In vitro Activity and β-Lactamase Stability of N-Formimidoyl Thienamycin Compared to that of Second and Third Generation Cephalosporins

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Abstract
N-Formimidoyl thienamycin (MK0787) was found to be active against 21 gram-negative isolates, selected for their β-lactamase production. None of the crude β-lactamases could hydrolyze MK0787 or cefoxitin, in contrast to cefotaxime which was moderately attacked by a number of enzymes. MK0787 behaved as a moderate inhibitor of most β-lactamases, whereas cefoxitin and cefotaxime were strong inhibitors of cephalo-sporinases but not of broad-spectrum enzymes. The new compound had good penetration characteristics in a strain of Enterobacter cloacae, in contrast to cefoxitin. Against a number of trained cefamandole- and cefoxitin-resistant variants, MK0787 was clearly the most active of the compounds tested.

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