Different roles of the diphosphate moieties of allylic and homoallylic diphosphates in prenyltransferase reaction.
In contrast to the reactivity of geranyl methylene-diphosphonate in the reaction catalyzed by farnesyl diphosphate synthase, that of isopentenyl methylenediphosphonate showed an optimum at a more acidic pH than that of isopentenyl diphosphate, and it was inhibited by magnesium ions under certain conditions. These facts suggest that isopentenyl diphosphate is engaged in the enzyme reaction in the form of metal-free substrate contrary to the allylic substrate, which reacts in the form of metal-complexed substrate. Thus the diphosphate moieties of allylic and homoallylic substrates have different roles in the prenyltransferase reaction.
Gotoh
T
T
Chemical Research Institute of Non-Aqueous Solutions, Tohoku University, Sendai, Japan.
Koyama
T
T
Ogura
K
K
D000818:Animals; D001665:Binding Sites; D004122:Dimethylallyltranstransferase / Q000378:metabolism*; D004164:Diphosphonates / Q000138:chemical synthesis / Q000378:metabolism* / Q000494:pharmacology; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D011485:Protein Binding; D013379:Substrate Specificity; D013552:Swine; D014166:Transferases / Q000378:metabolism*
D004164:Diphosphonates; C057370:isopentenyl methylenediphosphonate; D014166:Transferases; D004122:Dimethylallyltranstransferase