Analysis of the Importance of the Metallo-β-Lactamase Active Site Loop in Substrate Binding and Catalysis
- 30 April 2003
- journal article
- Published by Elsevier BV in Cell Chemical Biology
- Vol. 10 (4), 319-329
- https://doi.org/10.1016/s1074-5521(03)00070-x
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Biochemical Characterization of the FEZ-1 Metallo-β-Lactamase of Legionella gormanii ATCC 33297 T Produced in Escherichia coliAntimicrobial Agents and Chemotherapy, 2001
- Standard Numbering Scheme for Class B β-LactamasesAntimicrobial Agents and Chemotherapy, 2001
- Crystal Structure of the IMP-1 Metallo β-Lactamase from Pseudomonas aeruginosa and Its Complex with a Mercaptocarboxylate Inhibitor: Binding Determinants of a Potent, Broad-Spectrum Inhibitor,Biochemistry, 2000
- NMR Characterization of the Metallo-β-lactamase from Bacteroides fragilis and Its Interaction with a Tight-Binding Inhibitor: Role of an Active-Site LoopBiochemistry, 1999
- The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 å resolutionJournal of Molecular Biology, 1998
- Mono‐ and binuclear Zn‐β‐lactamase from Bacteroides fragilis: catalytic and structural roles of the zinc ionsFEBS Letters, 1998
- Crystal Structure of the Zinc-Dependent β-Lactamase from Bacillus cereus at 1.9 Å Resolution: Binuclear Active Site with Features of a Mononuclear Enzyme,Biochemistry, 1998
- Spectroscopic Characterization of a Binuclear Metal Site in Bacillus cereus β-Lactamase IIBiochemistry, 1998
- X-ray Structure of the ZnII β-Lactamase from Bacteroides fragilis in an Orthorhombic Crystal FormActa crystallographica. Section D, Structural biology, 1998
- Zn(II) Dependence of the Aeromonas hydrophila AE036 Metallo-β-lactamase Activity and StabilityBiochemistry, 1997