Exploring the role of a conserved class A residue in the Ω-loop of KPC-2 β-lactamase: A mechanism for ceftazidime hydrolysis

Journal of Biological Chemistry

Volumn 287, Issue 38, 2012, Pages 31783-31793

  Levitt, Peter S ^a   Papp Wallace, Krisztina M ^a,c   Taracila, Magdalena A ^a   Hujer, Andrea M ^a,c   Winkler, Marisa L ^a,c   Smith, Kerri M ^d   Xu, Yan ^d   Harris, Michael E ^b   Bonomo, Robert A ^a,c  

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

^b CASE WESTERN RESERVE UNIVERSITY   (United States)

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

^d CLEVELAND STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CD SPECTROSCOPY; CEFTAZIDIME; CLASS A; CONFORMATIONAL CHANGE; CONSERVED RESIDUES; DEACYLATION; GRAM-NEGATIVE BACTERIA; LACTAMASES; LOOP STRUCTURE; MINIMUM INHIBITORY CONCENTRATION; RATE LIMITING; STEADY STATE; WILD TYPES;

AMINO ACIDS; ANTIBIOTICS; CIRCULAR DICHROISM SPECTROSCOPY; ENZYMES; ESCHERICHIA COLI; MASS SPECTROMETRY;

HYDROLYSIS;

AMPICILLIN; ARGININE; AZTREONAM; BETA LACTAMASE; CEFALOTIN; CEFEPIME; CEFOTAXIME; CEFOXITIN; CEFTAZIDIME; CHLORAMPHENICOL; IMIPENEM; NITROCEFIN; PROTEIN KPC 2; PROTEIN VARIANT; SOLVENT; UNCLASSIFIED DRUG;

ACYLATION; AMINO ACID SUBSTITUTION; ANTIBIOTIC RESISTANCE; ARTICLE; BIOACCUMULATION; CIRCULAR DICHROISM; CONTROLLED STUDY; DEACYLATION; DRUG HYDROLYSIS; ENZYME CONFORMATION; ENZYME STRUCTURE; ESCHERICHIA COLI; KINETICS; MASS SPECTROMETRY; MINIMUM INHIBITORY CONCENTRATION; MOLECULAR MODEL; MOLECULAR PROBE; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; RESIDUE ANALYSIS; SITE SATURATION MUTAGENESIS; STEADY STATE;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; BETA-LACTAMASES; CEFTAZIDIME; CIRCULAR DICHROISM; HYDROLYSIS; KINETICS; KLEBSIELLA PNEUMONIAE; MASS SPECTROMETRY; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 84866389246     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.348540     Document Type: Article

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