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

Ajees, Abdul A (2015) As(III) S-Adenosylmethionine Methyltransferases and Other Arsenic Binding Proteins. Geomicrobiology Journal, 32 (7). pp. 570-576.

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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.

Item Type: Article
Uncontrolled Keywords: Arsenic; AS3MT; ArsM; As(III) S-adenosylmethionine methyltransferse; Glutathione
Subjects: Departments at MU > Atomic Molecular Physics
Depositing User: KMC Library
Date Deposited: 24 Sep 2015 09:50
Last Modified: 24 Sep 2015 09:50

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