Jump to main content
Jump to site search

Issue 15, 2018
Previous Article Next Article

Crystal structure and functional analysis of large-terpene synthases belonging to a newly found subclass

Author affiliations

Abstract

Thousands of terpenes have been identified to date. However, only two classes of enzymes are known to be involved in their biosynthesis, and each class has characteristic amino-acid motifs. We recently identified a novel large-terpene (C25/C30/C35) synthase, which shares no motifs with known enzymes. To elucidate the molecular mechanism of this enzyme, we determined the crystal structure of a large-β-prene synthase from B. alcalophilus (BalTS). Surprisingly, the overall structure of BalTS is similar to that of the α-domain of class I terpene synthases although their primary structures are totally different from each other. Two novel aspartate-rich motifs, DYLDNLxD and DY(F,L,W)IDxxED, are identified, and mutations of any one of the aspartates eliminate its enzymatic activity. The present work leads us to propose a new subclass of terpene synthases, class IB, which is probably responsible for large-terpene biosynthesis.

Graphical abstract: Crystal structure and functional analysis of large-terpene synthases belonging to a newly found subclass

Back to tab navigation

Supplementary files

Publication details

The article was received on 18 Jan 2018, accepted on 15 Mar 2018 and first published on 16 Mar 2018


Article type: Edge Article
DOI: 10.1039/C8SC00289D
Citation: Chem. Sci., 2018,9, 3754-3758
  • Open access: Creative Commons BY-NC license
  •   Request permissions

    Crystal structure and functional analysis of large-terpene synthases belonging to a newly found subclass

    M. Fujihashi, T. Sato, Y. Tanaka, D. Yamamoto, T. Nishi, D. Ueda, M. Murakami, Y. Yasuno, A. Sekihara, K. Fuku, T. Shinada and K. Miki, Chem. Sci., 2018, 9, 3754
    DOI: 10.1039/C8SC00289D

    This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material and it is not used for commercial purposes.

    Reproduced material should be attributed as follows:

    • For reproduction of material from NJC:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
    • For reproduction of material from PCCP:
      [Original citation] - Published by the PCCP Owner Societies.
    • For reproduction of material from PPS:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
    • For reproduction of material from all other RSC journals:
      [Original citation] - Published by The Royal Society of Chemistry.

    Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.

Search articles by author

Spotlight

Advertisements