The stereochemical course of thiophosphoryl group transfer catalyzed by T4 polynucleotide kinase.

F. R. Bryant, S. J. Benkovic, D. Sammons, P. A. Frey

Research output: Contribution to journalArticlepeer-review

Abstract

The stereochemical course of the phosphoryl transfer reaction catalyzed by T4 polynucleotide kinase has been determined using the chiral ATP analog, (Sp)-adenosine-5'-(3-thio-3-[18O]triphosphate). T4 polynucleotide kinase catalyzes the transfer of the gamma-thiophosphoryl group of (Sp)-adenosine-5'-(3-thio-3-[18O]triphosphate) to the 5'-hydroxyl group of ApA to give the thiophosphorylated dinucleotide adenyl-5'-[18O]phosphorothioate-(3'-5')adenosine. A sample of adenyl-5'-[18O]phosphorothioate-(3'-5')adenosine was subjected to venom phosphodiesterase digestion. The resulting adenosine-5'-[18O]phosphorothioate was shown to have the Rp configuration, thus indicating that the thiophosphoryl transfer reaction occurs with overall inversion of configuration of phosphorus.

Original languageEnglish (US)
Pages (from-to)5965-5966
Number of pages2
JournalJournal of Biological Chemistry
Volume256
Issue number12
StatePublished - Jun 25 1981
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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