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By L. Bryan (Eds.)

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Enzymol. Relat. Areas Mol. Biol. 28, 237. Cohen, S. Α . , and Pratt, R. F. (1980). Biochemistry 19, 3996. Collins, J. F. (1971). In "Metabolic P a t h w a y s " (H. G. ), Vol. V, p. 489. Academic Press, N e w York. , and H o w e , T. G. B. (1980). Antimicrob. Agents Chemother. 18, 667. Curtis, N . A . C , Orr, D . , R o s s , G. , and Boulton, M. G. (1979). Antimicrob. Agents Chemother. 16, 533. D e c a d , G. , and Nikaido, H. (1976). J. Bacteriol. 28, 325. , Klein, D . -M. (1981). Biochem. J.

Many older /3-lactams (ampicillin, cephalothin) are potent inducers for the expression of the Class C cephalosporinases found in numerous gramnegative pathogens (such as E. cloacae, P. mirabilis, and P. aeruginosa). This induction is also accomplished by many ß-lactamase-stable cephems, particularly cefoxitin (Fu and Neu, 1980; Then and Angehrn, 1982). The ^-lactamases that are expressed may have a greater affinity for the inducer (better acylation) and a greater hydrolytic ability (better deacylation) (Fu and Neu, 1980).

1981). 39 nm, and hence may possess antibiotic activity. This prediction will most certainly receive experimental scrutiny shortly and if it holds true may present a new strategy for cephem antibiotic design. Thus, the bicyclic templates that may be elaborated into broad-spectrum, /3-lactamase resistant antibiotics are those of the monolactams ( 1 ) , penams ( 2 ) , penems ( 3 ) , carbapenems ( 4 ) , and cephems ( 5 ) . The functional groups to be inserted derive for the most part from existing ßlactam antibiotics and as will be seen may lead to significant departures from structures 1 - 5 (such as the oxacephems, clavulanates, and asparenomycins).

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