The stereochemical course of thiophosphoryl group transfer catalyzed by adenosine kinase

John P. Richard; Michael C. Carr; David H. Ives; Perry A. Frey

doi:10.1016/0006-291X(80)90525-2

The stereochemical course of thiophosphoryl group transfer catalyzed by adenosine kinase

John P. Richard
, Michael C. Carr
, David H. Ives
, Perry A. Frey

Chemistry

Ohio State University

Research output: Contribution to journal › Article › peer-review

23 Scopus citations

Abstract

Adenosine kinase was partially purified form beef liver and used to catalyze the conversion of (γR)ATPγS,γ¹⁸O and adenosine to ADP and AMPαS,α¹⁸O. The configuration at phosphorus in AMPαS,α¹⁸O was established by subjecting it to stereospecific phosphorylation to (αS)ATPαS,α¹⁸O and showing that only the nonbridging oxygen bonded to the α-P was enriched with ¹⁸O. The configuration at α-P in AMPαS,α¹⁸O was therefore S, and the transfer of the [¹⁸O]thiophosphoryl group occurred with inversion of configuration.

Original language	English
Pages (from-to)	1052-1056
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	94
Issue number	4
DOIs	https://doi.org/10.1016/0006-291X(80)90525-2
State	Published - Jun 30 1980

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title = "The stereochemical course of thiophosphoryl group transfer catalyzed by adenosine kinase",

abstract = "Adenosine kinase was partially purified form beef liver and used to catalyze the conversion of (γR)ATPγS,γ18O and adenosine to ADP and AMPαS,α18O. The configuration at phosphorus in AMPαS,α18O was established by subjecting it to stereospecific phosphorylation to (αS)ATPαS,α18O and showing that only the nonbridging oxygen bonded to the α-P was enriched with 18O. The configuration at α-P in AMPαS,α18O was therefore S, and the transfer of the [18O]thiophosphoryl group occurred with inversion of configuration.",

author = "Richard, \{John P.\} and Carr, \{Michael C.\} and Ives, \{David H.\} and Frey, \{Perry A.\}",

year = "1980",

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doi = "10.1016/0006-291X(80)90525-2",

language = "English",

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journal = "Biochemical and Biophysical Research Communications",

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T1 - The stereochemical course of thiophosphoryl group transfer catalyzed by adenosine kinase

AU - Richard, John P.

AU - Carr, Michael C.

AU - Ives, David H.

AU - Frey, Perry A.

PY - 1980/6/30

Y1 - 1980/6/30

N2 - Adenosine kinase was partially purified form beef liver and used to catalyze the conversion of (γR)ATPγS,γ18O and adenosine to ADP and AMPαS,α18O. The configuration at phosphorus in AMPαS,α18O was established by subjecting it to stereospecific phosphorylation to (αS)ATPαS,α18O and showing that only the nonbridging oxygen bonded to the α-P was enriched with 18O. The configuration at α-P in AMPαS,α18O was therefore S, and the transfer of the [18O]thiophosphoryl group occurred with inversion of configuration.

AB - Adenosine kinase was partially purified form beef liver and used to catalyze the conversion of (γR)ATPγS,γ18O and adenosine to ADP and AMPαS,α18O. The configuration at phosphorus in AMPαS,α18O was established by subjecting it to stereospecific phosphorylation to (αS)ATPαS,α18O and showing that only the nonbridging oxygen bonded to the α-P was enriched with 18O. The configuration at α-P in AMPαS,α18O was therefore S, and the transfer of the [18O]thiophosphoryl group occurred with inversion of configuration.

UR - https://www.scopus.com/pages/publications/0019335866

U2 - 10.1016/0006-291X(80)90525-2

DO - 10.1016/0006-291X(80)90525-2

M3 - Article

C2 - 6249295

AN - SCOPUS:0019335866

SN - 0006-291X

VL - 94

SP - 1052

EP - 1056

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

The stereochemical course of thiophosphoryl group transfer catalyzed by adenosine kinase

Abstract

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