Characterization of a -Prenyltransferase from Anther.

A group of prenyltransferases catalyze chain elongation of farnesyl diphosphate (FPP) to designated lengths via consecutive condensation reactions with specific numbers of isopentenyl diphosphate (IPP). -Prenyltransferases, which catalyze -double bond formation during IPP condensation, usually synthesize long-chain products as lipid carriers to mediate peptidoglycan biosynthesis in prokaryotes and protein glycosylation in eukaryotes. Unlike only one or two -prenyltransferases in bacteria, yeast, and animals, plants have several -prenyltransferases and their functions are less understood. As reported here, a -prenyltransferase from anther, named LLA66, was expressed in and characterized to produce C40/C45 products without the capability to restore the growth defect from Rer2-deletion, although it was phylogenetically categorized as a long-chain enzyme. Our studies suggest that evolutional mutations may occur in the plant -prenyltransferase to convert it into a shorter-chain enzyme.