Cyclodimerization of Mohangamide A by Thioesterase Domain Is Directed by Substrates
- Authors
- Kim, Myoun-Su; Bae, Munhyung; Song, Myoung Chong; Hwang, Sunghoon; Oh, Dong-Chan; Yoon, Yeo Joon
- Issue Date
- Jun-2022
- Publisher
- AMER CHEMICAL SOC
- Citation
- ORGANIC LETTERS, v.24, no.24, pp.4444 - 4448
- Journal Title
- ORGANIC LETTERS
- Volume
- 24
- Number
- 24
- Start Page
- 4444
- End Page
- 4448
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/85353
- DOI
- 10.1021/acs.orglett.2c01670
- ISSN
- 1523-7060
- 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. SNMSS 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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