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Research efforts in Professor Armstrong's laboratory are embodied in three projects directed at elucidating the mechanisms of action of enzymes involved in the metabolism of foreign or xenobiotic molecules. These catalysts, known as detoxication enzymes, are essential components of any organism's ability to resist chemical insult. The first project is a study of glutathione transferases, a family of enzymes involved in the metabolism of electrophilic molecules such as expoxides, alkyl halides and a,b-unsaturated carbonyl compounds. From studies of the physical organic chemistry occurring in the active site, aspects of the kinetic, chemical, and stereochemical mechanisms of these enzymes have been elucidated. In addition, high-resolution three-dimensional structures of several glutathione transferases have been solved and are being used as a guide in the construction of chimeric or hybrid enzymes with altered catalytic properties. The functional properties of the mutant enzymes provide insight into the specific role of various amino acid residues in the region of the active site. The site-general and site-specific incorporation of unnatural amino acids into this enzyme is being investigated as a tool to refine our understanding of the mechanism of catalysis. Many detoxication enzymes are membrane-bound and pose unique problems for mechanistic analysis.
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PloS oneno. 9 (2016): e0163600-e0163600
mag(2015)
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