N152G,-S, and-T substitutions in CMY-2 β-lactamase increase catalytic efficiency for cefoxitin and inactivation rates for tazobactam

Antimicrobial Agents and Chemotherapy

Volumn 57, Issue 4, 2013, Pages 1596-1602

  Skalweit, Marion J ^a,b   Li, Mei ^a   Conklin, Benjamin C ^a   Taracila, Magdalena A ^a,b   Hutton, Rebecca A ^a  

^a LOUIS STOKES CLEVELAND VA MEDICAL CENTER   (United States)

^b CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APOENZYME; BETA LACTAMASE; BETA LACTAMASE CMY 2; CEFOXITIN; CEPHALOSPORINASE; PENICILLINASE; TAZOBACTAM; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; ASSAY; CATALYSIS; DRUG INACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; GENETIC VARIABILITY; IC 50; IN VITRO STUDY; MICHAELIS MENTEN KINETICS; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL;

ANTI-BACTERIAL AGENTS; BETA-LACTAMASES; CATALYSIS; CEFOXITIN; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MICROBIAL SENSITIVITY TESTS; PENICILLANIC ACID;

EID: 84875134188     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01334-12     Document Type: Article

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