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Engineering amino acid residues of pentacyclic triterpene synthases for improving the activity.
- Source :
-
Applied Microbiology & Biotechnology . 2024, Vol. 108 Issue 1, p1-13. 13p. - Publication Year :
- 2024
-
Abstract
- Pentacyclic triterpenoids exhibit a wide range of biological activities which have wide applications in the food, cosmetics, and pharmaceutical industries. High-performance chassis strains have been developed for the production of various pentacyclic triterpenoids, e.g., lupane-type and oleanane-type triterpenoids. The production of common pentacyclic triterpenes and their derivatives is limited by the poor activity of typical pentacyclic triterpene synthases (PTSs). However, a general strategy applicable to typical PTSs is still lacking. As typical pentacyclic triterpenes are derived from the baccharenyl cation, engineering the non-active-site residues in the MXXXXR motif might be beneficial for the catalytic efficiencies of typical PTSs by the stabilization of the baccharenyl cation. Here, we develop a general strategy for improving the activity of typical PTSs. As a proof of concept, the activity of three PTSs such as lupeol synthase, β-amyrin synthase, and α-amyrin synthases was significantly increased up to 7.3-fold by site-directed saturation mutagenesis. This strategy could be applied to improve the activity of various typical PTSs. Key points: • The strategy could be applied to typical PTSs for improving the activity. • The catalytic activity of typical PTSs was significantly increased. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 01757598
- Volume :
- 108
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Applied Microbiology & Biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 175316007
- Full Text :
- https://doi.org/10.1007/s00253-024-13030-8