A minimalistic approach to identify substrate binding features in B1 Metallo-β-lactamases
- 1 September 2007
- journal article
- research article
- Published by Elsevier in Bioorganic & Medicinal Chemistry Letters
- Vol. 17 (18) , 5171-5174
- https://doi.org/10.1016/j.bmcl.2007.06.089
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Metallo-β-lactamases: Novel Weaponry for Antibiotic Resistance in BacteriaAccounts of Chemical Research, 2006
- Antibiotic Recognition by Binuclear Metallo-β-Lactamases Revealed by X-ray CrystallographyJournal of the American Chemical Society, 2005
- Bacterial Resistance to β-Lactam Antibiotics: Compelling Opportunism, Compelling OpportunityChemical Reviews, 2005
- Structural Determinants of Substrate Binding to Bacillus cereus Metallo-β-lactamaseJournal of Biological Chemistry, 2004
- Substrate binding to mononuclear metallo‐β‐lactamase from Bacillus cereusProteins-Structure Function and Bioinformatics, 2003
- Thiomandelic Acid, a Broad Spectrum Inhibitor of Zinc β-LactamasesJournal of Biological Chemistry, 2001
- Standard Numbering Scheme for Class B β-LactamasesAntimicrobial Agents and Chemotherapy, 2001
- Spectroscopic Characterization of a Binuclear Metal Site in Bacillus cereus β-Lactamase IIBiochemistry, 1998
- Unanticipated Inhibition of the Metallo-β-lactamase from Bacteroides fragilis by 4-Morpholineethanesulfonic Acid (MES): A Crystallographic Study at 1.85-Å ResolutionBiochemistry, 1998
- An overview of the kinetic parameters of class B β-lactamasesBiochemical Journal, 1993