Peptidoglycan structure of Lactobacillus casei, a species highly resistant to glycopeptide antibiotics
| Autor: | R Legrand, J van Heijenoort, B Schoot, Laurent Gutmann, D Billot-Klein |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1997 |
| Předmět: |
Lactobacillus casei
medicine.drug_class Antibiotics Peptidoglycan Microbiology Mass Spectrometry chemistry.chemical_compound medicine Asparagine Molecular Biology Chromatography High Pressure Liquid Oligopeptide biology Acetylation Drug Resistance Microbial Penicillin G biology.organism_classification Glycopeptide Anti-Bacterial Agents Penicillin Molecular Weight Lacticaseibacillus casei Monomer Biochemistry chemistry Oligopeptides medicine.drug Research Article |
| Popis: | The structure of the peptidoglycan of Lactobacillus casei ATCC 393, a species highly resistant to glycopeptide antibiotics, was examined. After digestion, 23 muropeptides were identified; monomers represented 44.7% of all muropeptides, with monomer tetrapeptides being the major ones. Fifty-nine percent of the peptidoglycan was O-acetylated. The cross-bridge between D-alanine and L-lysine consisted of one asparagine, although aspartate could be found in minor quantities. Since UDP-MurNAc-tetrapeptide-D-lactate is the normal cytoplasmic precursor found in this species, monomer tetrapeptide-lactate was expected to be found. However, such a monomer was found only after exposure to penicillin, suggesting that penicillin-sensitive D,D-carboxypeptidases were very active in normal growing cells. |
| Databáze: | OpenAIRE |
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