Cyclodimerization of Mohangamide A by Thioesterase Domain Is Directed by Substrates

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-acetylcyst...

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Published inOrganic letters Vol. 24; no. 24; pp. 4444 - 4448
Main Authors Kim, Myoun-Su, Bae, Munhyung, Song, Myoung Chong, Hwang, Sunghoon, Oh, Dong-Chan, Yoon, Yeo Joon
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 24.06.2022
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Summary: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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ISSN:1523-7060
1523-7052
DOI:10.1021/acs.orglett.2c01670