The equilibrium constant of the phosphoglyceromutase reaction.
The equilibrium constant of the phosphoglyceromutase reaction was determined over a range of pH (5.4-7.9), in solutions of different ionic strength (0.06-0.3) and in the presence of Mg(2+), at 30 degrees C and at 20 degrees C. The values obtained (8.65-11.65) differ substantially from previously published values. The third acid dissociation constants were redetermined for 2- and 3-phosphoglycerate, and in contrast with previous reports the pK values (7.03 and 6.97 respectively at zero ionic strength) were closely similar. The Mg(2+)-binding constants were measured spectrophotometrically and the values, 286mm(-1) and 255mm(-1) for 2- and 3-phosphoglycerate at pH7 and ionic strength 0.02, were also very similar. From the relative lack of effect of temperature, pH and ionic strength it is concluded that the equilibrium constant differs from unity largely because of entropic factors. At low ionic strength, in the neutral region, the pH-dependence can be attributed to the small difference in the acid dissociation constants, but the difference in dissociation constants does not explain the pH-dependence in the acid region or at high ionic strength. Within physiological ranges of pH, Mg(2+) concentration and ionic strength there will be little variation in equilibrium constant.
D000136:Acid-Base Equilibrium; D001665:Binding Sites; D002021:Buffers; D004163:Diphosphoglyceric Acids; D007700:Kinetics; D008274:Magnesium; D010770:Phosphotransferases / Q000378:metabolism*; D011485:Protein Binding; D013696:Temperature
D002021:Buffers; D004163:Diphosphoglyceric Acids; D010770:Phosphotransferases; D008274:Magnesium