Insights into taxadiene synthase catalysis and promiscuity facilitated by mutability landscape and molecular dynamics.

ABSTRACT:

Main conclusion

Protein modeling, carbocation docking, and molecular dynamics along with structure-based mutability landscapes provided insight into taxadiene synthase catalysis (first step of the anticancer Taxol biosynthesis), protein structure-function correlations, and promiscuity. Plant terpenes belong to one of the largest and most diverse classes of natural products. This diversity is driven by the terpene synthase enzyme family which comprises numerous different synthases, several of which are promiscuous. Taxadiene synthase (TXS) is a class I diterpene synthase that catalyzes the first step in the biosynthesis pathway of the diterpene Taxol, an anticancer natural product produced by the Taxus plant. Exploring the molecular basis of TXS catalysis and its promiscuous potenti

SUBMITTER: He S 

PROVIDER: S-EPMC10924717 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature