Evidence that 1,3-bisphosphoglycerate dissociation from phosphoglycerate kinase is an intrinsically rapid reaction step.

The steady-state kinetics of 1,3-bisphosphoglycerate formation through the action of phosphoglycerate kinase on 3-phosphoglycerate and ATP have been examined. The results show that initial velocities determined by the standard method of coupling bisphosphoglycerate production to NADH reduction in the presence of glyceraldehyde-3-phosphate dehydrogenase do not differ significantly from those determined in the absence of the latter enzyme. This observation invalidates the proposal that bisphosphoglycerate dissociation from phosphoglycerate kinase is much too slow to account for the high rates of phosphoglycerate turnover observed in the coupled two-enzyme system. The capacity for rapid bisphosphoglycerate production and release is an intrinsic catalytic property of phosphoglycerate kinase that does not require the presence of other enzymes or the involvement of a mechanism of channelized (non-diffusional) transfer of bisphosphoglycerate from the producing enzyme to the consuming one.