Structure and Function of a "Head-to-Middle" Prenyltransferase: Lavandulyl Diphosphate Synthase.

作者: Meixia Liu , Chun-Chi Chen , Lu Chen , Xiansha Xiao , Yingying Zheng

DOI: 10.1002/ANIE.201600656

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摘要: We report the first X-ray structure of unique "head-to-middle" monoterpene synthase, lavandulyl diphosphate synthase (LPPS). LPPS catalyzes condensation two molecules dimethylallyl (DMAPP) to form diphosphate, a precursor fragrance lavandulol. The is similar that bacterial cis-prenyl undecaprenyl (UPPS), and contains an allylic site (S1) in which DMAPP ionizes second (S2) houses nucleophile. Both S-thiolo-dimethylallyl S-thiolo-isopentenyl bind intact S2, but are cleaved (thio)diphosphate, S1. His78 (Asn UPPS) essential for catalysis proposed facilitate release S1, while P1 phosphate S2 abstracts proton from carbocation LPP product. results interest since they provide structure-based mechanism this unusual prenyl synthase.

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