Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsenite + dimethylarsenite + trimethylarsine
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
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 + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
additional information
?
-
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

?
-
-
enzyme evolutionary analysis
-
-
-
additional information
?
-
enzyme evolutionary analysis
-
-
-
additional information
?
-
-
enzyme evolutionary analysis
-
-
-
additional information
?
-
-
enzyme evolutionary analysis
-
-
-
additional information
?
-
-
monomethylarsonous acid is not methylated
-
-
-
additional information
?
-
-
As3MT methylates inorganic arsenic and its metabolites
-
-
-
additional information
?
-
enzyme evolutionary analysis
-
-
-
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
?
-
-
enzyme evolutionary analysis
-
-
-
additional information
?
-
-
enzyme evolutionary analysis
-
-
-
additional information
?
-
-
enzyme evolutionary analysis
-
-
-
additional information
?
-
enzyme evolutionary analysis
-
-
-
additional information
?
-
-
enzyme evolutionary analysis
-
-
-
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.
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
S-adenosyl-L-methionine + methylarsonite
S-adenosyl-L-homocysteine + dimethylarsinate
additional information
?
-
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

?
-
-
enzyme evolutionary analysis
-
-
-
additional information
?
-
Q58DQ0
enzyme evolutionary analysis
-
-
-
additional information
?
-
-
enzyme evolutionary analysis
-
-
-
additional information
?
-
-
enzyme evolutionary analysis
-
-
-
additional information
?
-
-
As3MT methylates inorganic arsenic and its metabolites
-
-
-
additional information
?
-
Q9HBK9
enzyme evolutionary analysis
-
-
-
additional information
?
-
-
genetic susceptibility to arsenic toxicity in Asian is different from Africans and Caucasians, overview
-
-
-
additional information
?
-
-
enzyme evolutionary analysis
-
-
-
additional information
?
-
-
enzyme evolutionary analysis
-
-
-
additional information
?
-
-
enzyme evolutionary analysis
-
-
-
additional information
?
-
Q8VHT6
enzyme evolutionary analysis
-
-
-
additional information
?
-
-
enzyme evolutionary analysis
-
-
-
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0007 - 0.003
methylarsonate
0.0031 - 0.0512
S-adenosyl-L-methionine
0.0012
arsenite

-
mutant enzyme G134A, at pH 7.0 and 37°C
0.0016
arsenite
-
mutant enzyme C334S, in PBS (25 mM, pH 7.0), at 37°C
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
0.0018
arsenite
-
mutant enzyme R83A, at pH 7.0 and 37°C
0.00188
arsenite
-
mutant enzyme C271S, in PBS (25 mM, pH 7.0), at 37°C
0.002
arsenite
-
mutant enzyme M287T, in 100 mM Tris-HCl buffer (pH 7.4), at 37°C
0.0022
arsenite
-
mutant enzyme V157A, at pH 7.0 and 37°C
0.00232
arsenite
-
mutant enzyme C360S, in PBS (25 mM, pH 7.0), at 37°C
0.0026
arsenite
-
mutant enzyme R57A, at pH 7.0 and 37°C
0.0027
arsenite
-
mutant enzyme S81A, at pH 7.0 and 37°C
0.0032
arsenite
-
wild type enzyme, in PBS (25 mM, pH 7.0), 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
0.0032
arsenite
-
wild type enzyme, at pH 7.0 and 37°C
0.0041
arsenite
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 7.4), at 37°C
0.0044
arsenite
-
mutant enzyme D150N, at pH 7.0 and 37°C
0.0045
arsenite
-
37°C, pH 8.0, Thr287 allozyme
0.007
arsenite
-
mutant enzyme T104A, at pH 7.0 and 37°C; mutant enzyme Y135A, at pH 7.0 and 37°C
0.0076
arsenite
-
mutant enzyme Y58A, at pH 7.0 and 37°C
0.0087
arsenite
-
mutant enzyme G82A, at pH 7.0 and 37°C
0.0089
arsenite
-
37°C, pH 8.0, Trp173 allozyme
0.0096
arsenite
-
mutant enzyme L77A, at pH 7.0 and 37°C
0.0118
arsenite
-
37°C, pH 8.0, wild-type enzyme
0.0185
arsenite
-
mutant enzyme C375S, in PBS (25 mM, pH 7.0), 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
0.0031
S-adenosyl-L-methionine

-
37°C, pH 8.0, Trp173 allozyme
0.0046
S-adenosyl-L-methionine
-
37°C, pH 8.0, wild-type enzyme
0.011
S-adenosyl-L-methionine
-
37°C, pH 8.0, Thr287 allozyme
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
DNA and amino acid sequence determination and analysis, genotyping with method development and optimization, overview
-
expressed in an arsenic-sensitive strain of Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) pLysS cells
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expressed in Escherichia coli DH10B cells
-
expressed in Escherichia coli DH5alpha and AW3110 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
-
-

-
expressed in Escherichia coli BL21(DE3) cells

expressed in Escherichia coli BL21(DE3) cells
Cyanidioschyzon sp.
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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