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- W3204351412 abstract "Abstract Pimarane-type diterpenoids are widely distributed in all domains of life, but no structures or catalytic mechanisms of pimarane-type diterpene synthases (DTSs) have been characterized. Here, we report that two class I DTSs, Sat1646 and Stt4548, each accept copalyl diphosphate (CPP) as the substrate to produce isopimara-8,15-diene ( 1 ). Sat1646 can also accept syn -CPP and produce syn -isopimaradiene/pimaradiene analogues ( 2 – 7 ), among which 2 possesses a previously unreported 6/6/7 ring skeleton. We solve the crystal structures of Sat1646, Sat1646 complexed with magnesium ions, and Stt4548, thereby revealing the active sites of these pimarane-type DTSs. Substrate modeling and subsequent site-directed mutagenesis experiments demonstrate different structural bases of Sat1646 and Stt4548 for 1 production. Comparisons with previously reported DTSs reveal their distinct carbocation intermediate stabilization mechanisms, which control the conversion of a single substrate CPP into structurally diverse diterpene products. These results illustrate the structural bases for enzymatic catalyses of pimarane-type DTSs, potentially facilitating future DTS engineering and combinatorial biosynthesis." @default.
- W3204351412 created "2021-10-11" @default.
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- W3204351412 date "2021-09-30" @default.
- W3204351412 modified "2023-10-10" @default.
- W3204351412 title "Functional characterization and structural bases of two class I diterpene synthases in pimarane-type diterpene biosynthesis" @default.
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- W3204351412 doi "https://doi.org/10.1038/s42004-021-00578-z" @default.
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