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

• 藤橋 雅宏

• 三木, 邦夫

• Tanaka, Yuma

• Yamamoto, Daisuke

• Nishi, Tomoyuki

• Ueda, Daijiro

• Murakami, Mizuki

• Yasuno, Yoko

• Sekihara, Ai

• Fuku, Kazuma

• Shinada, Tetsuro

• Miki, Kunio

抄録

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.

収録刊行物

• Chemical Science

  Chemical Science 9 (15), 3754-3758, 2018-04-21

  Royal Society of Chemistry (RSC)

キーワード

• General Chemistry

詳細情報

• CRID: 1050564285810964736
• NII論文ID: 120006466632
• ISSN: 20416520
• ISSN: 20416539
• DOI: 10.1039/c8sc00289d
• HANDLE: 2433/231116
• Web Site: http://pubs.rsc.org/en/content/articlepdf/2018/SC/C8SC00289D
• 本文言語コード: en
• 資料種別: journal article
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