The Promiscuous Activity of the Radical SAM Enzyme NosL toward Two Unnatural Substrates
Author:
Affiliation:
1. Department of Chemistry Fudan University Shanghai 200433 China
Publisher
Wiley
Subject
General Chemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/cjoc.202100304
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2. Montalban‐Lopez M.; Scott T. A.; Ramesh S.; Rahman I. R.; van Heel A. J.; Viel J. H.; Bandarian V.; Dittmann E.; Genilloud O.; Goto Y.; Grande Burgos M. J.; Hill C.; Kim S.; Koehnke J.; Latham J. A.; Link A. J.; Martinez B.; Nair S. K.; Nicolet Y.; Rebuffat S.; Sahl H. G.; Sareen D.; Schmidt E. W.; Schmitt L.; Severinov K.; Sussmuth R. D.; Truman A. W.; Wang H.; Weng J. K.; van Wezel G. P.; Zhang Q.; Zhong J.; Piel J.; Mitchell D. A.; Kuipers O. P.; van der Donk W. A. New developments in RiPP discovery enzymology and engineering.Nat. Prod. Rep.2021 38 130–239.
3. Structure of nosiheptide, a polythiazole-containing antibiotic
4. Nosiheptide Biosynthesis Featuring a Unique Indole Side Ring Formation on the Characteristic Thiopeptide Framework
5. Radical-mediated enzymatic carbon chain fragmentation-recombination
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