Substrate specificities of wild and mutated farnesyl diphosphate synthases: Reactivity of allylic substrate homologs having hydrophilic groups at ω-position

Abstract

To investigate substrate specificities of wild and mutated types of farnesyl diphosphate synthases from Bacillus stearothermophilus, we have examined the reactivities of methoxymethoxydimethylallyl- and propoxygeranyl diphosphates as allylic substrate homologs. The wild type farnesyl diphosphate synthase reaction of methoxymethoxydimethylallyl and propoxygeranyl diphosphates with isopentenyl diphosphate gave methoxymethoxygeranyl and propoxyfarnesyl diphosphates which stopped at the first stage of the condensation. Using a mutated farnesyl diphosphate synthase (Y81D FPS), the reaction of methoxymethoxydimethylallyl diphosphate with isopentenyl diphosphate gave only methoxymethoxyfarnesyl diphosphate as single condensation product. Moreover, both of mutated farnesyl diphosphate synthase reaction with propoxygeranyl diphosphate of isopentenyl diphosphate gave propoxyfarnesyl- and propoxygeranylgeranyl diphosphate.