What Does the Bronsted Slope Measure in the Phosphoryl Transfer Transition State?

ABSTRACT: The structural and energetic features of phosphate and phosphonate hydrolysis in Protein Phosphatase-1 (PP1) and water are studied using quantum mechanical (QM) cluster models. The calculations are able to reproduce observed kinetic isotope effects and capture several key trends in the experimental Brønsted plots: the β l g values are rather different for phosphate and phosphonate ester hydrolysis in solution but are similar in PP1. Detailed analyses of structure, charge distribution and bond order of computed transition states support the general conclusion from experimental study that phosphoryl transfer transition states are different for the two classes of substrates in solution but similar in PP1. On the other hand, the microscopic models also highlight notable differences between

SUBMITTER: Lai R 

PROVIDER: S-EPMC8457673 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature