Discovery of the cryptic function of terpene cyclases as aromatic prenyltransferases
| Autor: | Tiangang Liu, Takahiro Mori, Stephen A. Shinsky, Haibing He, Xin Mu, Guangkai Bian, David W. Christianson, Zixin Deng, Ikuro Abe, Minjian Huang, Corey J Herbst-Gervasoni, Anwei Hou, Shu Cheng |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular 0301 basic medicine Indoles Science Prenyltransferase education General Physics and Astronomy Prenyltransferase activity 02 engineering and technology Ligands Cyclase Article General Biochemistry Genetics and Molecular Biology Terpene 03 medical and health sciences Fusarium Prenylation Catalytic Domain Escherichia coli Intramolecular Lyases lcsh:Science X-ray crystallography Enzyme Assays chemistry.chemical_classification Multidisciplinary Terpenes Chemistry Proteins Alternaria General Chemistry Dimethylallyltranstransferase 021001 nanoscience & nanotechnology Terpenoid Enzymes Kinetics 030104 developmental biology Enzyme Biochemistry Enzyme mechanisms lcsh:Q 0210 nano-technology Function (biology) |
| Zdroj: | Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | Catalytic versatility is an inherent property of many enzymes. In nature, terpene cyclases comprise the foundation of molecular biodiversity as they generate diverse hydrocarbon scaffolds found in thousands of terpenoid natural products. Here, we report that the catalytic activity of the terpene cyclases AaTPS and FgGS can be switched from cyclase to aromatic prenyltransferase at basic pH to generate prenylindoles. The crystal structures of AaTPS and FgGS provide insights into the catalytic mechanism of this cryptic function. Moreover, aromatic prenyltransferase activity discovered in other terpene cyclases indicates that this cryptic function is broadly conserved among the greater family of terpene cyclases. We suggest that this cryptic function is chemoprotective for the cell by regulating isoprenoid diphosphate concentrations so that they are maintained below toxic thresholds. Terpene cyclases catalyze the formation of diverse hydrocarbon scaffolds found in terpenoids. Here, the authors report the cryptic function of class I terpene cyclases as aromatic prenyltransferases and the universality of this cryptic feature is confirmed using enzymes from different sources. |
| Databáze: | OpenAIRE |
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