Reference : A Kinetic Study of the Replacement by Site Saturation Mutagenesis of Residue 119 in N...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/227009
A Kinetic Study of the Replacement by Site Saturation Mutagenesis of Residue 119 in NDM-1 Metallo- beta-Lactamase
English
Marcoccia, Francesca [> >]
Mercuri, Paola mailto [Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques >]
Galleni, Moreno mailto [Université de Liège - ULiège > Département des sciences de la vie > Macromolécules biologiques >]
Celenza, Giuseppe [> >]
Amicosante, Gianfranco [> >]
Perilli, Mariagrazia [> >]
2018
Antimicrobial Agents and Chemotherapy
American Society for Microbiology
62
8
Yes (verified by ORBi)
International
0066-4804
1098-6596
DC
[en] NDM ; kinetic ; metallo-beta-lactamase
[en] New Delhi metallo- beta-lactamase 1 (NDM-1) is a subclass B1 metallo-beta -
lactamase that exhibits a broad spectrum of activity against beta -lactam antibiotics. Here
we report the kinetic study of 6 Q119X variants obtained by site-directed mutagenesis
of NDM-1. All Q119X variants were able to hydrolyze carbapenems, penicillins and first-,
second-, third-, and fourth-generation cephalosporins very efficiently. In particular,
Q119E, Q119Y, Q119V, and Q119K mutants showed improvements in kcat/Km values for
penicillins, compared with NDM-1. The catalytic efficiencies of the Q119K variant for
benzylpenicillin and carbenicillin were about 65- and 70-fold higher, respectively, than
those of NDM-1. The Q119K and Q119Y enzymes had kcat/Km values for ceftazidime
about 25- and 89-fold higher, respectively, than that of NDM-1.
Researchers ; Students ; General public
http://hdl.handle.net/2268/227009
10.1128/AAC.02541-17

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