Abstract
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.
Original language | English |
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Pages (from-to) | 9959-9961 |
Number of pages | 3 |
Journal | Journal of Biological Chemistry |
Volume | 254 |
Issue number | 20 |
State | Published - Oct 25 1979 |