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Updated: Sep 8, 2025

Preparation of Enantiopure Non-Activated Aziridines and Synthesis of Biemamide B, D, and epiallo-Isomuscarine
Published on: June 13, 2022
Cyclodimerization of Mohangamide A by Thioesterase Domain Is Directed by Substrates
Myoun-Su Kim1, Munhyung Bae2, Myoung Chong Song1
1Natural Products Research Institute, College of Pharmacy, Seoul National University, Seoul 08826, Republic of Korea.
Abstract:
Mohangamide A is a pseudo-dimeric nonribosomal peptide biosynthesized along with its monomer, WS9326A, and is expected to be formed by the head-to-tail cyclodimerization of linear WS9326A and another identical peptide chain with a different acyl side chain. In vitro experiments with the N-acetylcysteamine thioesters of the corresponding monomeric intermediates and thioesterase domains of Streptomyces sp. SNM55 and S. calvus showed that this cyclodimerization reaction is directed by the substrate structures and occurs only with both linear intermediates.
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