Two laboratory mutant forms, TEM-149H240 and TEM-149H164-H240, of the TEM-149 extended-spectrum β-lactamase enzyme were constructed by site-directed mutagenesis. TEM-149H240 and TEM-149H164-H240 were similar in kinetic behavior, except with respect to benzylpenicillin and ceftazidime. Molecular modeling of the two mutant enzymes demonstrated the role of histidine at position 240 in the reduction of the affinity of the enzyme for ceftazidime
Replacement R164H and V240H by site-directed mutagenesis of TEM-149 ESBL: kinetic analysis of TEM-149H240 and TEM-149H164-H240 laboratory mutants
PERILLI, MARIAGRAZIA;CELENZA, GIUSEPPE;PELLEGRINI, CRISTINA;SEGATORE, Bernardetta;AMICOSANTE, Gianfranco
2013-01-01
Abstract
Two laboratory mutant forms, TEM-149H240 and TEM-149H164-H240, of the TEM-149 extended-spectrum β-lactamase enzyme were constructed by site-directed mutagenesis. TEM-149H240 and TEM-149H164-H240 were similar in kinetic behavior, except with respect to benzylpenicillin and ceftazidime. Molecular modeling of the two mutant enzymes demonstrated the role of histidine at position 240 in the reduction of the affinity of the enzyme for ceftazidimeFile in questo prodotto:
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