Selection of β-lactamases and penicillin binding mutants from a library of phage displayed TEM-1 β-lactamase randomly mutated in the active site Ω-loop
- 21 January 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 295 (3) , 527-540
- https://doi.org/10.1006/jmbi.1999.3376
Abstract
No abstract availableKeywords
This publication has 58 references indexed in Scilit:
- In vivo versus in vitro screening or selection for catalytic activity in enzymes and abzymesMolecular Biotechnology, 1997
- Amino Acid Sequence Determinants of β-Lactamase Structure and ActivityJournal of Molecular Biology, 1996
- Structural Basis of Extended Spectrum TEM β-LactamasesPublished by Elsevier ,1996
- Contribution of mutant analysis to the understanding of enzyme catalysis: The case of class A β-lactamasesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995
- Evolution of antibiotic resistance: several different amino acid substitutions in an active site loop alter the substrate profile of β‐lactamaseMolecular Microbiology, 1994
- Selection of β-Lactamase on Filamentous Bacteriophage by Catalytic ActivityJournal of Molecular Biology, 1994
- Structural basis for the inactivation of the P54 mutant of .beta.-lactamase from Staphylococcus aureus PC1Biochemistry, 1991
- Making antibody fragments using phage display librariesNature, 1991
- β-Lactamase of Bacillus licheniformis 749/C: Refinement at 2 Å resolution and analysis of hydrationJournal of Molecular Biology, 1991
- Site-directed mutagenesis on TEM-1 ß-lactamase: role of Glul66 in catalysis and substrate bindingProtein Engineering, Design and Selection, 1991