AS3MT

AS3MT
Identifiers
Aliases	AS3MT, CYT19, arsenite methyltransferase
External IDs	OMIM: 611806; MGI: 1929882; HomoloGene: 10754; GeneCards: AS3MT; OMA:AS3MT - orthologs
Gene location (Human)
Chr.	Chromosome 10 (human)
End	102,901,899 bp
Gene location (Mouse)
Chr.	Chromosome 19 (mouse)
End	46,729,538 bp
RNA expression pattern
	Top expressed in
	right adrenal gland; ; right adrenal cortex; ; left adrenal cortex; ; right lobe of liver; ; apex of heart; ; left ventricle; ; ganglionic eminence; ; ventricular zone; ; right auricle; ; spleen;
	Top expressed in
	yolk sac; ; right kidney; ; soleus muscle; ; proximal tubule; ; interventricular septum; ; median eminence; ; arcuate nucleus; ; myocardium of ventricle; ; neural layer of retina; ; Paneth cell;
	More reference expression data
	n/a
Gene ontology
Molecular function	methyltransferase activity; transferase activity; methylarsonite methyltransferase activity; arsenite methyltransferase activity;
Cellular component	cytosol; cytoplasm;
Biological process	toxin metabolic process; arsonoacetate metabolic process; methylation;
	Sources:Amigo / QuickGO
Orthologs
	57412
	57344
	ENSG00000214435
	ENSMUSG00000003559
	Q9HBK9
	Q91WU5
	NM_020682
	NM_020577
	NP_065733
	NP_065602
	Wikidata
View/Edit Human	View/Edit Mouse

Arsenite methyltransferase is an enzyme that in humans is encoded by the AS3MT gene.^[5]^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000214435 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000003559 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ "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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000214435 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000003559 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid11790780-5] 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[entrez-6] "Entrez Gene: AS3MT arsenic (+3 oxidation state) methyltransferase".

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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

References

Further reading