Protein engineering strategies for microbial production of isoprenoids
Name
1-s2.0-S2214030119300501-main.pdf
Description
Published version
Size
1.67 MB
Format
Adobe PDF
Checksum (MD5)
3917f189eb01b82ddec83fb521307bfd
Author(s)
Daletos, Georgios
Stephanopoulos, Gregory
Date Issued
2020
Journal
Metabolic Engineering Communications
Publisher
Elsevier BV
Version
Final published version
Abstract
© 2020 The Authors Isoprenoids comprise one of the most chemically diverse family of natural products with high commercial interest. The structural diversity of isoprenoids is mainly due to the modular activity of three distinct classes of enzymes, including prenyl diphosphate synthases, terpene synthases, and cytochrome P450s. The heterologous expression of these enzymes in microbial systems is suggested to be a promising sustainable way for the production of isoprenoids. Several limitations are associated with native enzymes, such as low stability, activity, and expression profiles. To address these challenges, protein engineering has been applied to improve the catalytic activity, selectivity, and substrate turnover of enzymes. In addition, the natural promiscuity and modular fashion of isoprenoid enzymes render them excellent targets for combinatorial studies and the production of new-to-nature metabolites. In this review, we discuss key individual and multienzyme level strategies for the successful implementation of enzyme engineering towards efficient microbial production of high-value isoprenoids. Challenges and future directions of protein engineering as a complementary strategy to metabolic engineering are likewise outlined.
MIT Department
Massachusetts Institute of Technology. Department of Chemical Engineering
Terms of Use
Creative Commons Attribution 4.0 International license
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1016/J.MEC.2020.E00129
