期刊
ORGANIC LETTERS
卷 23, 期 7, 页码 2616-2620出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.orglett.1c00525
关键词
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资金
- JSPS KAKENHI (B) [19H02891]
- JSPS [16H06446, 19H04635, 19H04644]
- Grants-in-Aid for Scientific Research [19H04635, 16H06446, 19H04644] Funding Source: KAKEN
In the biosynthetic pathway of mycotoxin cyclochlorotine, DUF3328 proteins mediate various tailoring processes, including chlorination and hydroxylation, demonstrating a much higher functional diversity than previously expected.
Mycotoxin cyclochlorotine (1) and structurally related astins are cyclic pentapeptides containing unique nonproteinogenic amino acids, such as beta-phenylalanine, L-allo-threonine, and 3,4-dichloroproline. Herein, we report the biosynthetic pathway for 1, which involves intriguing tailoring processes mediated by DUF3328 proteins, including stereo- and regiospecific chlorination and hydroxylation and intramolecular O,N-transacylation. Our findings demonstrate that DUF3328 proteins, which are known to be involved in oxidative cyclization of fungal ribosomal peptides, have much higher functional diversity than previously expected.
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