Abstract
Cooperation between 6-m-r hemiketalization and 26-m-r macrolactonization is reported for a thioesterase (pimTE) in type-I polyketide synthase. Intriguingly, the R-hemiketal intermediate is not only catalyzed by the D179 residue, but also twists the substrate hairpin structure to the 26-m-r lactonizing pre-reaction state. Thus, pimTE is believed to be a bifunctional enzyme, which can synergistically catalyze tandem 6-m-r and 26-m-r formations during the main-chain release of pimaricin biosynthesis. More information on this study can be found in the Research Article by Linquan Bai, Yi-Lei Zhao et al.
Published Version (Free)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have