Mutagenesis of amino acid residues in the SHV-1 β-lactamase: the premier role of Gly238Ser in penicillin and cephalosporin resistance
- 5 May 2001
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1547 (1) , 37-50
- https://doi.org/10.1016/s0167-4838(01)00164-9
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- Effects on Substrate Profile by Mutational Substitutions at Positions 164 and 179 of the Class A TEMpUC19 β-Lactamase from Escherichia coliJournal of Biological Chemistry, 1999
- OHIO-1 β-lactamase mutants: the Arg244Ser mutant and resistance to β-lactams and β-lactamase inhibitorsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1999
- Clinical inhibitor-resistant mutants of the β-lactamase TEM-1 at amino-acid position 69: Kinetic analysis and molecular modellingBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1998
- Amino Acid Sequence Determinants of β-Lactamase Structure and ActivityJournal of Molecular Biology, 1996
- Mass Spectral Kinetic Study of Acylation and Deacylation During the Hydrolysis of Penicillins and Cefotaxime by .beta.-Lactamase TEM-1 and the G238S MutantBiochemistry, 1995
- Complementary roles of mutations at positions 69 and 242 in a class A β-lactamaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995
- TEM β-Lactamase Mutants Hydrolysing Third-generation Cephalosporins: A Kinetic and Molecular Modelling AnalysisJournal of Molecular Biology, 1994
- Evolution of antibiotic resistance: several different amino acid substitutions in an active site loop alter the substrate profile of β‐lactamaseMolecular Microbiology, 1994
- β‐lactamase TEM1 of E. coli Crystal structure determination at 2.5 Å resolutionFEBS Letters, 1992
- Structural basis for the inactivation of the P54 mutant of .beta.-lactamase from Staphylococcus aureus PC1Biochemistry, 1991