Mechanistically Distinct Nonribosomal Peptide Synthetases Assemble the Structurally Related Antibiotics Viomycin and Capreomycin

Tuberactinomycin biosynthesis: Viomycin and capreomycin are structurally related antituberculosis drugs. Analysis of the nonribosomal peptide synthetases that assemble these molecules determined that peptide assembly occurs by distinct mechanisms. These unexpected differences provide insights into h...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Chembiochem : a European journal of chemical biology 2011-08, Vol.12 (12), p.1859-1867
Hauptverfasser:	Felnagle, Elizabeth A., Podevels, Angela M., Barkei, John J., Thomas, Michael G.
Format:	Artikel
Sprache:	eng
Schlagworte:	antibiotics Antitubercular Agents - chemistry Antitubercular Agents - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism capreomycin Capreomycin - chemistry Capreomycin - metabolism Chromatography, High Pressure Liquid DNA Primers Escherichia coli - enzymology Escherichia coli - genetics Extensively Drug-Resistant Tuberculosis - drug therapy Extensively Drug-Resistant Tuberculosis - microbiology Metabolic Engineering - methods Mycobacterium tuberculosis - drug effects Mycobacterium tuberculosis - growth & development natural products Peptide Biosynthesis, Nucleic Acid-Independent - genetics Peptide Synthases - chemistry Peptide Synthases - genetics Peptide Synthases - metabolism Plasmids Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Streptomyces lividans - enzymology Streptomyces lividans - genetics Structural Homology, Protein synthetases Transformation, Genetic viomycin Viomycin - chemistry Viomycin - metabolism
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	Tuberactinomycin biosynthesis: Viomycin and capreomycin are structurally related antituberculosis drugs. Analysis of the nonribosomal peptide synthetases that assemble these molecules determined that peptide assembly occurs by distinct mechanisms. These unexpected differences provide insights into how modifications to homologous nonribosomal peptide synthetases can result in structure diversification.
ISSN:	1439-4227 1439-7633
DOI:	10.1002/cbic.201100193