PMID: 6988421Apr 25, 1980Paper

Shift of the equilibrium constant of the 3-P-glycerate kinase reaction towards 1,3-bis-P-glycerate with adenosine 5'-O-(2-thiotriphosphate) (ATP beta S) as substrate.

The Journal of Biological Chemistry
E K Jaffe, M Cohn

Abstract

It has been demonstrated that the reaction of ATP beta S and 3-P-glycerate catalyzed by 3-P-glycerate kinase, unlike the reaction with ATP, can form a readily detectable amount of 1,3-bis-P-glycerate as observed by 31P NMR. By quantifying production of 1,3-bis-P-glycerate from the phosphorothioate analogue of ATP as a function of time as the reaction approaches equilibrium, Keq for the reaction was estimated to be approximately 400, about 1 order of magnitude less than the equilibrium constant previously reported for the analogous reaction of the normal nucleotide substrates.

Related Concepts

adenosine 5'-O-(2-thiotriphosphate)
Adenosine Triphosphate, Chromium Ammonium Salt
Diphosphoglyceric Acids
Kinetics
In Vivo NMR Spectroscopy
Phosphoglycerate KINASE
Saccharomyces cerevisiae
Substrate Specificity
Thionucleotides

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