Stereochemistry of hydrolysis of adenosine 3':5'-cyclic phosphorothioate by the cyclic phosphodiesterase from beef heart.
Adenosine 3':5'-cyclic phosphorothioate, Sp-diastereomer was hydrolyzed by cyclic phosphodiesterase from beef heart in the presence of [18O]water to [18O]adenosine 5'-phosphorothioate. This was phosphorylated by myokinase and pyruvate kinase to [18O]adenosine 5'-(1-thiotriphosphate),Sp-diastereomer. The position of 18O was determined to be in a nonbridging position. This result indicates that the hydrolysis proceeded with inversion of configuration at phosphorus.
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D000242:Cyclic AMP / Q000031:analogs & derivatives*; D008968:Molecular Conformation; D009206:Myocardium / Q000201:enzymology*; D010103:Oxygen Isotopes; D013237:Stereoisomerism; D013873:Thionucleotides
D010103:Oxygen Isotopes; D013873:Thionucleotides; D000242:Cyclic AMP; D015105:3',5'-Cyclic-AMP Phosphodiesterases