Substrate specificities of farnesyl diphosphate synthases from Bacillus stearothermophilus and porcine liver with cyclic substrate homologs

Masahiko Nagaki, Hiroshi Kanno, Tohru Musashi, Rie Shimizu, Yuji Maki, Hiroshi Sagami, Tanetoshi Koyama

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

We investigated the substrate specificity of farnesyl diphosphate (FPP) synthase derived from Bacillus stearothermophilus and porcine liver by examining the reactivities of two cyclic substrate homologs, cyclohexylideneethyl diphosphate and cyclohexenylethyl diphosphate. Reaction of geranyl diphosphate with 2-cyclohexenylethyl diphosphate using bacterial or porcine liver FPP synthase produced (S)-geranylcyclohexylideneethyl diphosphate, with relative yields of 13.6% for the bacterial enzyme and 42.2% for the porcine liver enzyme. Reaction of cyclohexylideneethyl diphosphate with isopentenyl diphosphate produced 10-cyclohexyliden-3,7-dimethyldeca-2,6-dien-1-ol as a double condensation product, with relative yields of 23.1% (bacterial enzyme) and 3.0% (porcine liver enzyme). Reaction of cyclohexylideneethyl diphosphate with 2-cyclohexenylethyl diphosphate using bacterial enzyme produced (cyclohexylideneethyl)-cyclohexylideneethyl diphosphate (0.8% yield).

Original languageEnglish
Pages (from-to)186-190
Number of pages5
JournalJournal of Molecular Catalysis B: Enzymatic
Volume60
Issue number3-4
DOIs
Publication statusPublished - 2009 Oct 1

Keywords

  • 2-Cyclohexenylethyl diphosphate
  • Bacillus stearothermophilus
  • Cyclohexylideneethyl diphosphate
  • Farnesyl diphosphate synthase
  • Substrate specificity

ASJC Scopus subject areas

  • Catalysis
  • Bioengineering
  • Biochemistry
  • Process Chemistry and Technology

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