Combinatorial active-site variants confer sustained clavulanate resistance in BlaC β-lactamase from Mycobacterium tuberculosis

Protein Science

Volumn 24, Issue 4, 2015, Pages 534-544

  Egesborg, Philippe ^a   Carlettini, Hélène ^a   Volpato, Jordan P ^a   Doucet, Nicolas ^a,b  

^a UNIVERSITÉ LAVAL   (Canada)

^b MCGILL UNIVERSITY   (Canada)

Author keywords

antibiotic resistance; Class A lactamases; clavulanic acid; combinatorial mutagenesis; Mycobacterium tuberculosis; site directed mutagenesis; lactam

Indexed keywords

BETA LACTAMASE; BETA LACTAMASE BLAC; CEFALOTIN; CEFOTAXIME; CEFTRIAXONE; CEPHALOSPORIN DERIVATIVE; CLAVULANIC ACID; HYDROLASE; PENICILLINASE; UNCLASSIFIED DRUG;

ANTIBIOTIC RESISTANCE; ANTIBIOTIC SENSITIVITY; ARTICLE; BACTERIAL GROWTH; CLINICAL EFFECTIVENESS; CONCENTRATION PROCESS; DRUG EFFICACY; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME STRUCTURE; IN VITRO STUDY; INHIBITOR RESISTANCE; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; CHEMISTRY; DRUG EFFECTS; GENETICS; KINETICS; METABOLISM; MOLECULAR MODEL; MUTATION;

BETA-LACTAMASES; CLAVULANIC ACID; DRUG RESISTANCE, BACTERIAL; KINETICS; MODELS, MOLECULAR; MUTATION; MYCOBACTERIUM TUBERCULOSIS;

EID: 84940948825     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2617     Document Type: Article

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