A rapid-kinetic study of the class C β-lactamase of Enterobacter cloacae 908R
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(92)80979-Q/fullpdf
Reference11 articles.
1. The acyl-enzyme mechanism of β-lactamase action. The evidence for class C β-lactamases
2. A survey of the kinetic parameters of class C β-lactamases. Penicillins
3. A survey of the kinetic parameters of class C β-lactamases. Cephalosporins and other β-lactam compounds
4. Role of lysine-67 in the active site of class C beta-lactamase from Citrobacter freundii GN346
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1. Mechanism and Kinetics of Aztreonam Hydrolysis Catalyzed by Class-C β-Lactamase: A Temperature-Accelerated Sliced Sampling Study;The Journal of Physical Chemistry B;2018-03-19
2. Exploring high dimensional free energy landscapes: Temperature accelerated sliced sampling;The Journal of Chemical Physics;2017-03-07
3. Deacylation Mechanism and Kinetics of Acyl–Enzyme Complex of Class C β-Lactamase and Cephalothin;The Journal of Physical Chemistry B;2016-03-08
4. Kinetics of β-Lactamases and Penicillin-Binding Proteins;Enzyme-Mediated Resistance to Antibiotics;2014-04-30
5. Actividad inhibitoria de dihidroxifenilpropenona sobre β-lactamasa de Enterobacter cloacae: estudio preliminar en el desarrollo de fármacos para enfrentar la resistencia bacteriana;Biomédica;2013-11-25
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