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

A. Abdul Ajees, Barry P. Rosen

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)570-576
Number of pages7
JournalGeomicrobiology Journal
Volume32
Issue number7
DOIs
Publication statusPublished - 01-01-2015

Fingerprint

S-Adenosylmethionine
Methyltransferases
Arsenic
arsenic
Carrier Proteins
Methylation
protein
methylation
Detoxification
Poisons
eukaryote
detoxification
Eukaryota
Databases
enzyme
Enzymes
Proteins

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Environmental Chemistry
  • Environmental Science(all)
  • Earth and Planetary Sciences (miscellaneous)

Cite this

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As(III) S-Adenosylmethionine Methyltransferases and Other Arsenic Binding Proteins. / Ajees, A. Abdul; Rosen, Barry P.

In: Geomicrobiology Journal, Vol. 32, No. 7, 01.01.2015, p. 570-576.

Research output: Contribution to journalArticle

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