Τίτλος:
Increased hydrolysis of oximino-β-lactams by CMY-107, a Tyr199Cys mutant form of CMY-2 produced by Escherichia coli
Γλώσσες Τεκμηρίου:
Αγγλικά
Περίληψη:
The cephalosporinase CMY-107, a Tyr199Cys mutant form of CMY-2 encoded by an IncI self-transferable plasmid carried by an Escherichia coli clinical strain, was characterized. The enzyme hydrolyzed oximino-cephalosporins and aztreonam more efficiently than CMY-2 did. © 2015, American Society for Microbiology. All Rights Reserved.
Συγγραφείς:
Kotsakis, S.D.
Miriagou, V.
Vetouli, E.E.
Bozavoutoglou, E.
Lebessi, E.
Tzelepi, E.
Tzouvelekis, L.S.
Περιοδικό:
Antimicrobial Agents and Chemotherapy
Εκδότης:
American Society for Microbiology
Λέξεις-κλειδιά:
aminoglycoside; aztreonam; beta lactam antibiotic; cefepime; cefuroxime; cephalosporinase; cloxacillin; cotrimoxazole; imipenem; oximino beta lactam; quinolone derivative; tazobactam; unclassified drug; antiinfective agent; beta lactamase; beta-lactamase CMY-2, E coli; cephalosporin derivative; cysteine; Escherichia coli protein; isoenzyme; tyrosine, antibiotic resistance; antibiotic sensitivity; Article; bacterial strain; bacterium isolate; drug hydrolysis; enzyme activity; extended spectrum beta lactamase producing Escherichia coli; human; isoelectric focusing; isoelectric point; kinetic parameters; minimum inhibitory concentration; multilocus sequence typing; nonhuman; principal component analysis; priority journal; restriction fragment length polymorphism; Salmonella enterica serovar Typhimurium; site directed mutagenesis; structure activity relation; thermostability; ultraviolet spectrophotometry; vesicoureteral reflux; amino acid substitution; chemistry; enzyme specificity; enzymology; Escherichia coli; Escherichia coli infection; gene expression; gene locus; genetics; hydrolysis; isolation and purification; kinetics; metabolism; microbial sensitivity test; microbiology; molecular model; mutation; plasmid; protein secondary structure; protein tertiary structure, Amino Acid Substitution; Anti-Bacterial Agents; beta-Lactamases; Cephalosporins; Cysteine; Escherichia coli; Escherichia coli Infections; Escherichia coli Proteins; Gene Expression; Genetic Loci; Humans; Hydrolysis; Isoenzymes; Kinetics; Microbial Sensitivity Tests; Models, Molecular; Multilocus Sequence Typing; Mutation; Plasmids; Protein Structure, Secondary; Protein Structure, Tertiary; Substrate Specificity; Tyrosine
DOI:
10.1128/AAC.01793-15
