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Enzyme Nomenclature
Information on EC 2.1.1.137 - arsenite methyltransferase
for references in articles please use BRENDA:EC2.1.1.137
Word Map on EC 2.1.1.137
- 2.1.1.137
-
dimethylarsinic
-
monomethylarsonic
-
arsms
-
trivalent
-
arsenic-induced
-
biomethylation
-
metalloid
-
arsenic-related
-
met287thr
- dimethylarsenate
-
dmasiii
- trimethylarsine
-
organoarsenical
-
methylarsenicals
-
arsenic-contaminated
-
methylarsonic
-
hplc-icpms
-
as-contaminated
- cyanidioschyzon
-
arsenic-exposed
-
urotsa
-
arseniciii
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Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
2.1.1.137
-
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RECOMMENDED NAME
GeneOntology No.
arsenite methyltransferase
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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
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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Cyanidioschyzon sp.
no activity in Callithrix jacchus
no activity in Saguinus oedipus
-
SwissProt
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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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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
-
-
-
?
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
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
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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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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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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%
additional information
-
the enzyme is universally expressed in zebrafish tissues
additional information
-
not detected in UROtsa cells, an immortalized cell line derived from normal human urothelium, after 45 cycles of amplification
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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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SUBUNITS
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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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
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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ENGINEERING
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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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.137)
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