Analysis of the Importance of the Metallo-β-Lactamase Active Site Loop in Substrate Binding and Catalysis

This publication has 37 references indexed in Scilit:

• Biochemical Characterization of the FEZ-1 Metallo-β-Lactamase of Legionella gormanii ATCC 33297 ^T Produced in Escherichia coli
  Antimicrobial Agents and Chemotherapy, 2001
• Standard Numbering Scheme for Class B β-Lactamases
  Antimicrobial 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 Loop
  Biochemistry, 1999
• The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 å resolution 1 1Edited by K. Nagai
  Journal of Molecular Biology, 1998
• Mono‐ and binuclear Zn‐β‐lactamase from Bacteroides fragilis: catalytic and structural roles of the zinc ions
  FEBS 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 II
  Biochemistry, 1998
• X-ray Structure of the Zn^II β-Lactamase from Bacteroides fragilis in an Orthorhombic Crystal Form
  Acta Crystallographica Section D Structural Biology, 1998
• Zn(II) Dependence of the Aeromonas hydrophila AE036 Metallo-β-lactamase Activity and Stability
  Biochemistry, 1997