2.1.1.137	C10S	activtiy similar to wild-type	757684	
2.1.1.137	C10S/C11S/C193S/C268S	mutant dispays activity	757684	
2.1.1.137	C11S	activity similar to wild-type	757684	
2.1.1.137	C145S	loss of catalytic activity	757684	
2.1.1.137	C165S	inactive	721074	
2.1.1.137	C174A	the mutation leads to loss of As(III) methylation	718946	
2.1.1.137	C186S	mutation abolishes the capability of As(III) methylation	757317	
2.1.1.137	C193S	activity similar to wild-type	757684	
2.1.1.137	C195S	loss of catalytic activity	757684	
2.1.1.137	C210S	inactive	721074	
2.1.1.137	C224A	the mutation leads to loss of As(III) methylation	718946	
2.1.1.137	C238S	mutation abolishes the capability of As(III) methylation	757317	
2.1.1.137	C250S	the mutation favors S-adenosyl-L-methionine binding to the enzyme	735126	
2.1.1.137	C268S	activity similar to wild-type	757684	
2.1.1.137	C271S	the mutation does not affect the activity and structure of the enzyme	719012	
2.1.1.137	C334S	the mutation decreases the enzymatic turnover and changes the conformation of the enzyme	719012	
2.1.1.137	C360S	the mutation decreases the enzymatic turnover and changes the conformation of the enzyme	719012	
2.1.1.137	C375S	the mutation does not affect the activity and structure of the enzyme	719012	
2.1.1.137	C44A	mutant is unable to methylate arsenic(III) but retains the ability to methylate methylarsenate	755717	
2.1.1.137	C44A/C72A	mutant is unable to methylate arsenic(III) but retains the ability to methylate methylarsenate	755717	
2.1.1.137	C59S	mutation abolishes the capability of As(III) methylation	757317	
2.1.1.137	C72A	the mutation leads to loss of As(III) methylation, but still shows trivalent methylarsenate methylation	718946	
2.1.1.137	C72S	the mutant is completely inactive	719012	
2.1.1.137	D102N	inactive	733865	
2.1.1.137	D102P	inactive	733865	
2.1.1.137	D150N	the mutant shows reduced activity compared to the wild type enzyme	733865	
2.1.1.137	D150P	inactive	733865	
2.1.1.137	D76N	inactive	733865	
2.1.1.137	D76P	inactive	733865	
2.1.1.137	D84N	inactive	733865	
2.1.1.137	D84P	inactive	733865	
2.1.1.137	G134A	the mutant’s activity is seriously impaired compared with that of wild type	733425	
2.1.1.137	G60A	inactive	733425	
2.1.1.137	G80A	inactive	733425	
2.1.1.137	G82A	the mutant’s activity is seriously impaired compared with that of wild type	733425	
2.1.1.137	I101A	inactive	733425	
2.1.1.137	L160A	inactive	733425	
2.1.1.137	L77A	the mutant’s activity is seriously impaired compared with that of wild type	733425	
2.1.1.137	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	700331	
2.1.1.137	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	701300	
2.1.1.137	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	721075	
2.1.1.137	M287T	naturally occuring mutant	697642	
2.1.1.137	M287T	the mutation is associated with an increased percentage of monomethylated arsenic in urine	718712	
2.1.1.137	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	733451	
2.1.1.137	additional information	an exon-4 and -5 skipping (DELTA4,5) truncated mutant form does not convert arsenite to monomethylarsonate or dimethylarsinic acid	718748	
2.1.1.137	N155A	inactive	733425	
2.1.1.137	R57A	the mutant's activity is seriously impaired compared with that of wild type	733425	
2.1.1.137	R83A	the mutant’s activity is seriously impaired compared with that of wild type	733425	
2.1.1.137	S81A	the mutant’s activity is seriously impaired compared with that of wild type	733425	
2.1.1.137	T104A	the mutant’s activity is seriously impaired compared with that of wild type	733425	
2.1.1.137	V157A	the mutant’s activity is seriously impaired compared with that of wild type	733425	
2.1.1.137	V161A	the mutant’s activity is seriously impaired compared with that of wild type	733425	
2.1.1.137	Y135A	the mutant’s activity is seriously impaired compared with that of wild type	733425	
2.1.1.137	Y58A	the mutant’s activity is seriously impaired compared with that of wild type	733425	
2.1.1.137	Y70W	the mutant exhibits metalloid binding	718946