Circular permutation in the ω-loop of TEM-1 β-lactamase results in improved activity and altered substrate specificity

PLoS ONE

Volumn 7, Issue 4, 2012, Pages

  Guntas, Gurkan ^a,b   Kanwar, Manu ^a   Ostermeier, Marc ^a  

^a Johns Hopkins University   (United States)

^b UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CEFALOTIN; CEFAZOLIN; CEFOTAXIME; GLUTAMINE; MALTOSE BINDING PROTEIN; PERIPLASMIC PROTEIN; PROTEIN TEM 1; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; BETA LACTAMASE TEM 1; BETA-LACTAMASE TEM-1; ESCHERICHIA COLI PROTEIN;

AMINO TERMINAL SEQUENCE; ANTIBIOTIC RESISTANCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CODON; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ESCHERICHIA COLI; GENE INSERTION; GENE SEQUENCE; HYDROLYSIS; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; POLYMERASE CHAIN REACTION; PROTEIN DOMAIN; PROTEIN EXPRESSION; STOP CODON; CHEMISTRY; DIRECTED MOLECULAR EVOLUTION; DRUG EFFECT; ENZYMOLOGY; GENE LIBRARY; GENETICS; MICROBIOLOGICAL EXAMINATION; MOLECULAR CLONING; MOLECULAR GENETICS; MUTAGENESIS; NUCLEOTIDE SEQUENCE; PROTEIN MOTIF;

AMINO ACID MOTIFS; ANTI-BACTERIAL AGENTS; BASE SEQUENCE; BETA-LACTAM RESISTANCE; BETA-LACTAMASES; CATALYTIC DOMAIN; CEFOTAXIME; CLONING, MOLECULAR; DIRECTED MOLECULAR EVOLUTION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE LIBRARY; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; MUTAGENESIS; SUBSTRATE SPECIFICITY;

EID: 84859833076     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0035998     Document Type: Article

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