2018年4月21日
Crystal structure and functional analysis of large-terpene synthases belonging to a newly found subclass.
Chemical science
- 巻
- 9
- 号
- 15
- 開始ページ
- 3754
- 終了ページ
- 3758
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1039/c8sc00289d
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.
- リンク情報
- ID情報
-
- DOI : 10.1039/c8sc00289d
- ISSN : 2041-6520
- PubMed ID : 29780507
- PubMed Central 記事ID : PMC5939612