Change of product specificity of hexaprenyl diphosphate synthase from Sulfolobus solfataricus by introducing mimetic mutations

Biochem Biophys Res Commun. 2002 Oct 11;297(5):1096-101. doi: 10.1016/s0006-291x(02)02348-3.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkyl and Aryl Transferases / genetics
  • Alkyl and Aryl Transferases / metabolism*
  • Amino Acid Sequence
  • Binding Sites
  • Chromatography, Thin Layer
  • Dimerization
  • Dimethylallyltranstransferase / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Evolution, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Mutation*
  • Plasmids / metabolism
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Sulfolobus / enzymology*
  • Sulfolobus / genetics
  • Temperature


  • Alkyl and Aryl Transferases
  • Dimethylallyltranstransferase
  • trans-pentaprenyltranstransferase