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Δευτέρα 21 Μαΐου 2018

Replacement by site-saturation mutagenesis of residue 119 in NDM-1 metallo-{beta}-lactamase: a kinetic study [PublishAheadOfPrint]

NDM-1 is a subclass B1 metallo-β-lactamase which exhibits a broad activity spectrum against β-lactam antibiotics. In this study we report the kinetic study of six Q119X variants obtained by site-directed mutagenesis on NDM-1. All Q119X variants were able to hydrolyze very efficiently carbapenems, penicillins and 1st, 2nd, 3rd and 4th generation cephalosporins. In particular, Q119E, Q119Y, Q119V and Q119K mutants showed an improvement of kcat/Km towards penicillins respect to NDM-1. The catalytic efficiency of Q119K variant is about 65- and 70-fold higher than that of NDM-1 for benzylpenicillin and carbenicillin, respectively. The Q119K and Q119Y enzymes have kcat/Km values for ceftazidime of about 25- and 89-fold higher than NDM-1.



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