Mehta R J, Newman D J, Bowie B A, Nash C H, Actor P
J Antibiot (Tokyo). 1981 Feb;34(2):202-5. doi: 10.7164/antibiotics.34.202.
The stability of cefonicid (SK&F 75073) towards representatives of six major classes of beta-lactamases was determined using a spectrophotometric assay. Cefonicid was stable to hydrolysis by the Type I enzyme from Enterobacter cloacae and by the enzyme from the anaerobe, Bacteroides fragilis. It was 6 to 7 times more stable than cefamandole to the Type IIIA and B enzymes from Escherichia coli, a little less stable than this antibiotic to the Type V enzyme from E. coli, and of equal stability to the Type IV enzyme from Klebsiella aerogenes. Cefonicid was a non-competitive inhibitor (Ki of 0.8 x 10(-6)M) of cephalothin hydrolysis by the Type I enzyme.