The cytoplasmic peptidoglycan precursor of vancomycin-resistant Enterococcus faecalis terminates in lactate
| Autor: | M. S. Lee, K. J. Volk, Sandra Handwerger, Jinping Liu, M. J. Pucci |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Cytoplasm
Molecular Sequence Data Peptidoglycan Microbiology Mass Spectrometry Enterococcus faecalis chemistry.chemical_compound Plasmid Biosynthesis Vancomycin medicine Amino Acid Sequence Molecular Biology Depsipeptide chemistry.chemical_classification biology Drug Resistance Microbial biochemical phenomena metabolism and nutrition biology.organism_classification Uridine Diphosphate N-Acetylmuramic Acid Enzyme chemistry Biochemistry Bacteria Research Article medicine.drug |
| Zdroj: | Journal of Bacteriology. 174:5982-5984 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.174.18.5982-5984.1992 |
| Popis: | Vancomycin resistance plasmids in enterococci carry the genes vanH and vanA, which encode enzymes catalyzing, respectively, the reduction of 2-keto acids to 2-D-hydroxy acids and the addition of D-hydroxy acids to D-alanine. It has therefore been postulated that resistant cells produce peptidoglycan precursors that terminate in the depsipeptide D-alanine-2-D-hydroxy acid rather than the dipeptide D-alanine-D-alanine, thus preventing vancomycin binding (M. Arthur, C. Molinas, T. D. H. Bugg, G. D. Wright, C. T. Walsh, and P. Courvalin, Antimicrob. Agents Chemother. 36:867-869, 1992). In the present work, a cytoplasmic peptidoglycan precursor was isolated from vancomycin-resistant Enterococcus faecalis and analyzed by mass spectrometry, which suggested the structure UDP-N-acetyl-muramyl-L-Ala-D-Glu-L-Lys-D-Ala-D-lactate. |
| Databáze: | OpenAIRE |
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