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

F. R. Bryant, Stephen Benkovic, D. Sammons, P. A. Frey

Research output: Contribution to journalArticle

17 Citations (Scopus)

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

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Polynucleotide 5'-Hydroxyl-Kinase
Adenosine
Venoms
Phosphoric Diester Hydrolases
Hydroxyl Radical
Phosphorus
Digestion
Adenosine Triphosphate
adenosine 5'-phosphorothioate
triphosphoric acid

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Bryant, F. R., Benkovic, S., Sammons, D., & Frey, P. A. (1981). The stereochemical course of thiophosphoryl group transfer catalyzed by T4 polynucleotide kinase. Journal of Biological Chemistry, 256(12), 5965-5966.
Bryant, F. R. ; Benkovic, Stephen ; Sammons, D. ; Frey, P. A. / The stereochemical course of thiophosphoryl group transfer catalyzed by T4 polynucleotide kinase. In: Journal of Biological Chemistry. 1981 ; Vol. 256, No. 12. pp. 5965-5966.
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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.",
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Bryant, FR, Benkovic, S, Sammons, D & Frey, PA 1981, 'The stereochemical course of thiophosphoryl group transfer catalyzed by T4 polynucleotide kinase.', Journal of Biological Chemistry, vol. 256, no. 12, pp. 5965-5966.

The stereochemical course of thiophosphoryl group transfer catalyzed by T4 polynucleotide kinase. / Bryant, F. R.; Benkovic, Stephen; Sammons, D.; Frey, P. A.

In: Journal of Biological Chemistry, Vol. 256, No. 12, 25.06.1981, p. 5965-5966.

Research output: Contribution to journalArticle

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T1 - The stereochemical course of thiophosphoryl group transfer catalyzed by T4 polynucleotide kinase.

AU - Bryant, F. R.

AU - Benkovic, Stephen

AU - Sammons, D.

AU - Frey, P. A.

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N2 - 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.

AB - 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.

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