Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 β-lactamase hydrolysing third-generation cephalosporins

This publication has 28 references indexed in Scilit:

• Site-directed Mutagenesis of Glutamate 166 in Two β-Lactamases
  Journal of Biological Chemistry, 1997
• Structural Basis of Extended Spectrum TEM β-Lactamases
  Published by Elsevier ,1996
• Mass Spectral Kinetic Study of Acylation and Deacylation During the Hydrolysis of Penicillins and Cefotaxime by .beta.-Lactamase TEM-1 and the G238S Mutant
  Biochemistry, 1995
• Contribution of mutant analysis to the understanding of enzyme catalysis: The case of class A β-lactamases
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995
• TEM β-Lactamase Mutants Hydrolysing Third-generation Cephalosporins: A Kinetic and Molecular Modelling Analysis
  Journal of Molecular Biology, 1994
• PdbMotif – A tool for the automatic identification and display of motifs in protein structures
  Bioinformatics, 1994
• Evolution of antibiotic resistance: several different amino acid substitutions in an active site loop alter the substrate profile of β‐lactamase
  Molecular Microbiology, 1994
• Improved methods for building protein models in electron density maps and the location of errors in these models
  Acta Crystallographica Section A Foundations of Crystallography, 1991
• New and versatile cloning vectors with kanamycin-resistance marker
  Gene, 1987
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970