作者: Jan KVASSMAN , Gosta PETTERSSON
DOI: 10.1111/J.1432-1033.1989.TB15204.X
关键词:
摘要: The steady-state kinetics of 1,3-bisphosphoglycerate formation through the action phosphoglycerate kinase on 3-phosphoglycerate and ATP have been examined. results show that initial velocities determined by standard method coupling bisphosphoglycerate production to NADH reduction in presence glyceraldehyde-3-phosphate dehydrogenase do not differ significantly from those absence latter enzyme. This observation invalidates proposal dissociation is much too slow account for high rates turnover observed coupled two-enzyme system. capacity rapid release an intrinsic catalytic property does require other enzymes or involvement a mechanism channelized (non-diffusional) transfer producing enzyme consuming one.