The Albicidin Resistance Factor AlbD Is a Serine Endopeptidase That Hydrolyzes Unusual Oligoaromatic-Type Peptides
| Autor: | Andi Mainz, Monique Royer, Dennis Kerwat, Roderich D. Süssmuth, Stéphane Cociancich, Julian Kretz, Stefan Grätz, Alexander Pesic, Laura Vieweg |
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| Rok vydání: | 2015 |
| Předmět: |
Xanthomonas albilineans
Peptide Isomerase Biochemistry DNA gyrase Colloid and Surface Chemistry Peptide bond Organic Chemicals Propriété antimicrobienne chemistry.chemical_classification Saccharum officinarum biology Chemistry Hydrolysis Serine Endopeptidases Enterobacteriaceae Infections 000 - Autres thèmes Composé aromatique Endopeptidase Anti-Bacterial Agents Bactérie gram négatif Activité enzymatique Xanthomonas Stereochemistry Détoxification métabolique Catalysis Drug Resistance Bacterial Hydrolase Humans Peptidase H20 - Maladies des plantes Isomérase Pantoea Inhibiteur d'enzyme Biologie moléculaire General Chemistry biology.organism_classification Acide benzoïque Antimicrobien Bacteria |
| Zdroj: | Journal of the American Chemical Society |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/jacs.5b04099 |
| Popis: | The para-aminobenzoic acid-containing peptide albicidin is a pathogenicity factor synthesized by Xanthomonas albilineans in infections of sugar cane. Albicidin is a nanomolar inhibitor of the bacterial DNA gyrase with a strong activity against various Gram-negative bacteria. The bacterium Pantoea dispersa expresses the hydrolase AlbD, conferring natural resistance against albicidin. We show that AlbD is a novel type of endopeptidase that catalyzes the cleavage of albicidin at a peptide backbone amide bond, thus abolishing its antimicrobial activity. Additionally, we determined the minimal cleavage motif of AlbD with substrates derived by chemical synthesis. Our results clearly identify AlbD as a unique endopeptidase that is the first member of a new subfamily of peptidases. Our findings provide the molecular basis for a natural detoxification mechanism, potentially rendering a new tool in biological chemistry approaches. |
| Databáze: | OpenAIRE |
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