A Heterotrimeric Dehydrogenase Complex Functions with 2 Distinct YcaO Proteins to Install 5 Azole Heterocycles into 35-Membered Sulfomycin Thiopeptides.
Journal
Journal of the American Chemical Society
ISSN: 1520-5126
Titre abrégé: J Am Chem Soc
Pays: United States
ID NLM: 7503056
Informations de publication
Date de publication:
06 05 2020
06 05 2020
Historique:
pubmed:
16
4
2020
medline:
14
4
2021
entrez:
16
4
2020
Statut:
ppublish
Résumé
Sulfomycins are sulfur-rich, ribosomally synthesized, and post-translationally modified peptides (RiPPs) that are characterized by a 35-membered macrocyclic ring system with a pyridine domain central to five azoles and additional dehydroamino acids. The pathway through which these large thiopeptide antibiotics are formed in
Identifiants
pubmed: 32293883
doi: 10.1021/jacs.0c02329
doi:
Substances chimiques
Azoles
0
Bacterial Proteins
0
Peptides
0
Sulfhydryl Compounds
0
sulfomycin
65454-59-3
Oxidoreductases
EC 1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
8454-8463Commentaires et corrections
Type : ErratumIn