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. 2010 Aug 4;584(15):3366-9.
doi: 10.1016/j.febslet.2010.06.022. Epub 2010 Jun 18.

The Human Xenobiotic-Metabolizing Enzyme Arylamine N-acetyltransferase 1 (NAT1) Is Irreversibly Inhibited by Inorganic (Hg2+) and Organic Mercury (CH3Hg+): Mechanism and Kinetics

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The Human Xenobiotic-Metabolizing Enzyme Arylamine N-acetyltransferase 1 (NAT1) Is Irreversibly Inhibited by Inorganic (Hg2+) and Organic Mercury (CH3Hg+): Mechanism and Kinetics

Nilusha Ragunathan et al. FEBS Lett. .
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Abstract

Human arylamine N-acetyltransferase 1 (NAT1) is a xenobiotic-metabolizing enzyme that biotransforms aromatic amine chemicals. We show here that biologically-relevant concentrations of inorganic (Hg2+) and organic (CH3Hg+) mercury inhibit the biotransformation functions of NAT1. Both compounds react irreversibly with the active-site cysteine of NAT1 (half-maximal inhibitory concentration (IC50)=250 nM and kinact=1.4x10(4) M(-1) s(-1) for Hg2+ and IC50=1.4 microM and kinact=2x10(2) M(-1) s(-1) for CH3Hg+). Exposure of lung epithelial cells led to the inhibition of cellular NAT1 (IC50=3 and 20 microM for Hg2+ and CH3Hg+, respectively). Our data suggest that exposure to mercury may affect the biotransformation of aromatic amines by NAT1.

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