Cysteinyl peptide Inhibitors of Bacillus cereus Zinc β-Lactamase

This publication has 14 references indexed in Scilit:

• Structural consequences of the active site substitution Cys181 ==> Ser in metallo-beta-lactamase from Bacteroides fragilis.
  Protein Science, 2008
• Metallo-β-lactamase: structure and mechanism
  Current Opinion in Chemical Biology, 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
• The mechanism of catalysis and the inhibition of β-lactamases
  Chemical Communications, 1998
• Crystal structures of the cadmium‐ and mercury‐substituted metallo‐β‐lactamase from Bacteroides fragilis
  Protein Science, 1997
• Inhibition of metallo-β-lactamases by a series of thiol ester derivatives of mercaptophenylacetic acid
  FEMS Microbiology Letters, 1997
• Characterization of the Metal-Binding Sites of the β-Lactamase from Bacteroides fragilis
  Biochemistry, 1996
• Carboxy ester hydrolysis catalysed by a dinuclear, hexaazamacrocyclic zinc(II) complex. A model for zinc(II) aminopeptidases
  J. Chem. Soc., Dalton Trans., 1996