ROLE OF THE PHOSPHATE MOIETY IN THE AFFINITY OF INHIBITORS FOR THE GLYCOLYTIC ENZYME GLYCERALDEHYDEPHOSPHATE DEHYDROGENASE (GAPDH)

Kinetic inhibition studies of the title enzyme by substrate analogues bearing reactive groups, epoxyde or alpha-enone, indicate that the sub stituents on the phosphorus atom play a crucial role in the efficiency of these inhibitors. This result is accounted for by their affinity f or an hydrophobic part of the protein, in close vicinity to the residu e responsible for the covalent binding.