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|dc.description.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.|
|dc.publisher||Royal Society of Chemistry (RSC)|
|dc.rights||This Open Access Article is licensed under a Creative Commons Attribution-Non Commercial 3.0 Unported Licence|
|dc.title||Crystal structure and functional analysis of large-terpene synthases belonging to a newly found subclass|
|Appears in Collections:||Journal Articles|
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