A rapid-kinetic study of the class C β-lactamase of Enterobacter cloacae 908R
Autor: | Richard Virden, Jean-Marie Frère, Didier Monnaie |
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Rok vydání: | 1992 |
Předmět: |
medicine.drug_class
Stereochemistry Cephalosporin Enterobacter Biophysics Rapid kinetics Biochemistry beta-Lactamases Substrate Specificity Acylation Structural Biology Ampicillin Enterobacter cloacae polycyclic compounds Genetics medicine Molecular Biology β-Lactamase Cephalosporinase biology Chemistry Cell Biology biochemical phenomena metabolism and nutrition Carbenicillin Penicillin biology.organism_classification Enterobacteriaceae Kinetics beta-Lactamase Inhibitors medicine.drug |
Zdroj: | FEBS Letters. 306:108-112 |
ISSN: | 0014-5793 |
DOI: | 10.1016/0014-5793(92)80979-q |
Popis: | The individual rate constants for acylation and deacylation ( k 2 and k 3 , respectively) of the class C β-lactamase of Enterobacter cloacae 908R by ampicillin and carbenicillin have been determined. For several other β-lactams, the value of k 2 was too high to be determined and the k 2 / k 3 ratio could be larger than 10,000. Branched pathways were also shown to occur with several penicillins and cephalosporins. |
Databáze: | OpenAIRE |
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