Complementary roles of mutations at positions 69 and 242 in a class A β-lactamase
- 22 February 1995
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1247 (1), 113-120
- https://doi.org/10.1016/0167-4838(94)00187-l
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Clinical isolates of Escherichia coli producing TRI β-lactamases: novel TEM-enzymes conferring resistance to β-lactamase inhibitorsJournal of Antimicrobial Chemotherapy, 1992
- Elucidation of the role of arginine-224 in the turnover processes of class A .beta.-lactamasesBiochemistry, 1992
- OHIO-1 β-lactamase resistant to mechanism-based inactivatorsFEMS Microbiology Letters, 1992
- β‐lactamase TEM1 of E. coli Crystal structure determination at 2.5 Å resolutionFEBS Letters, 1992
- MOLSCRIPT: a program to produce both detailed and schematic plots of protein structuresJournal of Applied Crystallography, 1991
- β-Lactamase of Bacillus licheniformis 749/C: Refinement at 2 Å resolution and analysis of hydrationJournal of Molecular Biology, 1991
- Efficient Degradation of Trichloroethylene by a Recombinant Escherichia ColiNature Biotechnology, 1989
- Crystal structure of 2 ‐ (2‐Amino‐4‐thiazolyl) 2 Z ‐ methoxyimino methylacetamide hydrochloride monohydrate an analog to the C7 side chain of cefotaximeBulletin des Sociétés Chimiques Belges, 1988
- Interior and surface of monomeric proteinsJournal of Molecular Biology, 1987
- Tertiary templates for proteinsJournal of Molecular Biology, 1987