Using peptide substrate analogs to characterize a radical intermediate in NosN catalysis
Author:
Funder
National Science Foundation
National Institutes of Health
Howard Hughes Medical Institute
Publisher
Elsevier
Reference15 articles.
1. Rerouting the pathway for the biosynthesis of the side ring system of Nosiheptide: The roles of NosI, NosJ, and NosK;Badding;Journal of the American Chemical Society,2017
2. Mechanistic diversity of radical S-adenosylmethionine (SAM)-dependent methylation;Bauerle;The Journal of Biological Chemistry,2015
3. Mechanistic studies on tryptophan Lyase (NosL): Identification of cyanide as a reaction product;Bhandari;Journal of the American Chemical Society,2018
4. Activity of the thiopeptide antibiotic nosiheptide against contemporary strains of methicillin-resistant Staphylococcus aureus;Haste;Journal of Antibiotics (Tokyo),2012
5. A radical S-adenosyl-L-methionine enzyme and a methyltransferase catalyze cyclopropane formation in natural product biosynthesis;Jin;Nature Communications,2018
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