Configuration of the active Mg-ATP complex in protein kinase C reaction.
To probe the active site structure of protein kinase C stereochemical studies were carried out by using ATP beta S. The enzyme utilizes either one of the diastereomers (SP and RP) of ATP beta 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.
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D007700:Kinetics; D008968:Molecular Conformation; D011493:Protein Kinase C / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013873:Thionucleotides / Q000378:metabolism
D013873:Thionucleotides; C022570:adenosine 5'-O-(2-thiotriphosphate); D000255:Adenosine Triphosphate; D011494:Protein Kinases; D011493:Protein Kinase C