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A rapid‐kinetic study of the class C β‐lactamase of Enterobacter cloacae 908R
Author(s) -
Monnaie Didier,
Virden Richard,
Frère Jean-Marie
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80979-q
Subject(s) - enterobacter cloacae , carbenicillin , cephalosporin , enterobacter , chemistry , ampicillin , acylation , microbiology and biotechnology , enterobacteriaceae , antibiotics , biology , biochemistry , escherichia coli , catalysis , gene
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.