Dall-Larsen T, Kryvi H, Klungsoyr L
Eur J Biochem. 1976 Jul 15;66(3):443-6. doi: 10.1111/j.1432-1033.1976.tb10568.x.
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.
来自大肠杆菌的三磷酸腺苷磷酸核糖基转移酶受到双香豆素和五氯酚的抑制，它们与ATP存在竞争关系。双香豆素的抑制常数Ki约为60μM，五氯酚的Ki约为50μM。羰基氰化物间氯苯腙似乎没有任何动力学效应。双香豆素以每个酶六聚体6个位点的程度结合，解离常数Kd为50μM。双香豆素和五氯酚部分阻止ATP和AMP与转移酶的结合。逆反应受到双香豆素和五氯酚的抑制，而磷酸核糖基腺苷三磷酸的[s]0.5没有变化。双香豆素、二硝基苯酚和五氯酚显然通过作为寄生底物降低了转移酶反应中磷酸核糖基腺苷三磷酸的产量；羰基氰化物间氯苯腙没有作用。
