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- W97716245 abstract "This chapter focuses on the physiology, biochemistry, and inactivation of β-lactamases. The significance of β-lactamase in the resistance of pathogens to treatment by β-lactam antibiotics has been the subject of considerable controversy. The activity of a particular β-lactam antibiotic on a particular bacterial strain is often the result of a complex combination of factors in which β-lactamase may play a variety of roles. The factors to be considered in β-lactam-cell interactions include permeability or penetrability, nonlethal binding, susceptibility of target sites, and lytic response. The overall importance of β-lactamase in the response of a bacterial strain to a particular antibiotic is, thus, based on the capacity of the enzyme to complement the basic tolerance or to compensate for a lack of it. β-lactamases hydrolyze the cyclic amide bond in β-lactam-containing molecules such as penicillins and cephalosporins. When the β-lactam ring of a penicillin is hydrolyzed by β-lactamase, the corresponding antibiotically inactive penicilloate is produced in stoichiometric proportions. The first product of β-lactamase attack on a cephalosporin is, hypothetically, a cephalosporoate analogous to penicilloates. Thus, although the determination of the rate of hydrolysis of penicillins by β-lactamases is a relatively simple matter, the situation with cephalosporins is more complex." @default.
- W97716245 created "2016-06-24" @default.
- W97716245 creator A5022556893 @default.
- W97716245 creator A5068520849 @default.
- W97716245 date "1982-01-01" @default.
- W97716245 modified "2023-10-14" @default.
- W97716245 title "Physiology, Biochemistry, and Inactivation of β - Lactamases" @default.
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