Differences in the Nature of the Phosphoryl Transfer Transition State in Protein Phosphatase 1 and Alkaline Phosphatase: Insights from QM Cluster Models.

ABSTRACT: Quantum mechanical (QM) cluster models are used to probe effects on the catalytic properties of protein phosphatase 1 (PP1) and alkaline phosphatase (AP) due to metal ions and active site residues. The calculations suggest that the phosphoryl transfer transition states in PP1 are synchronous in nature with a significant degree of P-O_lg cleavage, while those in AP are tighter with a modest degree of P-O_lg cleavage and a range of P-O_nuc formation. Similar to observations made in our recent work, a significant degree of cross talk between the forming and breaking P-O bonds complicates the interpretation of the Brønsted relation, especially in regard to AP for which the computed β_lg/β_EQ,lg value does not correlate with the degree of P-O

SUBMITTER: Lai R 

PROVIDER: S-EPMC7647665 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature