Impact of remote mutations on metallo-β-lactamase substrate specificity: Implications for the evolution of antibiotic resistance

Protein Science

Volumn 14, Issue 3, 2005, Pages 765-774

  Oelschlaeger, Peter ^a   Mayo, Stephen L ^b   Pleiss, Juergen ^c  

^a California Institute of Technology HHMI   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^c UNIVERSITY OF STUTTGART   (Germany)

Author keywords

Enzyme evolution; Metallo lactamase; Metalloenzyme; Point mutation; Substrate specificity

Indexed keywords

AMPICILLIN; BETA LACTAMASE; CEFALOTIN; CEFOTAXIME; CEFTAZIDIME; IMIPENEM; NITROCEFIN; PENICILLIN G;

AMINO ACID SUBSTITUTION; ANTIBIOTIC RESISTANCE; ARTICLE; CATALYSIS; CHEMICAL STRUCTURE; ELECTRON; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME STABILITY; ESCHERICHIA COLI; EVOLUTIONARY ADAPTATION; HYDROLYSIS; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL;

BETA-LACTAMASES; DRUG DESIGN; DRUG RESISTANCE, BACTERIAL; ESCHERICHIA COLI; EVOLUTION; KINETICS; MUTATION; SUBSTRATE SPECIFICITY;

EID: 14144255746     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041093405     Document Type: Article

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