Substrate specificities of farnesyl diphosphate synthases with respect to cyclic substrate homologs

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  • Musashi Tohru
    Graduate School of Science and Technology, Hirosaki University
  • Kanno Hiroshi
    Graduate School of Science and Technology, Hirosaki University
  • Kawakami Jun
    Graduate School of Science and Technology, Hirosaki University
  • Yokota Saki
    Department of Material and Biological Chemistry, Faculty of Science, Yamagata University
  • Ohya Norimasa
    Department of Material and Biological Chemistry, Faculty of Science, Yamagata University
  • Nagaki Masahiko
    Graduate School of Science and Technology, Hirosaki University

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We investigated substrate specificities of farnesyl diphosphate synthases (FPSs) derived from porcine liver and Bacillus stearothermophilus by examining the reactivity of cyclopentylideneethyl diphosphate with several 3-alkyl homologs of isopentenyl diphosphate. Reaction of cyclopentylideneethyl diphosphate with isopentenyl diphosphate using porcine liver or bacterial enzyme gave 10-cyclopentyliden-3,7-dimethyldeca-2,6-dinenyl diphosphate as a double condensation product, with relative yields of 40.9% for the porcine liver enzyme and 15.9% for the bacterial enzyme. Reaction of cyclohexlideneethyl diphosphate with 3-ethylbut-3-enyl diphosphate using the bacterial enzyme gave 10-cyclohexliden-3,7-diethyldeca-2,6-dinenyl diphosphate (yield: 24.6%).

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