As(III) S-Adenosylmethionine Methyltransferases and Other Arsenic Binding Proteins

作者：Ajees A Abdul; Rosen Barry P^*

来源：Geomicrobiology Journal, 2015, 32(7): 570-576.

DOI：10.1080/01490451.2014.908983

• arsenic
• AS3MT
• ArsM
• As(III) S-adenosylmethionine methyltransferse
• glutathione

Efflux is by far the most common means of arsenic detoxification. Another mechanism is methylation catalyzed by a family of As(III) S-adenosylmethionine (SAM) methyltransferases (MTs) enzymes designated ArsM in microbes or AS3MT in higher eukaryotes. The protein sequence of more than 5000 AS3MT/ArsM orthologues were deposited in the NCBI database, primarily in prokaryotic and eukaryotic microbes. As(III) SAM MTs are members of a large superfamily of MTs involved in numerous physiological functions. ArsMs detoxify arsenic by conversion of inorganic trivalent arsenic (As(III)) into mono-, di- and trimethylated species that may be more toxic and carcinogenic than inorganic arsenic. The pathway of methylation remains controversial. Several hypotheses are examined in this review.

• 出版日期2015-8-9