AS3MT

Arsenite methyltransferase

Identifiers

AS3MT ; CYT19

External IDs

OMIM: 611806 MGI: 1929882 HomoloGene: 10754 GeneCards: AS3MT Gene

2.1.1.137

Gene ontology
Molecular function	• S-adenosylmethionine-dependent methyltransferase activity • arsenite methyltransferase activity • methylarsonite methyltransferase activity
Cellular component	• mitochondrion • cytosol
Biological process	• toxin metabolic process • arsonoacetate metabolic process • methylation
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 10:
102.87 – 102.9 Mb

Chr 19:
46.71 – 46.74 Mb

PubMed search

Arsenite methyltransferase is an enzyme that in humans is encoded by the AS3MT gene.^[1]^[2]

References

↑ Lin S, Shi Q, Nix FB, Styblo M, Beck MA, Herbin-Davis KM, Hall LL, Simeonsson JB, Thomas DJ (2002). "A novel S-adenosyl-L-methionine:arsenic(III) methyltransferase from rat liver cytosol". J. Biol. Chem. 277 (13): 10795–803. doi:10.1074/jbc.M110246200. PMID 11790780.
↑ "Entrez Gene: AS3MT arsenic (+3 oxidation state) methyltransferase".

Hernández A, Xamena N, Sekaran C, Tokunaga H, Sampayo-Reyes A, Quinteros D, Creus A, Marcos R (2008). "High arsenic metabolic efficiency in AS3MT287Thr allele carriers". Pharmacogenet. Genomics 18 (4): 349–55. doi:10.1097/FPC.0b013e3282f7f46b. PMID 18334919.
Fujihara J, Kunito T, Agusa T, Yasuda T, Iida R, Fujii Y, Takeshita H (2007). "Population differences in the human arsenic (+3 oxidation state) methyltransferase (AS3MT) gene polymorphism detected by using genotyping method". Toxicol. Appl. Pharmacol. 225 (3): 251–4. doi:10.1016/j.taap.2007.08.010. PMID 17889916.
Hernández A, Xamena N, Surrallés J, Sekaran C, Tokunaga H, Quinteros D, Creus A, Marcos R (2008). "Role of the Met(287)Thr polymorphism in the AS3MT gene on the metabolic arsenic profile". Mutat. Res. 637 (1-2): 80–92. doi:10.1016/j.mrfmmm.2007.07.004. PMID 17850829.
Lindberg AL, Kumar R, Goessler W, Thirumaran R, Gurzau E, Koppova K, Rudnai P, Leonardi G, Fletcher T, Vahter M (2007). "Metabolism of low-dose inorganic arsenic in a central European population: influence of sex and genetic polymorphisms". Environ. Health Perspect. 115 (7): 1081–6. doi:10.1289/ehp.10026. PMC 1913583. PMID 17637926.
Schläwicke Engström K, Broberg K, Concha G, Nermell B, Warholm M, Vahter M (2007). "Genetic polymorphisms influencing arsenic metabolism: evidence from Argentina". Environ. Health Perspect. 115 (4): 599–605. doi:10.1289/ehp.9734. PMC 1852682. PMID 17450230.
Meza M, Gandolfi AJ, Klimecki WT (2007). "Developmental and genetic modulation of arsenic biotransformation: a gene by environment interaction?". Toxicol. Appl. Pharmacol. 222 (3): 381–7. doi:10.1016/j.taap.2006.12.018. PMC 2040165. PMID 17306849.
Wood TC, Salavagionne OE, Mukherjee B, Wang L, Klumpp AF, Thomae BA, Eckloff BW, Schaid DJ, Wieben ED, Weinshilboum RM (2006). "Human arsenic methyltransferase (AS3MT) pharmacogenetics: gene resequencing and functional genomics studies". J. Biol. Chem. 281 (11): 7364–73. doi:10.1074/jbc.M512227200. PMID 16407288.
Meza MM, Yu L, Rodriguez YY, Guild M, Thompson D, Gandolfi AJ, Klimecki WT (2005). "Developmentally restricted genetic determinants of human arsenic metabolism: association between urinary methylated arsenic and CYT19 polymorphisms in children". Environ. Health Perspect. 113 (6): 775–81. doi:10.1289/ehp.7780. PMC 1257606. PMID 15929903.
Li J, Waters SB, Drobna Z, Devesa V, Styblo M, Thomas DJ (2005). "Arsenic (+3 oxidation state) methyltransferase and the inorganic arsenic methylation phenotype". Toxicol. Appl. Pharmacol. 204 (2): 164–9. doi:10.1016/j.taap.2004.12.002. PMID 15808521.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.

Transferase: one carbon transferases (EC 2.1)

2.1.1: Methyl-

N-	Histamine N-methyltransferase Phenylethanolamine N-methyltransferase Amine N-methyltransferase Phosphatidylethanolamine N-methyltransferase

O-	5-hydroxyindole-O-methyltransferase/Acetylserotonin O-methyltransferase Catechol-O-methyl transferase

Homocysteine	Betaine-homocysteine methyltransferase Homocysteine methyltransferase Methionine synthase

Other	Phosphatidyl ethanolamine methyltransferase DNMT3B Histone methyltransferase Thymidylate synthase DNA methyltransferase Thiopurine methyltransferase

2.1.2: Hydroxymethyl-,
Formyl- and Related

Hydroxymethyltransferase	Serine hydroxymethyltransferase 3-methyl-2-oxobutanoate hydroxymethyltransferase

Formyltransferase	Phosphoribosylglycinamide formyltransferase Inosine monophosphate synthase

Other	Glutamate formimidoyltransferase Aminomethyltransferase

2.1.3: Carboxy-
and Carbamoyl

Carboxy	methylmalonyl-CoA carboxytransferase

Carbamoyl	Aspartate carbamoyltransferase Ornithine carbamoyltransferase Oxamate carbamoyltransferase Putrescine carbamoyltransferase 3-hydroxymethylcephem carbamoyltransferase Lysine carbamoyltransferase N-acetylornithine carbamoyltransferase

2.1.4: Amidine

Arginine:glycine amidinotransferase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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AS3MT

References

Further reading