Open AccessStability of cefdinir (CI-983, FK482) to extendedspectrum plasmid-mediated -lactamases
Author(s) -
D. J. Payne,
S. G. B. Amyes
Publication year - 1993
Publication title -
journal of medical microbiology/journal of medical microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.91
H-Index - 117
eISSN - 1473-5644
pISSN - 0022-2615
DOI - 10.1099/00222615-38-2-114
Subject(s) - cefdinir , cephaloridine , cefuroxime , cefixime , ceftazidime , cefotaxime , cephalosporin , ampicillin , chemistry , microbiology and biotechnology , carbenicillin , beta lactamase , antibiotics , biology , escherichia coli , biochemistry , bacteria , genetics , gene , pseudomonas aeruginosa
Fourteen plasmid-encoded extended-spectrum beta-lactamases were purified from Escherichia coli transconjugants of original clinical isolates. The Vmax, Km and Vmax/Km were each determined for ampicillin, carbenicillin, cephaloridine, cephalexin, cefuroxime, cefixime, cefdinir, ceftazidime and cefotaxime as substrates with eight of these enzymes and with the narrow-spectrum beta-lactamase, TEM-1. The relative rates of hydrolysis of ampicillin, cephaloridine, cephalexin, cefuroxime, cefixime, cefdinir, ceftazidime and cefotaxime were also determined for the remaining six enzymes. Cefdinir had Vmax/Km or relative rates of hydrolysis values either equal to or lower than ampicillin, cephaloridine, cephalexin and cefotaxime for all the enzymes tested. Overall, cefdinir was more stable to the 15 beta-lactamases tested than either cefuroxime or cefixime; however, ceftazidime was more stable than cefdinir to hydrolysis by eight of the enzymes tested.