Configuration of the active Mg‐ATP complex in protein kinase C reaction

Abstract

To probe the active site structure of protein kinase C stereochemical studies were carried out by using ATPBS. The enzyme utilizes either one of the diastereomers (Sr and RP) of ATPj?S almost equally well as a substrate. This result contrasts with that for cyclic AMP-dependent protein kinase, suggesting that the topography of the nucleotide-binding site is significantly different between the two kinases. Phosphorylation Protein kinase C ATP/?S Stereospecijicity