ArticleJournal of the American Chemical Society2017
Rerouting the Pathway for the Biosynthesis of the Side Ring System of Nosiheptide: The Roles of NosI, NosJ, and NosK.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 33 citations in OpenAlex.
- Discovery and Biosynthesis of Persiathiacins: Unusual Polyglycosylated Thiopeptides Active Against Multidrug Resistant Tuberculosis.ACS infectious diseases · 2024Article
- Thiopeptides: antibiotics with unique chemical structures and diverse biological activities.The Journal of antibiotics · 2021Review
- Whole genome sequencing ofBiotechnology reports (Amsterdam, Netherlands) · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Minimal lactazole scaffold for in vitro thiopeptide bioengineering.Nature communications · 2020Article
- The hidden enzymology of bacterial natural product biosynthesis.Nature reviews. Chemistry · 2019Article
- Capturing Intermediates in the Reaction Catalyzed by NosN, a Class C Radical S-Adenosylmethionine Methylase Involved in the Biosynthesis of the Nosiheptide Side-Ring System.Journal of the American Chemical Society · 2019Article
- Using Peptide Mimics to Study the Biosynthesis of the Side-Ring System of Nosiheptide.Methods in enzymology · 2018Article
- NosN, a Radical S-Adenosylmethionine Methylase, Catalyzes Both C1 Transfer and Formation of the Ester Linkage of the Side-Ring System during the Biosynthesis of Nosiheptide.Journal of the American Chemical Society · 2017Article
- Biosynthesis of the nosiheptide indole side ring centers on a cryptic carrier protein NosJ.Nature communications · 2017Article
- Ribosomal Natural Products, Tailored To Fit.Accounts of chemical research · 2017Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Nosiheptide (NOS) is a highly modified thiopeptide antibiotic that displays formidable in vitro activity against a variety of Gram-positive bacteria. In addition to a central hydroxypyridine ring, NOS contains several other modifications, including multiple thiazole rings, dehydro-amino acids, and a 3,4-dimethylindolic acid (DMIA) moiety. The DMIA moiety is required for NOS efficacy and is synthesized from l-tryptophan in a series of reactions that have not been fully elucidated. Herein, we describe the role of NosJ, the product of an unannotated gene in the biosynthetic operon for NOS, as an acyl carrier protein that delivers 3-methylindolic acid (MIA) to NosK. We also reassign the role of NosI as the enzyme responsible for catalyzing the ATP-dependent activation of MIA and MIA's attachment to the phosphopantetheine moiety of NosJ. Lastly, NosK catalyzes the transfer of the MIA group from NosJ-MIA to a conserved serine residue (Ser102) on NosK. The X-ray crystal structure of NosK, solved to 2.3 Å resolution, reveals that the protein is an α/β-fold hydrolase. Ser102 interacts with Glu210 and His234 to form a catalytic triad located at the bottom of an open cleft that is large enough to accommodate the thiopeptide framework.
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