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dc.contributor.authorFujihashi, Masahiro
dc.contributor.authorSato, Tsutomu
dc.contributor.authorTanaka, Yuma
dc.contributor.authorYamamoto, Daisuke
dc.contributor.authorNishi, Tomoyuki
dc.contributor.authorUeda, Daijiro
dc.contributor.authorMurakami, Mizuki
dc.contributor.authorYasuno, Yoko
dc.contributor.authorSekihara, Ai
dc.contributor.authorFuku, Kazuma
dc.contributor.authorShinada, Tetsuro
dc.contributor.authorMiki, Kunio
dc.contributor.alternative藤橋 雅宏
dc.contributor.alternative三木, 邦夫
dc.description.abstractThousands 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.
dc.publisherRoyal Society of Chemistry (RSC)
dc.rightsThis Open Access Article is licensed under a Creative Commons Attribution-Non Commercial 3.0 Unported Licence
dc.titleCrystal structure and functional analysis of large-terpene synthases belonging to a newly found subclass
dc.type.niitypeJournal Article
dc.identifier.jtitleChemical Science
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