By L. Bryan (Eds.)

ISBN-10: 012138120X

ISBN-13: 9780121381202

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Extra resources for Antimicrobial Drug Resistance

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Although Kl /3-lactamase hydrolyzes aztreonam and cefotaxime more efficiently than does TEM /3-lactamase, the combination of the two enzymes in a single organism does not result in increased resis- E. coli SC 10,404 Κ. pneumoniae SC 10,436 Κ. 0091 Units of enzyme activity per mg cells0 Identified using isolectric focusing and substrate profiles. 1 106 Cefuroxime 1. 0 - L A C T A M - j 3 - L A C T A M A S E I N T E R A C T I O N S 25 tance to the antibiotics. The fact that the total amount of ß-lactamase present in SC 11,066 is at least an order of magnitude less than the enzyme levels in the other two organisms must be an important factor in this observed behavior.

1982). Antimicrob. Agents Chemother. 2 2 , 62. Kushner, D . , and Breil, C. (1977). Arch. Microbiol. 112, 219. , Pechere, J . - C , and Allard-Leprohon, D . (1977). Antimicrob. Agents Chemother. 12, 201. Manson, E. E. D . , Pollock, M. , and Tridgell, E. J. (1954). J. Gen Microbiol. 11, 493. Martin, H. H . , Schilf, W . , and M a s k o s , C. (1976). Eur. J. Biochem. 7 1 , 585. Matthew, M. (1978). FEMS Microbiol. Lett. 4, 241. , and Harris, Α . M. (1976). J. Gen. Microbiol. 94, 55. Mehta, R. , and N a s h , C.

The structures of many new, naturally occurring ß-lactams have identified several strategies for achieving this goal, corresponding to the incorporation of particular functional groups at C-6 of penams and C-7 of cephems. Although the mechanistic characterization of the processes that operate is most incomplete—the following statement is an hypothesis rather than a generalization—it appears that these functional groups improve antibiotic activity by interfering with the catalytic mechanism of the ß-lactamases.

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Antimicrobial Drug Resistance by L. Bryan (Eds.)

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