Reversible inhibition of penicillinase by quinacillin: Evaluation of mechanisms involving two conformational states of the enzyme
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference10 articles.
1. Substrate-specific inactivation of staphylococcal penicillinase
2. The active site of penicillinase from Staphylococcus aureus PC1. Isolation of a specific covalent complex with the substrate quinacillin
3. The mechanism of folding of globular proteins. Suitability of a penicillinase from Staphylococcus Aureus as a model for refolding studies
4. Preferential nitration with tetranitromethane of a specific tyrosine residue in penicillinase from Staphylococcus aureus PCl. Evidence that the preferentially nitrated residue is not part of the active site but that loss of activity is due to intermolecular cross-linking
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1. Evidence for Structural Elasticity of Class A β-Lactamases in the Course of Catalytic Turnover of the Novel Cephalosporin Cefepime;Journal of the American Chemical Society;1996-01-01
2. Mechanism of turnover of imipenem by the TEM .beta.-lactamase revisited;Journal of the American Chemical Society;1995-07
3. Substrate-induced inactivation of the OXA2 β-lactamase;Biochemical Journal;1993-11-01
4. Interactions between active-site-serine β-lactamases and mechanism-based inactivators: a kinetic study and an overview;Biochemical Journal;1993-11-01
5. Identification of the site of covalent attachment of nafcillin, a reversible suicide inhibitor of β-lactamase;Biochemical Journal;1992-01-01
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