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Information on EC 2.1.1.137 - arsenite methyltransferase and Organism(s) Homo sapiens
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2.1.1.137 arsenite methyltransferaseIUBMB Comments
An enzyme responsible for synthesis of trivalent methylarsenical antibiotics in microbes or detoxification of inorganic arsenous acid in animals. The in vivo substrate is arsenic triglutathione or similar thiol (depending on the organism) , from which the arsenic is transferred to the enzyme forming bonds with the thiol groups of three cysteine residues via a disulfide bond cascade pathway [7, 8]. Most of the substrates undergo two methylations and are converted to dimethylarsinous acid . However, a small fraction are released earlier as methylarsonous acid, and a smaller amount proceeds via a third methylation, resulting in the volatile product trimethylarsane. Methylation involves temporary oxidation to arsenic(V) valency, followed by reduction back to arsenic(III) valency using electrons provided by thioredoxin or a similar reduction system. The arsenic(III) products are quickly oxidized in the presence of oxygen to the corresponding arsenic(V) species.
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Word Map
- 2.1.1.137
-
dimethylarsinic
-
monomethylarsonic
-
trivalent
-
arsenic-induced
-
arsenic-related
-
metalloid
- trimethylarsine
-
biomethylation
-
dmasiii
- dimethylarsenate
-
gstos
-
organoarsenical
-
hplc-icpms
-
arsenic-contaminated
-
methylarsenicals
- cyanidioschyzon
-
as-contaminated
-
arsenic-exposed
-
methylarsonic
- medicine
- degradation
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
as3mt, arsenic (+3 oxidation state) methyltransferase, n6amt1, has3mt, arsenite methyltransferase, cyt19, as(iii) s-adenosylmethionine methyltransferase, arsenic (iii) methyltransferase, arsenite s-adenosylmethionine methyltransferase, arsenic (+3) methyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
arsenic (+3 oxidation state) methyltransferase
arsenic (+3) methyltransferase
ArsM
-
-
-
-
AS3MT
methylarsonite methyltransferase
-
-
-
-
S-adenosyl-L-methionine:arsenic(III) methyltransferase
S-adenosyl-L-methionine:methylarsonite As-methyltransferase
-
-
-
-
arsenic (+3 oxidation state) methyltransferase
-
-
arsenic (+3 oxidation state) methyltransferase
-
AS3MT
-
-
-
-
AS3MT
-
S-adenosyl-L-methionine:arsenic(III) methyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
reaction modelling, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
transfer of methyl group
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:arsenous acid As-methyltransferase
An enzyme responsible for synthesis of trivalent methylarsenical antibiotics in microbes [11] or detoxification of inorganic arsenous acid in animals. The in vivo substrate is arsenic triglutathione or similar thiol (depending on the organism) [6], from which the arsenic is transferred to the enzyme forming bonds with the thiol groups of three cysteine residues [10] via a disulfide bond cascade pathway [7, 8]. Most of the substrates undergo two methylations and are converted to dimethylarsinous acid [9]. However, a small fraction are released earlier as methylarsonous acid, and a smaller amount proceeds via a third methylation, resulting in the volatile product trimethylarsane. Methylation involves temporary oxidation to arsenic(V) valency, followed by reduction back to arsenic(III) valency using electrons provided by thioredoxin or a similar reduction system. The arsenic(III) products are quickly oxidized in the presence of oxygen to the corresponding arsenic(V) species.
CAS REGISTRY NUMBER
COMMENTARY
167140-41-2
-
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 + methylarsonate + dimethylarsinous acid + dimethylarsinic acid
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + monomethylarsonate + dimethylarsinic acid
S-adenosyl-L-methionine + methylarsonate
S-adenosyl-L-homocysteine + dimethylarsinous acid
-
-
-
?
S-adenosyl-L-methionine + methylarsonate
S-adenosyl-L-homocysteine + dimethylarsinous acid + dimethylarsinic acid
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
AS3MT may contribute to variation in arsenic metabolism and, perhaps, arsenic-dependent carcinogenesis in humans
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
hAS3MT is the key enzyme in the pathway for methylation of iAs in human hepatic cells
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
As3MT enzyme is indispensable for conversion of the arsenic metabolites to their corresponding methylated products, metabolism of arsenic proceeds through sequential reduction and oxidative methylation involving several enzymes including the arsenic (+3) methyltransferase, overview
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + monomethylarsonate + dimethylarsinic acid
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + monomethylarsonate + dimethylarsinic acid
-
maximal conversion of arsenite to monomethylarsonate occurs at about 0.1 mM arsenite. Higher substrate concentrations inhibit monomethylarsonate yields. The production of dimethylarsinic acid increases as arsenite concentration increases from 0.0005 to 0.0083 mM, and then quickly decreases to zero
-
-
?
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
?
-
-
genetic susceptibility to arsenic toxicity in Asian is different from Africans and Caucasians, overview
-
-
?
additional information
?
-
the enzyme does not methylate selenium and tellurium
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
?
S-adenosyl-L-methionine + arsenite
S-adenosyl-L-homocysteine + methylarsonate
-
-
-
-
?
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 + 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
?
-
-
genetic susceptibility to arsenic toxicity in Asian is different from Africans and Caucasians, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
trimethyl-selenonium iodide
-
weak activator of recombinant As(III)-methyltransferase, weak inhibitor of arsenite methylation in hepatocytes
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dimethylselenoxide
-
weak activator of recombinant As(III)-methyltransferase, weak inhibitor of arsenite methylation in hepatocytes
thioredoxin
dependent on, activates formation of methyl arsenic, dimethyl arsenic, and trimethyl arsenic
trimethyl-selenonium iodide
-
weak activator of recombinant As(III)-methyltransferase, weak inhibitor of arsenite methylation in hepatocytes
glutathione
-
1 mM GSH decreases Km and increases Vmax estimates for arsenite and methylarsonous acid
glutathione
-
GSH should combine with the enzyme after the methylation to reduce the disulfide bond formed during the catalytic cycle to resume the active form of the enzyme
GSH
-
nonenzymatic generation of arsenic triglutathione from arsenite when GSH is present at concentrations 2 mM or higher. Methylation of arsenic is catalyzed by Cyt19 only when arsenic triglutathione is present in the reaction mixture
GSH
addition of GSH stimulates the overall rate for As methylation, but inhibits formation of trimethylarsenite
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0016
arsenite
-
mutant enzyme M287T, in the presence of 1 mM glutathione, in 100 mM Tris-HCl buffer (pH 7.4), at 37°C
0.0016
arsenite
-
wild type enzyme, in the presence of 1 mM glutathione, in 100 mM Tris-HCl buffer (pH 7.4), at 37°C
0.002
arsenite
-
mutant enzyme M287T, in 100 mM Tris-HCl buffer (pH 7.4), at 37°C
0.0007
methylarsonate
-
wild type enzyme, in the presence of 1 mM glutathione, in 100 mM Tris-HCl buffer (pH 7.4), at 25°C
0.0009
methylarsonate
-
mutant enzyme M287T, in the presence of 1 mM glutathione, in 100 mM Tris-HCl buffer (pH 7.4), at 25°C
0.0015
methylarsonate
-
wild type enzyme, in 100 mM Tris-HCl buffer (pH 7.4), at 25°C
0.003
methylarsonate
-
mutant enzyme M287T, in 100 mM Tris-HCl buffer (pH 7.4), at 25°C
0.0478
S-adenosyl-L-methionine
-
wild type enzyme, in PBS (25 mM, pH 7.0), at 37°C
0.049
S-adenosyl-L-methionine
-
mutant enzyme C375S, in PBS (25 mM, pH 7.0), at 37°C
0.0495
S-adenosyl-L-methionine
-
mutant enzyme C360S, in PBS (25 mM, pH 7.0), at 37°C
0.0503
S-adenosyl-L-methionine
-
mutant enzyme C334S, in PBS (25 mM, pH 7.0), at 37°C
0.0512
S-adenosyl-L-methionine
-
mutant enzyme C271S, in PBS (25 mM, pH 7.0), at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
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
not detected in UROtsa cells, an immortalized cell line derived from normal human urothelium, after 45 cycles of amplification
additional information
-
not detected in UROtsa cells, an immortalized cell line derived from normal human urothelium, after 45 cycles of amplification
additional information
the As3MT protein level is lower in cancer tissues in comparison to normal tissues
additional information
the As3MT protein level is lower in cancer tissues in comparison to normal tissues
additional information
-
the As3MT protein level is lower in cancer tissues in comparison to normal tissues
additional information
the level of N6AMT1 protein in most cancer tissues is comparable to the levels in normal tissues
additional information
the level of N6AMT1 protein in most cancer tissues is comparable to the levels in normal tissues
additional information
-
the level of N6AMT1 protein in most cancer tissues is comparable to the levels in normal tissues
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
splicing of AS3MT pre-mRNA is disconcerted by oxidative stress and abnormal alternative splicing of AS3MT mRNA may affect arsenic methylation ability. Exposure of HepG2 cells to H2O2 results in increased levels of a spliced form skipping exon-3 to exon-10 in an H2O2-concentration-dependent manner
physiological function
-
the enzyme plays an important role in the detoxification of arsenicals
physiological function
N6AMT1 converts monomethylarsonous acid(III) into the less toxic dimethylarsonic acid (V). The effects of N6AMT1 in arsenic metabolism are relatively minor and limited when compared with the action of As3MT
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AS3MT_HUMAN
375
0
41748
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31100
-
x * 31100, truncated exon-4 and -5 skipping (DELTA4,5) mutant form, calculated from amino acid sequence
41700
41700
-
x * 41700, full-lenth wild type form, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 31100, truncated exon-4 and -5 skipping (DELTA4,5) mutant form, calculated from amino acid sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 mutants activity is seriously impaired compared with that of wild type
G82A
the mutants activity is seriously impaired compared with that of wild type
L77A
the mutants 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 mutants activity is seriously impaired compared with that of wild type
S81A
the mutants activity is seriously impaired compared with that of wild type
T104A
the mutants activity is seriously impaired compared with that of wild type
V157A
the mutants activity is seriously impaired compared with that of wild type
V161A
the mutants activity is seriously impaired compared with that of wild type
Y135A
the mutants activity is seriously impaired compared with that of wild type
Y58A
the mutants activity is seriously impaired compared with that of wild type
additional information
-
an exon-4 and -5 skipping (DELTA4,5) truncated mutant form does not convert arsenite to monomethylarsonate or dimethylarsinic acid
M287T
a naturally occurring T/C polymorphism in AS3MT among Japanese, Koreans, Chinese, Mongolians, Uygurs, Tibetans, Tamangs, Tamils, Sinhalese, Turks, Ovambos, Ghanaians, and Xhosas. Xhosas have the highest 287T frequency
M287T
genotype distribution and allele frequencies of M287T in Ovambo, Turkish, Mongolian, Korean, and Japanese populations , the mutation frequencies in Asian populations are relatively lower than those of African and Caucasian populations, the frequencies of mutation in the Mongolian, Korean, and Japanese populations, overview
M287T
-
in the absence of glutathione, the mutant shows decreased Vmax and Km for arsenite and increased Vmax and Km for methylarsonate compared to the wild type enzyme
M287T
-
the mutation is associated with an increased percentage of monomethylated arsenic in urine
M287T
the substitution results in an increase in the capacity of the first step of methylation, leading to an increase in the percentage of urinary methylarsonate, but not the second step of methylation
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
the wild type enzyme exhibits about 40% residual activity after 120 min at 45°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
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
-
DNA and amino acid sequence determination and analysis, genotyping with method development and optimization, overview
expressed in Escherichia coli BL21 (DE3) pLysS cells
gene arsM, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, genotype-phenotype correlations for arsenic methylation and AS3MT, recombinant expression
genotyping
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
the proliferation of NB4 cells is significantly inhibited in a transwell system cocultured with AS3MT-transfected HepG2 cells after exposure to arsenite. The therapeutic efficacy of As2O3 (i.e., iAsIII) in acute promyelocytic leukemia patients is probably associated with the production of methylated arsenic metabolites by AS3MT
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Lin, S.; Shi, Q.; Nix, F.B.; Styblo, M.; Beck, M.A.; Herbin-Davis, K.M.; Hall, L.L.; Simeonsson, J.B.; Thomas, D.J.
A novel S-adenosyl-L-methionine:arsenic(III) methyltransferase from rat liver cytosol
J. Biol. Chem.
277
10795-10803
2002
Rattus norvegicus (Q8VHT6), Homo sapiens (Q9HBK9), Homo sapiens
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
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, Rattus norvegicus (Q8VHT6), Rhodopseudomonas palustris, Strongylocentrotus purpuratus
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
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)
Fujihara, J.; Soejima, M.; Koda, Y.; Kunito, T.; Takeshita, H.
Asian specific low mutation frequencies of the M287T polymorphism in the human arsenic (+3 oxidation state) methyltransferase (AS3MT) gene
Mutat. Res.
654
158-161
2008
Homo sapiens (Q9HBK9), Homo sapiens
Fujihara, J.; Kunito, T.; Agusa, T.; Yasuda, T.; Iida, R.; Fujii, Y.; Takeshita, H.
Population differences in the human arsenic (+3 oxidation state) methyltransferase (AS3MT) gene polymorphism detected by using genotyping method
Toxicol. Appl. Pharmacol.
225
251-254
2007
Homo sapiens (Q9HBK9), Homo sapiens
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
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
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
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
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
Li, X.; Geng, Z.; Chang, J.; Song, X.; Wang, Z.
Mutational analysis of residues in human arsenic (III) methyltransferase (hAS3MT) belonging to 5 A around S-adenosylmethionine (SAM)
Biochimie
107 Pt B
396-405
2014
Homo sapiens (Q9HBK9), Homo sapiens
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)
Li, X.; Geng, Z.; Wang, S.; Song, X.; Hu, X.; Wang, Z.
Functional evaluation of Asp76, 84, 102 and 150 in human arsenic(III) methyltransferase (hAS3MT) interacting with S-adenosylmethionine
FEBS Lett.
587
2232-2240
2013
Homo sapiens (Q9HBK9), Homo sapiens
Wang, S.; Li, X.; Song, X.; Geng, Z.; Hu, X.; Wang, Z.
Rapid equilibrium kinetic analysis of arsenite methylation catalyzed by recombinant human arsenic (+3 oxidation state) methyltransferase (hAS3MT)
J. Biol. Chem.
287
38790-38799
2012
Homo sapiens (Q9HBK9), Homo sapiens
Wang, S.; Geng, Z.; Shi, N.; Li, X.; Wang, Z.
The functions of crucial cysteine residues in the arsenite methylation catalyzed by recombinant human arsenic (III) methyltransferase
PLoS ONE
9
e110924
2014
Homo sapiens (Q9HBK9), Homo sapiens
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)
Sumi, D.; Takeda, C.; Yasuoka, D.; Himeno, S.
Hydrogen peroxide triggers a novel alternative splicing of arsenic (+3 oxidation state) methyltransferase gene
Biochem. Biophys. Res. Commun.
480
18-22
2016
Homo sapiens (Q9HBK9), Homo sapiens
Maimaitiyiming, Y.; Wang, C.; Xu, S.; Islam, K.; Chen, Y.J.; Yang, C.; Wang, Q.Q.; Naranmandura, H.
Role of arsenic (+3 oxidation state) methyltransferase in arsenic mediated APL treatment an in vitro investigation
Metallomics
10
828-837
2018
Homo sapiens (Q9HBK9), Homo sapiens
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