New insights into the mechanism of arsenite methylation with the recombinant human arsenic (+3) methyltransferase (hAS3MT)

Biochimie
Xiaoli SongZhilin Wang

Abstract

The catalytic mechanism of the recombinant human arsenic (+3) methyltransferase (hAS3MT) was studied using kinetics, initial velocity and spectroscopy. The production and the distribution of methylated arsenicals changed with various concentrations of arsenite/S-adenosyl-L-methionine (SAM)/thiols, enzyme contents, and incubation times. These results suggest a sequential methylation of arsenite to monomethylated arsenicals (MMA) and dimethylated arsenicals (DMA). In addition, competition exists between the two reactions. hAS3MT showed the greatest activity at pH 8.5 with glutathione (GSH) as the reductant. This might indicate that a balance between the deprotonation and protonation of sulfhydryl groups is required. Initial velocity studies illuminate an ordered sequence for the binding of SAM and arsenite to the hAS3MT; while GSH should probably be placed either as the first reactant or as a reactant combining with the enzyme only after products have been released. The interactions between substrate/cofactors and the hAS3MT were first monitored by UV-visible and circular dichroism spectroscopy. It revealed that arsenite and SAM combined with the hAS3MT before reaction started; whereas, no interactions between GSH and the hAS3MT ...Continue Reading

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Jul 20, 2012·Archives of Toxicology·Takayuki Watanabe, Seishiro Hirano
Oct 18, 2011·Applied and Environmental Microbiology·Frank ThomasReinhard Hensel
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