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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
-
biomethylation
-
metalloid
-
met287thr
- dimethylarsenate
-
dmasiii
-
arsenic-related
- trimethylarsine
- cyanidioschyzon
-
hplc-icpms
-
methylarsenicals
-
arsenic-contaminated
-
as-contaminated
-
arsenic-exposed
-
organoarsenical
- n6amt1
-
methylarsonic
-
gstos
-
chromatography-inductively
-
urotsa
-
arseniciii
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
as3mt, has3mt, arsenic (+3 oxidation state) methyltransferase, cyt19, as(iii) s-adenosylmethionine methyltransferase, arsenic (iii) methyltransferase, arsenite s-adenosylmethionine methyltransferase, arsenic (+3) methyltransferase, s-adenosyl-l-methionine:arsenic(iii) methyltransferase, arsenic (+3 oxidation state)-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
ArsM7B
As(III) S-adenosylmethionine methyltransferase
As(III) SAM 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 modelling, overview
Q58DQ0
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 mechanism, 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 + methylarsenite + dimethylarsenite + 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 + methylarsonate
S-adenosyl-L-homocysteine + dimethylarsinous acid + dimethylarsinic acid
-
-
-
-
?
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 + methylarsenite + dimethylarsenite + trimethylarsine
-
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
Q58DQ0
-
-
-
?
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
-
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
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
-
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
?
-
-
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
?
-
-
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
A0A0D3MJQ5
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
A0A0D3MJQ5
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
Cyanidioschyzon sp.
C0JV69
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
C0JV69
-
-
-
?
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
Q91WU5
-
-
-
?
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
U2ZU49
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
U2ZU49
-
-
-
?
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
A0A0D3MJQ5
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
A0A0D3MJQ5
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
Cyanidioschyzon sp.
C0JV69
-
-
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
C0JV69
-
-
-
?
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
U2ZU49
-
the enzyme also produces also produces dimethylarsine and trimethylarsine gases as by-products
-
?
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
U2ZU49
-
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
?
-
-
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
-
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
-
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
glutathione
-
1 mM GSH decreases Km and increases Vmax estimates for arsenite and methylarsonous acid
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
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.
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 Disease
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
Role of arsenic (+3 oxidation state) methyltransferase in arsenic mediated APL treatment: an in vitro investigation.
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.
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
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
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; 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
0.0032
arsenite
-
mutant enzyme V161A, at pH 7.0 and 37°C; wild type enzyme, at pH 7.0 and 37°C
0.007
arsenite
-
mutant enzyme T104A, at pH 7.0 and 37°C; mutant enzyme Y135A, at pH 7.0 and 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
-
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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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
-
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
-
the enzyme plays a role in arsenite methylation and detoxification of As3+
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
ARSM_HALSA
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
391
0
41696
Swiss-Prot
ARSM_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
249
0
26671
Swiss-Prot
ARSM_PSEA4
Pseudomonas alcaligenes (strain ATCC 14909 / DSM 50342 / JCM 20561 / NBRC 14159 / NCIMB 9945 / NCTC 10367 / 1577)
346
0
38023
Swiss-Prot
ARSM_RHOPA
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
283
0
29656
Swiss-Prot
A0A0A7LE69_9EURY
363
0
40781
TrEMBL
G0QP22_ICHMG
Ichthyophthirius multifiliis (strain G5)
212
0
24516
TrEMBL
K9Z2X3_CYAAP
Cyanobacterium aponinum (strain PCC 10605)
382
0
43335
TrEMBL
A0A1N0SNT7_9MYCO
253
0
26402
TrEMBL
A0A0A8P203_XENNE
360
0
39759
TrEMBL
M5CDB5_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
247
0
26432
TrEMBL
A0A0T5ZPL2_9BACT
836
0
93507
TrEMBL
G4SX17_META2
Methylomicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z)
348
0
38764
TrEMBL
K4LD22_THEPS
Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 12270 / PB)
269
0
29113
TrEMBL
G3J0Z1_METTV
Methylobacter tundripaludum (strain ATCC BAA-1195 / SV96)
348
0
38146
TrEMBL
M5C6L8_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
141
0
15209
TrEMBL
A0A0H3J6L3_CLOPA
277
0
30190
TrEMBL
D9S1V3_THEOJ
Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 / JW/IW-1228P)
272
0
29793
TrEMBL
I7F9S7_MYCS2
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
268
0
28153
TrEMBL
A0A0T6AFI6_9BACT
278
0
29568
TrEMBL
Q4WRJ3_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
253
0
27337
TrEMBL
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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
?
-
x * 31100, truncated exon-4 and -5 skipping (DELTA4,5) mutant form, calculated from amino acid sequence; x * 41700, full-lenth wild type form, calculated from amino acid sequence
?
-
x * 30000, His-tagged enzyme, SDS-PAGE; x * 35400, His-tagged enzyme, calculated from amino acid sequence
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
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.
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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
C72A
-
the mutation leads to loss of As(III) methylation, but still shows trivalent methylarsenate methylation
-
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
-
the mutation is associated with an increased percentage of monomethylated arsenic in urine
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 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 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) cells
expressed in the arsenite-sensitive Escherichia coli strain AW3110(DE3)
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
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
-
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
Q58DQ0
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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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
Macaca mulatta, no activity in Callithrix jacchus, no activity in Saguinus oedipus, Oryctolagus cuniculus
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
Homo sapiens, Homo sapiens (Q9HBK9), Rattus norvegicus (Q8VHT6)
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, Macaca nemestrina, no activity in Aotus sp., no activity in Callithrix jacchus, no activity in Cheirogaleus medius, no activity in Daubentonia madagascariensis, no activity in Galago senegalensis, no activity in Gorilla gorilla, no activity in Lemur catta, no activity in Nycticebus coucang, no activity in Pan troglodytes, no activity in Papio cynocephalus, no activity in Pongo pygmaeus, no activity in Propithecus verreauxi, no activity in Saguinus oedipus, Saimiri sp.
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), Ciona intestinalis, Gallus gallus, Homo sapiens (Q9HBK9), Mus musculus, no activity in Caenorhabditis elegans, no activity in Drosophila melanogaster, Oncorhynchus mykiss, Pan troglodytes, Rattus norvegicus (Q8VHT6), Rattus norvegicus, Rhodopseudomonas palustris, Strongylocentrotus purpuratus
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, Mus musculus (Q91WU5)
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, Homo sapiens (Q9HBK9)
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, Homo sapiens (Q9HBK9)
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., Cyanidioschyzon sp. 5508
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, Pseudomonas alcaligenes (U2ZU49), 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), Cyanidioschyzon sp. 5508 (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, Homo sapiens (Q9HBK9)
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, Homo sapiens (Q9HBK9)
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, Homo sapiens (Q9HBK9)
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, Homo sapiens (Q9HBK9)
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
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