Stereochemistry of hydrolysis of adenosine 3':5'-cyclic phosphorothioate by the cyclic phosphodiesterase from beef heart.

P. M. Burgers, F. Eckstein, D. H. Hunneman, J. Baraniak, R. W. Kinas, K. Lesiak, W. J. Stec

Research output: Contribution to journalArticlepeer-review

64 Scopus citations

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 languageEnglish
Pages (from-to)9959-9961
Number of pages3
JournalJournal of Biological Chemistry
Volume254
Issue number20
StatePublished - Oct 25 1979

Fingerprint

Dive into the research topics of 'Stereochemistry of hydrolysis of adenosine 3':5'-cyclic phosphorothioate by the cyclic phosphodiesterase from beef heart.'. Together they form a unique fingerprint.

Cite this