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.
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.
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives; D004163:Diphosphoglyceric Acids; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D010735:Phosphoglycerate Kinase / Q000378:metabolism*; D012441:Saccharomyces cerevisiae; D013379:Substrate Specificity; D013873:Thionucleotides
D004163:Diphosphoglyceric Acids; D013873:Thionucleotides; C022570:adenosine 5'-O-(2-thiotriphosphate); D000255:Adenosine Triphosphate; D010735:Phosphoglycerate Kinase