Structure and Function of a “Head‐to‐Middle” Prenyltransferase: Lavandulyl Diphosphate Synthase |
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| Authors: | Meixia Liu Prof. Dr. Chun‐Chi Chen Lu Chen Xiansha Xiao Prof. Dr. Yingying Zheng Dr. Jian‐Wen Huang Prof. Dr. Weidong Liu Dr. Tzu‐Ping Ko Ya‐Shan Cheng Dr. Xinxin Feng Prof. Dr. Eric Oldfield Prof. Dr. Rey‐Ting Guo Prof. Dr. Yanhe Ma |
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| Affiliation: | 1. College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China;2. Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, China;3. Department of Biochemistry, University of Illinois, Urbana, IL, USA;4. AsiaPac Biotechnology Co., Ltd., Dongguan, China;5. Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan;6. Department of Chemistry, University of Illinois, Urbana, IL, USA |
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| Abstract: | We report the first X‐ray structure of the unique “head‐to‐middle” monoterpene synthase, lavandulyl diphosphate synthase (LPPS). LPPS catalyzes the condensation of two molecules of dimethylallyl diphosphate (DMAPP) to form lavandulyl diphosphate, a precursor to the fragrance lavandulol. The structure is similar to that of the bacterial cis‐prenyl synthase, undecaprenyl diphosphate synthase (UPPS), and contains an allylic site (S1) in which DMAPP ionizes and a second site (S2) which houses the DMAPP nucleophile. Both S‐thiolo‐dimethylallyl diphosphate and S‐thiolo‐isopentenyl diphosphate bind intact to S2, but are cleaved to (thio)diphosphate, in S1. His78 (Asn in UPPS) is essential for catalysis and is proposed to facilitate diphosphate release in S1, while the P1 phosphate in S2 abstracts a proton from the lavandulyl carbocation to form the LPP product. The results are of interest since they provide the first structure and structure‐based mechanism of this unusual prenyl synthase. |
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| Keywords: | biosynthesis fragrance monoterpenes natural products structure elucidation |
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