R164H and V240H replacements by site-directed mutagenesis of TEM-149 extended-spectrum beta-lactamase: kinetic analysis of TEM-149H240 and TEM-149H164-H240 laboratory mutants.
[en] Two laboratory mutant forms, TEM-149(H240) and TEM-149(H164-H240), of the TEM-149 extended-spectrum beta-lactamase enzyme were constructed by site-directed mutagenesis. TEM-149(H240) and TEM-149(H164-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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Perilli, Mariagrazia
Celenza, Giuseppe
Mercuri, Paola ; Université de Liège > Département des sciences de la vie > Macromolécules biologiques
R164H and V240H replacements by site-directed mutagenesis of TEM-149 extended-spectrum beta-lactamase: kinetic analysis of TEM-149H240 and TEM-149H164-H240 laboratory mutants.
Publication date :
2013
Journal title :
Antimicrobial Agents and Chemotherapy
ISSN :
0066-4804
eISSN :
1098-6596
Publisher :
American Society for Microbiology, Washington, United States - District of Columbia
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