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Title: | Crystal structure and functional analysis of large-terpene synthases belonging to a newly found subclass |
Authors: | Fujihashi, Masahiro ![]() Sato, Tsutomu Tanaka, Yuma Yamamoto, Daisuke Nishi, Tomoyuki Ueda, Daijiro Murakami, Mizuki Yasuno, Yoko Sekihara, Ai Fuku, Kazuma Shinada, Tetsuro Miki, Kunio |
Author's alias: | 藤橋 雅宏 三木, 邦夫 |
Issue Date: | 21-Apr-2018 |
Publisher: | Royal Society of Chemistry (RSC) |
Journal title: | Chemical Science |
Volume: | 9 |
Issue: | 15 |
Start page: | 3754 |
End page: | 3758 |
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. |
Rights: | This Open Access Article is licensed under a Creative Commons Attribution-Non Commercial 3.0 Unported Licence |
URI: | http://hdl.handle.net/2433/231116 |
DOI(Published Version): | 10.1039/C8SC00289D |
PubMed ID: | 29780507 |
Appears in Collections: | Journal Articles |

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