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J. Biol. Chem., Vol. 255, Issue 8, 3240-3241, Apr, 1980

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

EK Jaffe and M Cohn

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.
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