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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.date.accessioned2018-05-17T05:28:25Z-
dc.date.available2018-05-17T05:28:25Z-
dc.date.issued2018-04-21
dc.identifier.issn2041-6520
dc.identifier.urihttp://hdl.handle.net/2433/231116-
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.format.mimetypeapplication/pdf
dc.language.isoeng
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
dc.identifier.volume9
dc.identifier.issue15
dc.identifier.spage3754
dc.identifier.epage3758
dc.relation.doi10.1039/C8SC00289D
dc.textversionpublisher
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