prenyltransferaseslike

Prenyltransferases are a group of enzymes that catalyze the transfer of prenyl groups, such as isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP), to various acceptor molecules. These enzymes play crucial roles in the biosynthesis of a wide array of natural products, including terpenes, terpenoids, and prenylated secondary metabolites. The prenyl group is a five-carbon branched chain isoprenoid unit, and its addition to other molecules often modifies their lipophilicity, stability, and biological activity.

There are several classes of prenyltransferases, distinguished by the specific prenyl donor and acceptor molecules they utilize. For instance, geranylgeranyl pyrophosphate synthases (GGPPS) elongate the prenyl chain to a C20 unit, while farnesyl pyrophosphate synthases (FPPS) produce a C15 unit. These enzymes are involved in the synthesis of essential molecules like carotenoids, sterols, and dolichols. Other prenyltransferases target proteins, attaching prenyl groups to specific amino acid residues, a process known as protein prenylation, which is vital for membrane localization and protein function.

The study of prenyltransferases is important for understanding metabolic pathways in plants, fungi, bacteria, and animals. Their involvement in producing compounds with pharmacological properties, such as anticancer drugs and antibiotics, also makes them targets for drug discovery and biotechnological applications. Modifying prenyltransferase activity can lead to the production of novel compounds or the increased yield of existing ones.