Abstract
Aromatic prenyltransferases (PTases) catalyze the transfer of a C5 (dimethylallyl), C10 (geranyl) or C15 (farnesyl) prenyl group derived from the corresponding isoprenyl diphosphate metabolites onto a variety of electron-rich aromatic acceptors. Prenyl groups appear in a wide variety of bioactive natural products of microbial and plant origin, including amino acids, stilbenes, alkaloids, polyketides and phenylpropanoids such as flavonoids, creating natural product hybrids with altered or enhanced bioactivities. Prenylation of flavonoids enhances some of the desirable pharmacological properties of these plant compounds [1], as demonstrated for apigenin and liquiritigenin [2]. Prenylation appears in many cases to provide a higher level of bioactivity compared to the non-prenylated precursor, often by increasing affinity for biological membranes and interactions with cellular targets [3]. With the recent identification of these enzymes there is increased interest in the role of these regiospecific catalysts in expanding the diversity and bioactivities of several important classes of natural products in vivo and in vitro.
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