title: Chain-length determination mechanism of isoprenyl diphosphate synthases and implications for molecular evolution.
abstract: In the synthesis of isoprenoids, isoprenyl diphosphate synthases catalyze the consecutive condensation of isopentenyl diphosphate with allylic diphosphates to produce a variety of prenyl diphosphates with well-defined chain lengths. Site-directed mutagenesis in conjunction with X-ray crystallographic studies have identified specific amino acid residues responsible for chain-length determination. Simple combinations of these residues within a characteristic motif are not only sufficient to confer product specificities to all isoprenyl diphosphate synthases but represent structural features that reflect the enzyme family's evolutionary course.
authors.affiliation: University of California San Francisco, School of Medicine, S 245, Box 0454, San Francisco, CA 94143, USA.
authors.forename: K
authors.initials: K
authors.lastname: Wang
authors.forename: S
authors.initials: S
authors.lastname: Ohnuma
mesh_terms: D019883:Alkyl and Aryl Transferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence / Q000235:genetics; D019143:Evolution, Molecular; D051231:Farnesyltranstransferase; D014644:Genetic Variation / Q000235:genetics; D006801:Humans; D008970:Molecular Weight; D010802:Phylogeny; D011487:Protein Conformation
chemical_list: D019883:Alkyl and Aryl Transferases; D051231:Farnesyltranstransferase