4.7 Article

syn-Elimination of glutamylated threonine in lanthipeptide biosynthesis

Journal

CHEMICAL COMMUNICATIONS
Volume 59, Issue 9, Pages 1165-1168

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/d2cc06345j

Keywords

-

Ask authors/readers for more resources

This report demonstrates that the biosynthesis of lanthipeptides containing the d-allo-l-MeLan macrocycle proceeds through (E)-Dhb intermediates formed by net syn-elimination of l-Thr.
Methyllanthionine (MeLan) containing macrocycles are key structural features of lanthipeptides. They are formed typically by anti-elimination of l-Thr residues followed by cyclization of l-Cys residues onto the (Z)-dehydrobutyrine (Dhb) intermediates. In this report we demonstrate that the biosynthesis of lanthipeptides containing the d-allo-l-MeLan macrocycle such as the morphogenetic lanthipeptide SapT proceeds through (E)-Dhb intermediates formed by net syn-elimination of l-Thr.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available