Elucidating pathway arsenic methylation

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About 90% of the molybdenum eaten in foods is eliminated by the body through the urine.

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Because methylation of inorganic arsenic activates it to more reactive and toxic forms, elucidating the pathway for the methylation of this metalloid is a topic of considerable importance.Here we describe a new S-adenosylmethionine (Ado Met)-dependent methyltransferase from rat liver cytosol that catalyzes the conversion of arsenite to methylated and dimethylated species.This 42-k Da protein has sequence motifs common to many non-nucleic acid methyltransferases and is closely related to methyltransferases of previously unknown function that have been identified by conceptual translations of cyt19 genes of mouse and human genomes.Our studies with recombinant rat cyt19 find that, in the presence of an exogenous or a physiological reductant, this protein can catalyze the entire sequence of reactions that convert arsenite to methylated metabolites. A scheme linking cyt19 and thioredoxin-thioredoxin reductase in the methylation and reduction of arsenicals is proposed.

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