New structural and chemical insight into the catalytic mechanism of epoxide hydrolases.
New structural and mechanistic data on epoxide hydrolases provide additional insight into the details of how these enzymes function. The data reveal that, in addition to the catalytic triad located in the core domain that carries out the hydrolytic reaction, there are two tyrosine residues, located in the cap domain, which assist in the initial alkylation event.
Armstrong
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Department of Biochemistry, Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146, USA. armstrong@toxicology.mc.vanderbilt.edu
Cassidy
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D001667:Binding, Competitive; D002384:Catalysis; D004851:Epoxide Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D004852:Epoxy Compounds / Q000378:metabolism; D005544:Forecasting; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D008958:Models, Molecular; D011487:Protein Conformation
D004852:Epoxy Compounds; D004851:Epoxide Hydrolases