Exploring novel bacterial terpene synthases

Terpenes are the largest class of natural products with extensive structural diversity and are widely used as pharmaceuticals, herbicides, flavourings, fragrances, and biofuels. While they have mostly been isolated from plants and fungi, the availability and analysis of bacterial genome sequence dat...

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Bibliographic Details
Published in:PloS one 2020-04, Vol.15 (4), p.e0232220-e0232220
Main Authors: Reddy, Gajendar Komati, Leferink, Nicole G H, Umemura, Maiko, Ahmed, Syed T, Breitling, Rainer, Scrutton, Nigel S, Takano, Eriko
Format: Article
Language:English
Subjects:
Bacteria
Biofuels
Biology and Life Sciences
Biotechnology
Chemistry
Diterpenes
E coli
Enzymes
Flavorings
Fragrances
Fungi
Genes
Genomes
Herbicides
Medicine and Health Sciences
Natural products
Nucleotide sequence
Physical Sciences
Research and Analysis Methods
Substrates
Synthetic biology
Terpene synthase
Terpenes
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Summary:Terpenes are the largest class of natural products with extensive structural diversity and are widely used as pharmaceuticals, herbicides, flavourings, fragrances, and biofuels. While they have mostly been isolated from plants and fungi, the availability and analysis of bacterial genome sequence data indicates that bacteria also possess many putative terpene synthase genes. In this study, we further explore this potential for terpene synthase activity in bacteria. Twenty two potential class I terpene synthase genes (TSs) were selected to represent the full sequence diversity of bacterial synthase candidates and recombinantly expressed in E. coli. Terpene synthase activity was detected for 15 of these enzymes, and included mono-, sesqui- and diterpene synthase activities. A number of confirmed sesquiterpene synthases also exhibited promiscuous monoterpene synthase activity, suggesting that bacteria are potentially a richer source of monoterpene synthase activity then previously assumed. Several terpenoid products not previously detected in bacteria were identified, including aromandendrene, acora-3,7(14)-diene and longiborneol. Overall, we have identified promiscuous terpene synthases in bacteria and demonstrated that terpene synthases with substrate promiscuity are widely distributed in nature, forming a rich resource for engineering terpene biosynthetic pathways for biotechnology.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0232220