Diverse catalytic activities in the alphabeta-hydrolase family of enzymes: activation of H2O, HCN, H2O2, and O2.
The article describes the observation of novel catalytic activities in the alphabeta-hydrolase superfamily apparently unrelated to ester hydrolysis and unexpected biochemical observations relating to the structure and function of the serine catalytic triad in these enzymes. One common feature of these novel activities is the activation of a small diatomic molecule, but via diverse chemistry. Possible mechanisms of catalysis are discussed.
Bugg
Timothy D H
TD
Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK. T.D.Bugg@warwick.ac.uk
D002384:Catalysis; D006856:Hydrogen Cyanide / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000737:chemistry*; D006867:Hydrolases / Q000737:chemistry* / Q000378:metabolism; D007527:Isoenzymes / Q000737:chemistry* / Q000378:metabolism; D010100:Oxygen / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D014867:Water / Q000737:chemistry*
D007527:Isoenzymes; D014867:Water; D006856:Hydrogen Cyanide; D006861:Hydrogen Peroxide; D006867:Hydrolases; D010100:Oxygen