Bioinformatics-aided identification, characterization and applications of mushroom linalool synthases
| Autor: | Rehka T, Sebastian Maurer-Stroh, Martin Rühl, Xixian Chen, Congqiang Zhang, Raphael T.C. Lee |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
QH301-705.5 Protein Conformation Acyclic Monoterpenes Medicine (miscellaneous) medicine.disease_cause Industrial microbiology Biosynthesis 01 natural sciences General Biochemistry Genetics and Molecular Biology Article Metabolic engineering Evolution Molecular Fungal Proteins 03 medical and health sciences chemistry.chemical_compound Structure-Activity Relationship Linalool medicine Biology (General) Agrocybe pediades Escherichia coli Hydro-Lyases Phylogeny Nerolidol chemistry.chemical_classification biology 010405 organic chemistry Computational Biology biology.organism_classification Bioproduction 0104 chemical sciences Kinetics 030104 developmental biology Enzyme chemistry Biochemistry Biocatalysis General Agricultural and Biological Sciences Agaricales |
| Zdroj: | Communications Biology Communications Biology, Vol 4, Iss 1, Pp 1-11 (2021) |
| ISSN: | 2399-3642 |
| Popis: | Enzymes empower chemical industries and are the keystone for metabolic engineering. For example, linalool synthases are indispensable for the biosynthesis of linalool, an important fragrance used in 60–80% cosmetic and personal care products. However, plant linalool synthases have low activities while expressed in microbes. Aided by bioinformatics analysis, four linalool/nerolidol synthases (LNSs) from various Agaricomycetes were accurately predicted and validated experimentally. Furthermore, we discovered a linalool synthase (Ap.LS) with exceptionally high levels of selectivity and activity from Agrocybe pediades, ideal for linalool bioproduction. It effectively converted glucose into enantiopure (R)-linalool in Escherichia coli, 44-fold and 287-fold more efficient than its bacterial and plant counterparts, respectively. Phylogenetic analysis indicated the divergent evolution paths for plant, bacterial and fungal linalool synthases. More critically, structural comparison provided catalytic insights into Ap.LS superior specificity and activity, and mutational experiments validated the key residues responsible for the specificity. Zhang et al. identified four linalool/nerolidol synthases from fungi using bioinformatics and phylogenetic analysis and validated their functions with in vitro and in vivo methods. One of them is a rare and highly specific monoterpene synthase and responsible for impressive titres of the commercially sought-after fragrance (R)-linalool. |
| Databáze: | OpenAIRE |
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