Dinitrophenol, dicoumarol and pentachlorophenol as inhibitors and parasite substrates in the ATP phosphoribosyltransferase reaction.

Adenosine-triphosphate phosphoribosyltransferase from Escherichia coli is inhibited by dicoumarol and pentachlorophenol in competition with ATP. Ki was approximately 60 muM for dicoumarol and 50 muM for pentachlorophenol. Carbonylcyanide m-chlorphenylhydrazine did not seem to have any kinetic effect. Dicoumarol is bound to the extent of 6 sites per enzyme hexamer with a dissociation constant Kd of 50 muM. Dicoumarol and pentachlorophenol partly prevent the binding of ATP and AMP to the transferase. The reverse reaction is inhibited by dicoumarol and pentachlorophenol without changes in [s]0.5 for phosphoribostladenosine trophosphate. Dicumarol, dinitrophenol and pentachlorophenol diminish the yield of phosphoribosyladenosine triphosphate in the transferase reaction apparently by acting as parasite substrates; carbonylcyanide m-chlorophenylhydrazone had no effect.