Change of product specificity of hexaprenyl diphosphate synthase from Sulfolobus solfataricus by introducing mimetic mutations.
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.
Hemmi
Hisashi
H
Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University, Aoba-yama 07, Sendai-shi, 980-8579, Miyagi-ken, Japan.
Noike
Motoyoshi
M
Nakayama
Toru
T
Nishino
Tokuzo
T
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
D019883:Alkyl and Aryl Transferases; D004122:Dimethylallyltranstransferase; C036826:trans-pentaprenyltranstransferase