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Title: Crystal structure and functional analysis of large-terpene synthases belonging to a newly found subclass
Authors: Fujihashi, Masahiro  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-6882-9697 (unconfirmed)
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
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