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TitleDiscovery of non-squalene triterpenes.
Journal, issue, pagesNature, Vol. 606, Issue 7913, Page 414-419, Year 2022
Publish dateJun 1, 2022
AuthorsHui 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 AbstractAll 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.
External linksNature / PubMed:35650436 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2 - 4.0 Å
Structure data

32531

7wij

EMDB-32531: Cryo-EM structure of prenyltransferase domain of Macrophoma phaseolina macrophomene synthase at 3.17 angstrom resolution
PDB-7wij: Cryo-EM structure of prenyltransferase domain of Macrophoma phaseolina macrophomene synthase
Method: EM (single particle) / Resolution: 3.17 Å

EMDB-32532: Cryo-EM structure of cross-linked Macrophomina phaseolina macrophomene synthase at 4.0 angstrom resolution
Method: EM (single particle) / Resolution: 4.0 Å

PDB-7vta:
Talaromyces verruculosus talaropentaene synthase apo
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-7vtb:
Partially closed conformation of talaropentaene synthase cyclase domain
Method: X-RAY DIFFRACTION / Resolution: 2.0 Å

Chemicals

ChemComp-HOH:
WATER / Water

ChemComp-NI:
NICKEL (II) ION / Nickel

Source
  • macrophomina phaseolina ms6 (fungus)
  • talaromyces verruculosus (fungus)
KeywordsTRANSFERASE / Talaromyces verruculosus / talaropentaene synthase / triterpene / Macrophoma phaseolina / Macrophomene Synthase / prenyltransferase

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