Related Experiment Video
Updated: Jun 15, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Insights into heterocyclization from two highly similar enzymes
John A McIntosh1, Mohamed S Donia, Eric W Schmidt
1Department of Medicinal Chemistry, University of Utah, Salt Lake City, Utah 84112, USA.
None:
The cyanobactin biosynthetic pathways pat and tru, isolated from metagenomes of marine animals, lead to diverse natural products containing heterocycles derived from Cys, Ser, and Thr. Previous work has shown that PatD and TruD are extremely broad-substrate heterocyclase enzymes. These enzymes are virtually identical in their N-terminal putative catalytic domains, but only approximately 77% identical in their C-terminal putative substrate-binding domains. Here, we show that these differences allow the enzymes to control regioselectivity of posttranslational modifications, helping to control product chemistry in this hypervariable family of marine natural products.
More Related Videos
10:17Efficient Construction of Drug-like Bispirocyclic Scaffolds Via Organocatalytic Cycloadditions of α-Imino γ-Lactones and Alkylidene Pyrazolones
Published on: February 7, 2019
08:25Development of Heterogeneous Enantioselective Catalysts using Chiral Metal-Organic Frameworks (MOFs)
Published on: January 17, 2020
Related Concept Videos
Prochirality
Diels–Alder Reaction Forming Bridged Bicyclic Products: Stereochemistry
Cycloaddition Reactions: Overview
Regioselectivity and Stereochemistry of Acid-Catalyzed Hydration
Stereoisomerism of Cyclic Compounds
Heterogeneous Catalysis