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Farnesyl diphosphate synthase; regulation of product specificity Szkopinska A; Plochocka DActa Biochim Pol 2005[]; 52 (1): 45-55Farnesyl diphosphate synthase (FPPS) is a key enzyme in isoprenoid biosynthesis which supplies sesquiterpene precursors for several classes of essential metabolites including sterols, dolichols, ubiquinones and carotenoids as well as substrates for farnesylation and geranylgeranylation of proteins. It catalyzes the sequential head-to-tail condensation of two molecules of isopentenyl diphosphate with dimethylallyl diphosphate. The enzyme is a homodimer of subunits, typically having two aspartate-rich motifs with two sets of substrate binding sites for an allylic diphosphate and isopentenyl diphosphate per homodimer. The synthase amino-acid residues at the 4th and 5th positions before the first aspartate rich motif mainly determine product specificity. Hypothetically, type I (eukaryotic) and type II (eubacterial) FPPSs evolved from archeal geranylgeranyl diphosphate synthase by substitutions in the chain length determination region. FPPS belongs to enzymes encoded by gene families. In plants this offers the possibility of differential regulation in response to environmental changes or to herbivore or pathogen attack.|Alkyl and Aryl Transferases/chemistry/*metabolism[MESH]|Amino Acid Sequence[MESH]|Arginine/metabolism[MESH]|Dimerization[MESH]|Geranyltranstransferase[MESH]|Lysine/metabolism[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Sequence Homology, Amino Acid[MESH]|Substrate Specificity[MESH] |
