期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 59, 期 10, 页码 3988-3993出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201916269
关键词
biosynthesis; cytochrome P450 monooxygenases; enzymes; natural products; teleocidin
资金
- Ministry of Education, Culture, Sports, Science and Technology, Japan [KAKENHI 16H06276]
- Ministry of Education, Culture, Sports, Science and Technology, Japan (JSPS KAKENHI) [JP16H06443, JP18K19139, JP 19K15703]
- Japan Science and Technology Agency (JST SICORP) [JPMJSC1701]
- AMED [JP19ak0101101]
- MEXT's Nanotechnology Platform Program (Molecule and Material Synthesis)
C-S bond formation reactions are widely distributed in the biosynthesis of biologically active molecules, and thus have received much attention over the past decades. Herein, we report intramolecular C-S bond formation by a P450 monooxygenase, TleB, which normally catalyzes a C-N bond formation in teleocidin biosynthesis. Based on the proposed reaction mechanism of TleB, a thiol-substituted substrate analogue was synthesized and tested in the enzyme reaction, which afforded the unprecedented sulfur-containing thio-indolactam V, in addition to an unusual indole-fused 6/5/8-tricyclic product whose structure was determined by the crystalline sponge method. Interestingly, conformational analysis revealed that the SOFA conformation is stable in thio-indolactam V, in sharp contrast to the major TWIST form in indolactam V, resulting in differences in their biological activities.
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