Efficient production of oxidized terpenoids via engineering fusion proteins of terpene synthase and cytochrome P450.

ABSTRACT: The functionalization of terpenes using cytochrome P450 enzymes is a versatile route to the production of useful derivatives that can be further converted to value-added products. Many terpenes are hydrophobic and volatile making their availability as a substrate for P450 enzymes significantly limited during microbial production. In this study, we developed a strategy to improve the accessibility of terpene molecules for the P450 reaction by linking terpene synthase and P450 together. As a model system, fusion proteins of 1,8-cineole synthase (CS) and P450_cin were investigated and it showed an improved hydroxylation of the monoterpenoid 1,8-cineole up to 5.4-fold. Structural analysis of the CS-P450_cin fusion proteins by SEC-SAXS indicated a dimer formation with prefer

SUBMITTER: Wang X 

PROVIDER: S-EPMC7987753 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature