title: Change of product specificity of hexaprenyl diphosphate synthase from Sulfolobus solfataricus by introducing mimetic mutations.
abstract: The introduction of several sets of amino acid substitutions into the region around a substrate-binding site of a medium-chain (all-E) prenyl diphosphate synthase, hexaprenyl diphosphate synthase from a thermoacidophilic archaeon Sulfolobus solfataricus, to mimic the product determination mechanisms of various kinds of short-chain enzymes revealed that the structure around the region of the medium-chain enzyme resembles those of eukaryotic farnesyl diphosphate synthases but not those of the other short-chain enzymes, reflecting the evolutional relationships among these enzymes.
authors.affiliation: Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University, Aoba-yama 07, Sendai-shi, 980-8579, Miyagi-ken, Japan.
authors.forename: Hisashi
authors.initials: H
authors.lastname: Hemmi
authors.forename: Motoyoshi
authors.initials: M
authors.lastname: Noike
authors.forename: Toru
authors.initials: T
authors.lastname: Nakayama
authors.forename: Tokuzo
authors.initials: T
authors.lastname: Nishino
mesh_terms: D019883:Alkyl and Aryl Transferases / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D001665:Binding Sites; D002855:Chromatography, Thin Layer; D019281:Dimerization; D004122:Dimethylallyltranstransferase / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D019143:Evolution, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D010957:Plasmids / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D016944:Sulfolobus / Q000201:enzymology* / Q000235:genetics; D013696:Temperature
chemical_list: D019883:Alkyl and Aryl Transferases; D004122:Dimethylallyltranstransferase; C036826:trans-pentaprenyltranstransferase