Cloning and functional analysis of novel short-chain cis-prenyltransferases

Takanori Ambo, Motoyoshi Noike, Hirofumi Kurokawa, Tanetoshi Koyama

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

cis-Prenyltransferase catalyzes the synthesis of Z,E-mixed prenyl diphosphates by sequential condensation of isopentenyl diphosphate with allylic diphosphate. cis-Prenyltransferases can be classified into three subgroups: short-, medium-, and long-chain cis-prenyltransferase, according to their product chain lengths. cis-Farnesyl diphosphate synthase from Mycobacterium tuberculosis has been the only example as short-chain cis-prenyltransferase so far characterized. In this study, we cloned the novel short-chain cis-prenyltransferases from three different bacteria, and characterized their enzymatic activities to compare and elucidate a common feature of the short-chain cis-prenyltransferases. Furthermore, we identified a specific isoleucine that is conserved in short-chain cis-prenyltransferases and located in close proximity of the ω-end of the geranyl diphosphate. Several site-directed mutants with respect to the isoleucine residue synthesized longer prenyl chain products and showed broader allylic substrate specificity. These results suggested that the isoleucine plays an important role in the substrate specificity and chain length determination mechanism of cis-prenyltransferase. Crown

Original languageEnglish
Pages (from-to)536-540
Number of pages5
JournalBiochemical and biophysical research communications
Volume375
Issue number4
DOIs
Publication statusPublished - 2008 Oct 31

Keywords

  • Chain-length determination
  • Prenyltransferase
  • Substrate specificity
  • cis-Farnesyl diphosphate synthase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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