Isotope effects in the study of phosphoryl and sulfuryl transfer reactions.
Phosphoryl and sulfuryl transfer reactions are essential biological processes. Multiple kinetic isotope effects have provided significant insights into the transition states of these reactions. The data are reviewed for the uncatalyzed reactions of phosphate and sulfate monoesters and for a number of enzymatic phosphoryl transfer reactions. Uncatalyzed phosphoryl and sulfuryl hydrolysis reactions are found to have very similar transition states. The phosphoryl transfer reaction catalyzed by protein-tyrosine phosphatases proceeds by a transition state very similar to that of the uncatalyzed reaction, but isotope effect data reveal an interesting interplay between the conserved arginine and enzyme dynamics involving general acid catalysis.
Hengge
Alvan C
AC
Department of Chemistry & Biochemistry, Utah State University, Logan, Utah 84322, USA.
D002384:Catalysis / Q000187:drug effects; D006867:Hydrolases / Q000737:chemistry*; D007554:Isotopes / Q000494:pharmacology; D007700:Kinetics; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry; D010770:Phosphotransferases / Q000737:chemistry; D013429:Sulfatases / Q000737:chemistry
D007554:Isotopes; D010770:Phosphotransferases; D006867:Hydrolases; D010744:Phosphoric Monoester Hydrolases; D013429:Sulfatases