Substrate specificities of wild- and mutated-type farnesyl diphosphate synthases with artificial substrate homologs

  • Nagaki Masahiko
    Graduate School of Science and Technology, Hirosaki University
  • Miyata Kazuhiko
    Graduate School of Science and Technology, Hirosaki University
  • Kawakami Jun
    Graduate School of Science and Technology, Hirosaki University
  • Miyamoto Ryo
    Graduate School of Science and Technology, Hirosaki University
  • Maki Yuji
    Department of Material and Biological Chemistry, Faculty of Science, Yamagata University
  • Sagami Hiroshi
    Institute of Multidisciplinary Research for Advanced Materials, Tohoku University
  • Koyama Tanetoshi
    Institute of Multidisciplinary Research for Advanced Materials, Tohoku University

抄録

6,7-Epoxygeranyl diphosphate was examined for reactivity as an allylic substrate of wild and mutated farnesyl diphosphate (FPP) synthases of Bacillus stearothermophilus. 6,7-Epoxygeranyl diphosphate was accepted by wild and mutated (Y81R, Y81D, and Y81S) farnesyl diphosphate synthases as a substrate in reaction with isopentenyl diphosphate, yielding 10,11-epoxyfarnesyl and 14,15-epoxygeranylgeranyl diphosphates, respectively.

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