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• W1528450034 endingPage "1746" @default.
• W1528450034 startingPage "1743" @default.
• W1528450034 abstract "ABSTRACT It has been suggested that class C β-lactamases have evolved to carry out a metabolic reaction other than hydrolysis of β-lactam antibiotics. It is demonstrated in the present study that the class C β-lactamase from Enterobacter cloacae P99 has reached the diffusion limit in its ability to hydrolyze its preferred cephalosporin substrates. The increase in the solution viscosity by addition of a microviscogen (sucrose) caused the decline in the parameter k cat / K m for hydrolysis of cephaloridine and cephalosporin C (approximately 2.5-fold at a relative viscosity of 2.9). A similar increase in viscosity has no effect on the turnover rate of the poorer substrates cefepime and penicillin G. Addition of a macroviscogen (polyethylene glycol) to the reaction mixture did not change the rate of turnover for any of the substrates tested because in this case the viscogen would not interfere with the motion of small molecules, as was expected. Therefore, it would appear that the driving force behind the evolution of this class C β-lactamase and, in principle, other enzymes of this class is indeed the functional reaction of this enzyme as a drug resistance factor." @default.
• W1528450034 created "2016-06-24" @default.
• W1528450034 creator A5013812375 @default.
• W1528450034 creator A5089124080 @default.
• W1528450034 date "1999-07-01" @default.
• W1528450034 modified "2023-09-29" @default.
• W1528450034 title "Class C β-Lactamases Operate at the Diffusion Limit for Turnover of Their Preferred Cephalosporin Substrates" @default.
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• W1528450034 doi "https://doi.org/10.1128/aac.43.7.1743" @default.
• W1528450034 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/89354" @default.
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