The Asparagine to Aspartic Acid Substitution at Position 276 of TEM-35 and TEM-36 Is Involved in the β-Lactamase Resistance to Clavulanic Acid
Open Access
- 1 August 1995
- journal article
- research article
- Published by Elsevier
- Vol. 270 (31) , 18240-18245
- https://doi.org/10.1074/jbc.270.31.18240
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Inhibition of β-lactamase by clavulanate: Trapped intermediates in cryocrystallographic studiesPublished by Elsevier ,2004
- β-Lactamase mutations far from the active site influence inhibitor bindingBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995
- Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to β-lactamase inhibitorsFEMS Microbiology Letters, 1994
- Nucleotide sequences of the genes coding for the TEM-like β-lactamases IRT-1 and IRT-2 (formerly called TRI-1 and TRI-2)FEMS Microbiology Letters, 1994
- Site‐directed mutagenesis of β‐lactamase TEM‐1European Journal of Biochemistry, 1993
- A rapid finite difference algorithm, utilizing successive over‐relaxation to solve the Poisson–Boltzmann equationJournal of Computational Chemistry, 1991
- Construction of Escherichia coli amber suppressor tRNA genesJournal of Molecular Biology, 1990
- Probing the active site of β-lactamase R-TEM1 by informational suppressionBiochimie, 1990
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976