Nature chemical biology, 2016-01, Vol.12 (1), p.9
2016
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- Autor(en) / Beteiligte
- Titel
- Class D β-lactamases do exist in Gram-positive bacteria
- Ist Teil von
- Nature chemical biology, 2016-01, Vol.12 (1), p.9
- Ort / Verlag
- United States
- Erscheinungsjahr
- 2016
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- Production of β-lactamases of one of four molecular classes (A, B, C and D) is the major mechanism of bacterial resistance to β-lactams, the largest class of antibiotics, which have saved countless lives since their inception 70 years ago. Although several hundred efficient class D enzymes have been identified in Gram-negative pathogens over the last four decades, none have been reported in Gram-positive bacteria. Here we demonstrate that efficient class D β-lactamases capable of hydrolyzing a wide array of β-lactam substrates are widely disseminated in various species of environmental Gram-positive organisms. Class D enzymes of Gram-positive bacteria have a distinct structural architecture and employ a unique substrate-binding mode that is quite different from that of all currently known class A, C and D β-lactamases. These enzymes thus constitute a previously unknown reservoir of novel antibiotic-resistance enzymes.
- Sprache
- Englisch
- Identifikatoren
- eISSN: 1552-4469DOI: 10.1038/nchembio.1950Titel-ID: cdi_pubmed_primary_26551395
- Format
- –
- Schlagworte
- Amino Acid Sequence, Arginine - chemistry, Arginine - metabolism, Bacillaceae - enzymology, Bacillaceae - genetics, beta-Lactamases - chemistry, beta-Lactamases - genetics, beta-Lactamases - metabolism, beta-Lactams - metabolism, beta-Lactams - pharmacology, Crystallography, X-Ray, Drug Resistance, Bacterial - drug effects, Drug Resistance, Bacterial - genetics, Escherichia coli - drug effects, Escherichia coli - genetics, Gram-Positive Bacteria - enzymology, Gram-Positive Bacteria - genetics, Hydrolysis, Microbial Sensitivity Tests, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid