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-Structure paper
タイトル | Discovery of non-squalene triterpenes. |
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ジャーナル・号・ページ | Nature, Vol. 606, Issue 7913, Page 414-419, Year 2022 |
掲載日 | 2022年6月1日 |
著者 | Hui Tao / Lukas Lauterbach / Guangkai Bian / Rong Chen / Anwei Hou / Takahiro Mori / Shu Cheng / Ben Hu / Li Lu / Xin Mu / Min Li / Naruhiko Adachi / Masato Kawasaki / Toshio Moriya / Toshiya Senda / Xinghuan Wang / Zixin Deng / Ikuro Abe / Jeroen S Dickschat / Tiangang Liu / |
PubMed 要旨 | All known triterpenes are generated by triterpene synthases (TrTSs) from squalene or oxidosqualene. This approach is fundamentally different from the biosynthesis of short-chain (C-C) terpenes that ...All known triterpenes are generated by triterpene synthases (TrTSs) from squalene or oxidosqualene. This approach is fundamentally different from the biosynthesis of short-chain (C-C) terpenes that are formed from polyisoprenyl diphosphates. In this study, two fungal chimeric class I TrTSs, Talaromyces verruculosus talaropentaene synthase (TvTS) and Macrophomina phaseolina macrophomene synthase (MpMS), were characterized. Both enzymes use dimethylallyl diphosphate and isopentenyl diphosphate or hexaprenyl diphosphate as substrates, representing the first examples, to our knowledge, of non-squalene-dependent triterpene biosynthesis. The cyclization mechanisms of TvTS and MpMS and the absolute configurations of their products were investigated in isotopic labelling experiments. Structural analyses of the terpene cyclase domain of TvTS and full-length MpMS provide detailed insights into their catalytic mechanisms. An AlphaFold2-based screening platform was developed to mine a third TrTS, Colletotrichum gloeosporioides colleterpenol synthase (CgCS). Our findings identify a new enzymatic mechanism for the biosynthesis of triterpenes and enhance understanding of terpene biosynthesis in nature. |
リンク | Nature / PubMed:35650436 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 2 - 4.0 Å |
構造データ | EMDB-32531: Cryo-EM structure of prenyltransferase domain of Macrophoma phaseolina macrophomene synthase at 3.17 angstrom resolution EMDB-32532: Cryo-EM structure of cross-linked Macrophomina phaseolina macrophomene synthase at 4.0 angstrom resolution PDB-7vta: PDB-7vtb: |
化合物 | ChemComp-HOH: ChemComp-NI: |
由来 |
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キーワード | TRANSFERASE (転移酵素) / Talaromyces verruculosus / talaropentaene synthase / triterpene / Macrophoma phaseolina / Macrophomene Synthase / prenyltransferase (プレニル基転移酵素) |