The Evolution of Cefotaximase Activity in the TEM β-Lactamase (original) (raw)
Covalent docking and molecular dynamics simulations reveal the specificity-shifting mutations Ala237Arg and Ala237Lys in TEM beta-lactamase
Brenda Rubenstein
PLOS Computational Biology
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Molecular dynamics at the root of expansion of function in the M69L inhibitor-resistant TEM beta-lactamase from Escherichia coli
P. Roblin, Laurent Maveyraud
Journal of the American Chemical Society, 2002
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Simulated annealing exploration of an active-site tyrosine in TEM-1β-lactamase suggests the existence of alternate conformations
Joelle Pelletier
Proteins: Structure, Function, and Bioinformatics, 2007
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Molecular Basis for the Catalytic Specificity of the CTX-M Extended-Spectrum β-Lactamases
Lori Banks
Biochemistry, 2015
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Evolution of an Antibiotic Resistance Enzyme Constrained by Stability and Activity Trade-offs
George Minasov
Journal of Molecular Biology, 2002
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Structure and Dynamics of CTX-M Enzymes Reveal Insights into Substrate Accommodation by Extended-spectrum β-Lactamases
Julien Delmas
Journal of Molecular Biology, 2008
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Structure and dynamics of CTX-M enzymes reveal insights into substrate accommodation by extended-spectrum beta-lactamases
Julien Delmas
Journal of molecular biology, 2008
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Effects on Substrate Profile by Mutational Substitutions at Positions 164 and 179 of the Class A TEMpUC19 β-Lactamase from Escherichia coli
pascale tronche
Journal of Biological Chemistry, 1999
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Multiple substitutions at position 104 of β -lactamase TEM-1: assessing the role of this residue in substrate specificity
Laurent Maveyraud
Biochemical Journal, 1995
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Mutual influence of secondary and key drug-resistance mutations on catalytic properties and thermal stability of TEM-type β-lactamases
Alexey Egorov
FEBS open bio, 2018
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Evolution of antibiotic resistance: several different amino acid substitutions in an active site loop alter the substrate profile of ?-lactamase
Quyen Le
Molecular Microbiology, 1994
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Catalytic properties of class A β-lactamases: efficiency and diversity
A. Matagne
Biochemical Journal, 1998
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Evolutionary Trajectories of Beta-Lactamase CTX-M-1 Cluster Enzymes: Predicting Antibiotic Resistance
Iñaki Comas
PLoS Pathogens, 2010
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Atomic Resolution Structures of CTX-M β-Lactamases: Extended Spectrum Activities from Increased Mobility and Decreased Stability
Julien Delmas
Journal of Molecular Biology, 2005
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Impact of Mutations at Arg220 and Thr237 in PER-2 β-Lactamase on Conformation, Activity, and Susceptibility to Inhibitors
Gabriel Gutkind
Antimicrobial Agents and Chemotherapy, 2017
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Molecular evolution of ubiquitous ?-lactamases towards extended-spectrum enzymes active against newer ?-lactam antibiotics
Professeur Labia
Molecular Microbiology, 1990
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Recognition and Resistance in TEM β-Lactamase †
George Minasov
Biochemistry, 2003
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Known Evolutionary Paths Are Accessible to Engineered ß-Lactamases Having Altered Protein Motions at the Timescale of Catalytic Turnover
Carles Perez Lopez
Frontiers in Molecular Biosciences, 2020
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A secondary drug resistance mutation of TEM-1 beta -lactamase that suppresses misfolding and aggregation
T. Palzkill
Proceedings of the National Academy of Sciences, 2000
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Capturing the mutational landscape of the beta-lactamase TEM-1
B. Bercot
Proceedings of the National Academy of Sciences, 2013
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Structural Basis for Clinical Longevity of Carbapenem Antibiotics in the Face of Challenge by the Common Class A β-Lactamases from the Antibiotic-Resistant Bacteria
Jean-Denis Pédelacq
Journal of the American Chemical Society, 1998
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Characterization of TEM-1 beta-lactamase mutants from positions 238 to 241 with increased catalytic efficiency for ceftazidime
T. Palzkill
Journal of Biological Chemistry, 1994
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Twelve Positions in a β-Lactamase That Can Expand Its Substrate Spectrum with a Single Amino Acid Substitution
Yun Hwan Cho
PLoS ONE, 2012
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Semi-rational approaches to engineering enzyme activity: combining the benefits of directed evolution and rational design
Joelle Pelletier
Current Opinion in Biotechnology, 2005
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Clinical inhibitor-resistant mutants of the β-lactamase TEM-1 at amino-acid position 69
Professeur Labia
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1998
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Site-saturation Mutagenesis of Tyr-105 Reveals Its Importance in Substrate Stabilization and Discrimination in TEM-1 -Lactamase
Joelle Pelletier
Journal of Biological Chemistry, 2004
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Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability
Julien Delmas
Journal of molecular biology, 2005
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