A complete initial velocity study of the 6-phosphogluconate dehydrogenase from Candida utilis at pH 7 and 25 degrees C in both reaction directions suggests a rapid equilibrium random kinetic mechanism with dead-end E:NADP:(ribulose 5-phosphate) and E:NADPH:(6-phosphogluconate) complexes. Like substrate-product (NADP/NADPH and 6-phosphogluconate/ribulose 5-phosphate) pairs are competitive whatever the concentration of the other substrates but noncompetitive versus the other substrates, e.g., NADPH exhibits noncompetitive inhibition versus 6-phosphogluconate. This trend also holds true for all dead-end analogs, e.g., ATP-ribose is competitive versus NADP and noncompetitive versus 6-phosphogluconate. A quantitative analysis of the kinetic inhibition constants supports the assignment of kinetic mechanism. The ratio of the maximum velocities in the oxidative decarboxylation and reductive carboxylation directions is 75.
No takes yet. Share an insight, caveat, or question.
Berdis et al. (1993) studied this question.
Synapse has enriched 5 related papers. Consider them for comparative context: