res. Toxicol.
19
894-898
2006
Homo sapiens
brenda
Thomas, D.J.; Li, J.; Waters, S.B.; Xing, W.; Adair, B.M.; Drobna, Z.; Devesa, V.; Styblo, M.
Arsenic (+3 oxidation state) methyltransferase and the methylation of arsenicals
Exp. Biol. Med.
232
3-13
2007
Bos taurus, Bos taurus (Q58DQ0), Gallus gallus, Ciona intestinalis, Mus musculus, no activity in Caenorhabditis elegans, no activity in Drosophila melanogaster, Oncorhynchus mykiss, Pan troglodytes, Rattus norvegicus, Rattus norvegicus (Q8VHT6), Rhodopseudomonas palustris, Strongylocentrotus purpuratus, Homo sapiens (Q9HBK9)
brenda
Wood, T.C.; Salavagionne, O.E.; Mukherjee, B.; Wang, L.; Klumpp, A.F.; Thomae, B.A.; Eckloff, B.W.; Schaid, D.J.; Wieben, E.D.; Weinshilboum, R.M.
Human arsenic methyltransferase (AS3MT) pharmacogenetics: gene resequencing and functional genomics studies
J. Biol. Chem.
281
7364-7373
2006
Homo sapiens
brenda
Qin, J.; Rosen, B.P.; Zhang, Y.; Wang, G.; Franke, S.; Rensing, C.
Arsenic detoxification and evolution of trimethylarsine gas by a microbial arsenite S-adenosylmethionine methyltransferase
Proc. Natl. Acad. Sci. USA
103
2075-2080
2006
Rhodopseudomonas palustris, Rhodopseudomonas palustris CGA009
brenda
Drobna, Z.; Waters, S.B.; Devesa, V.; Harmon, A.W.; Thomas, D.J.; Styblo, M.
Metabolism and toxicity of arsenic in human urothelial cells expressing rat arsenic (+3 oxidation state)-methyltransferase
Toxicol. Appl. Pharmacol.
207
147-159
2005
Rattus norvegicus
brenda
John, J.P.; Oh, J.E.; Pollak, A.; Lubec, G.
Identification and characterisation of arsenite (+3 oxidation state) methyltransferase (AS3MT) in mouse neuroblastoma cell line N1E-115
Amino Acids
35
355-358
2008
Mus musculus (Q91WU5), Mus musculus
brenda
De Chaudhuri, S.; Ghosh, P.; Sarma, N.; Majumdar, P.; Sau, T.J.; Basu, S.; Roychoudhury, S.; Ray, K.; Giri, A.K.
Genetic variants associated with arsenic susceptibility: study of purine nucleoside phosphorylase, arsenic (+3) methyltransferase, and glutathione s-transferase omega genes
Environ. Health Perspect.
116
501-505
2008
Homo sapiens (Q9HBK9)
brenda
Yuan, C.; Lu, X.; Qin, J.; Rosen, B.P.; Le, X.C.
Volatile arsenic species released from Escherichia coli expressing the AsIII S-adenosylmethionine methyltransferase gene
Environ. Sci. Technol.
42
3201-3206
2008
Rhodopseudomonas palustris
brenda
Fujihara, J.; Soejima, M.; Koda, Y.; Kunito, T.; Takeshita, H.
Asian specific low mutation frequencies of the M287T polymorphism in the human arsenic (+3 oxidation state) methyltransferase (AS3MT) gene
Mutat. Res.
654
158-161
2008
Homo sapiens (Q9HBK9), Homo sapiens
brenda
Fujihara, J.; Kunito, T.; Agusa, T.; Yasuda, T.; Iida, R.; Fujii, Y.; Takeshita, H.
Population differences in the human arsenic (+3 oxidation state) methyltransferase (AS3MT) gene polymorphism detected by using genotyping method
Toxicol. Appl. Pharmacol.
225
251-254
2007
Homo sapiens (Q9HBK9), Homo sapiens
brenda
Fujihara, J.; Yasuda, T.; Kato, H.; Yuasa, I.; Panduro, A.; Kunito, T.; Takeshita, H.
Genetic variants associated with arsenic metabolism within human arsenic (+3 oxidation state) methyltransferase show wide variation across multiple populations
Arch. Toxicol.
85
119-125
2011
Homo sapiens
brenda
Sumi, D.; Fukushima, K.; Miyataka, H.; Himeno, S.
Alternative splicing variants of human arsenic (+3 oxidation state) methyltransferase
Biochem. Biophys. Res. Commun.
415
48-53
2011
Homo sapiens
brenda
Marapakala, K.; Qin, J.; Rosen, B.P.
Identification of catalytic residues in the As(III) S-adenosylmethionine methyltransferase
Biochemistry
51
944-951
2012
Cyanidioschyzon sp.
brenda
Song, X.; Geng, Z.; Li, X.; Hu, X.; Bian, N.; Zhang, X.; Wang, Z.
New insights into the mechanism of arsenite methylation with the recombinant human arsenic (+3) methyltransferase (hAS3MT)
Biochimie
92
1397-1406
2010
Homo sapiens
brenda
Song, X.; Geng, Z.; Li, X.; Zhao, Q.; Hu, X.; Zhang, X.; Wang, Z.
Functional and structural evaluation of cysteine residues in the human arsenic (+3 oxidation state) methyltransferase (hAS3MT)
Biochimie
93
369-375
2011
Homo sapiens
brenda
Hamdi, M.; Yoshinaga, M.; Packianathan, C.; Qin, J.; Hallauer, J.; McDermott, J.R.; Yang, H.C.; Tsai, K.J.; Liu, Z.
Identification of an S-adenosylmethionine (SAM) dependent arsenic methyltransferase in Danio rerio
Toxicol. Appl. Pharmacol.
262
185-193
2012
Danio rerio
brenda
Ding, L.; Saunders, R.J.; Drobna, Z.; Walton, F.S.; Xun, P.; Thomas, D.J.; Styblo, M.
Methylation of arsenic by recombinant human wild-type arsenic (+3 oxidation state) methyltransferase and its methionine 287 threonine (M287T) polymorph: Role of glutathione
Toxicol. Appl. Pharmacol.
264
121-130
2012
Homo sapiens
brenda
Zhang, J.; Cao, T.; Tang, Z.; Shen, Q.; Rosen, B.P.; Zhao, F.J.
Arsenic methylation and volatilization by arsenite S-adenosylmethionine methyltransferase in Pseudomonas alcaligenes NBRC14159
Appl. Environ. Microbiol.
81
2852-2860
2015
Pseudomonas alcaligenes (U2ZU49), Pseudomonas alcaligenes, Pseudomonas alcaligenes NBRC 14159 (U2ZU49)
brenda
Ye, J.; Chang, Y.; Yan, Y.; Xiong, J.; Xue, X.M.; Yuan, D.; Sun, G.X.; Zhu, Y.G.; Miao, W.
Identification and characterization of the arsenite methyltransferase from a protozoan, Tetrahymena pyriformis
Aquat. Toxicol.
149
50-57
2014
Tetrahymena pyriformis
brenda
Ajees, A.A.; Marapakala, K.; Packianathan, C.; Sankaran, B.; Rosen, B.P.
Structure of an As(III) S-adenosylmethionine methyltransferase: insights into the mechanism of arsenic biotransformation
Biochemistry
51
5476-5485
2012
Cyanidioschyzon sp. (C0JV69)
brenda
Li, X.; Geng, Z.; Chang, J.; Song, X.; Wang, Z.
Mutational analysis of residues in human arsenic (III) methyltransferase (hAS3MT) belonging to 5 A around S-adenosylmethionine (SAM)
Biochimie
107 Pt B
396-405
2014
Homo sapiens (Q9HBK9), Homo sapiens
brenda
Sumi, D.; Himeno, S.
Role of arsenic (+3 oxidation state) methyltransferase in arsenic metabolism and toxicity
Biol. Pharm. Bull.
35
1870-1875
2012
Homo sapiens (Q9HBK9)
brenda
Wang, P.P.; Sun, G.X.; Zhu, Y.G.
Identification and characterization of arsenite methyltransferase from an archaeon, Methanosarcina acetivorans C2A
Environ. Sci. Technol.
48
12706-12713
2014
Methanosarcina acetivorans
brenda
Li, X.; Geng, Z.; Wang, S.; Song, X.; Hu, X.; Wang, Z.
Functional evaluation of Asp76, 84, 102 and 150 in human arsenic(III) methyltransferase (hAS3MT) interacting with S-adenosylmethionine
FEBS Lett.
587
2232-2240
2013
Homo sapiens (Q9HBK9), Homo sapiens
brenda
Wang, P.P.; Bao, P.; Sun, G.X.
Identification and catalytic residues of the arsenite methyltransferase from a sulfate-reducing bacterium, Clostridium sp. BXM
FEMS Microbiol. Lett.
362(4)
1-8
2015
Clostridium sp. (A0A0D3MJQ5), Clostridium sp. BXM (A0A0D3MJQ5)
brenda
Huang, L.; Yu, F.; Xu, C.; Tang, L.; He, J.
Crystallization and preliminary X-ray crystallographic analysis of the arsenic (III) S-adenosylmethionine methyltransferase from Rhodopseudanonas palustris
He Jishu Nuclear Techniques
35
326-330
2012
Rhodopseudomonas palustris
-
brenda
Wang, S.; Li, X.; Song, X.; Geng, Z.; Hu, X.; Wang, Z.
Rapid equilibrium kinetic analysis of arsenite methylation catalyzed by recombinant human arsenic (+3 oxidation state) methyltransferase (hAS3MT)
J. Biol. Chem.
287
38790-38799
2012
Homo sapiens (Q9HBK9), Homo sapiens
brenda
Wang, S.; Geng, Z.; Shi, N.; Li, X.; Wang, Z.
The functions of crucial cysteine residues in the arsenite methylation catalyzed by recombinant human arsenic (III) methyltransferase
PLoS ONE
9
e110924
2014
Homo sapiens (Q9HBK9), Homo sapiens
brenda
Tokumoto, M.; Kutsukake, N.; Yamanishi, E.; Katsuta, D.; Anan, Y.; Ogra, Y.
Arsenic (+3 oxidation state) methyltransferase is a specific but replaceable factor against arsenic toxicity
Toxicol. Rep.
1
589-595
2014
Homo sapiens (Q9HBK9)
brenda
Marapakala, K.; Packianathan, C.; Ajees, A.A.; Dheeman, D.S.; Sankaran, B.; Kandavelu, P.; Rosen, B.P.
A disulfide-bond cascade mechanism for arsenic(III) S-adenosylmethionine methyltransferase
Acta Crystallogr. Sect. D
71
505-515
2015
Cyanidioschyzon sp. 5508 (C0JV69)
brenda
Huang, K.; Chen, C.; Shen, Q.; Rosen, B.P.; Zhao, F.J.
Genetically engineering Bacillus subtilis with a heat-resistant arsenite methyltransferase for bioremediation of arsenic-contaminated organic waste
Appl. Environ. Microbiol.
81
6718-6724
2015
Cyanidioschyzon sp. 5508 (C0JV69)
brenda
Sumi, D.; Takeda, C.; Yasuoka, D.; Himeno, S.
Hydrogen peroxide triggers a novel alternative splicing of arsenic (+3 oxidation state) methyltransferase gene
Biochem. Biophys. Res. Commun.
480
18-22
2016
Homo sapiens (Q9HBK9), Homo sapiens
brenda
Guo, Y.; Xue, X.; Yan, Y.; Zhu, Y.; Yang, G.; Ye, J.
Arsenic methylation by an arsenite S-adenosylmethionine methyltransferase from Spirulina platensis
J. Environ. Sci. (China)
49
162-168
2016
Arthrospira platensis
brenda
Maimaitiyiming, Y.; Wang, C.; Xu, S.; Islam, K.; Chen, Y.J.; Yang, C.; Wang, Q.Q.; Naranmandura, H.
Role of arsenic (+3 oxidation state) methyltransferase in arsenic mediated APL treatment an in vitro investigation
Metallomics
10
828-837
2018
Homo sapiens (Q9HBK9), Homo sapiens
brenda
Huang, K.; Xu, Y.; Packianathan, C.; Gao, F.; Chen, C.; Zhang, J.; Shen, Q.; Rosen, B.P.; Zhao, F.J.
Arsenic methylation by a novel ArsM As(III) S-adenosylmethionine methyltransferase that requires only two conserved cysteine residues
Mol. Microbiol.
107
265-276
2018
Bacillus sp. CX-1 (A0A2P1M875)
brenda
Zhang, H.; Ge, Y.; He, P.; Chen, X.; Carina, A.; Qiu, Y.; Aga, D.S.; Ren, X.
Interactive effects of N6AMT1 and As3MT in arsenic biomethylation
Toxicol. Sci.
146
354-362
2015
Homo sapiens (Q9HBK9), Homo sapiens (Q9Y5N5), Homo sapiens
brenda
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