prenyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the transfer of a prenyl group from one compound (donor) to another (acceptor). [GOC:mah]

Prenyltransferases are a diverse family of enzymes that catalyze the transfer of isoprenoid units from prenyl diphosphate donors to a wide variety of acceptor molecules. These reactions are essential for the biosynthesis of a vast array of biologically important molecules, including sterols, ubiquinones, dolichols, and many secondary metabolites. The isoprenoid units transferred by prenyltransferases are typically isopentenyl diphosphate (IPP) or dimethylallyl diphosphate (DMAPP), which are derived from the mevalonate pathway or the methylerythritol 4-phosphate (MEP) pathway. Prenyltransferases employ a two-step reaction mechanism: first, the prenyl diphosphate donor binds to the enzyme, followed by the binding of the acceptor molecule. The enzyme then catalyzes the transfer of the isoprenoid unit from the donor to the acceptor molecule, generating a new prenylated product. The prenyltransferases exhibit a wide range of substrate specificity, which is determined by the specific amino acid residues in the active site of the enzyme. The diversity of prenyltransferases and their substrate specificities reflect the wide range of prenylated molecules that are essential for cellular function.'
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Proteins (2)

Compounds (13)