Partial characterization of farnesyl and geranylgeranyl diphosphatases induced in rice seedlings by UV-C irradiation

This study reports the identification and characterization of allyl diphosphatases (EC 3.1.7.1) in plants by using rice seedlings. Two distinct Mg(2+)-independent allyl diphosphatases, which convert farnesyl diphosphate (FDP) and geranylgeranyl diphosphate (GGDP) into farnesol and geranylgeraniol, respectively, were induced in rice seedlings irradiated with UV-C. Farnesyl diphosphatase (FDPase) and geranylgeranyl diphosphatase (GGDPase) are located in the microsomal fraction. The relative specific activity of FDPase was much higher than the specific activity of GGDPase. FDPase activity was inhibited by GGDP (50% inhibition at 5 microM) and geranyl diphosphate (50% inhibition at 100 microM). In contrast, GGDPase activity was inhibited 50% by 50 microM isopentenyl diphosphate or 100 microM FDP. The optimal pH for FDPase was 6.3 and for GGDPase was 7.9.