Mutagenesis of zinc ligand residue Cys221 reveals plasticity in the IMP-1 metallo-β-lactamase active site

Antimicrobial Agents and Chemotherapy

Volumn 56, Issue 11, 2012, Pages 5667-5677

  Horton, Lori B ^a   Shanker, Sreejesh ^a   Mikulski, Rose ^a   Brown, Nicholas G ^a   Phillips, Kevin J ^b   Lykissa, Ernest ^c   Venkataram Prasad, B V ^a   Palzkill, Timothy ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b HOUSTON METHODIST RESEARCH INSTITUTE   (United States)

^c ExperTox   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN; AZTREONAM; CEFOTAXIME; CEFTAZIDIME; CYSTEINE; GLYCINE; IMIPENEM; INOSINE PHOSPHATE; MEROPENEM; METAL CHELATE; METALLO BETA LACTAMASE; THIOL; ZINC BINDING PROTEIN; ZINC ION;

ANTIBIOTIC SENSITIVITY; ARTICLE; BACTERIAL GENE; BINDING AFFINITY; BINDING SITE; CATALYSIS; ENZYME STRUCTURE; ESCHERICHIA COLI; HYDROLYSIS; IMP 1 GENE; IN VIVO STUDY; MINIMUM INHIBITORY CONCENTRATION; MOLECULAR MODEL; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; STEADY STATE;

AMINO ACID SUBSTITUTION; BETA-LACTAMASES; BETA-LACTAMS; CATALYTIC DOMAIN; CYSTEINE; ESCHERICHIA COLI; GLYCINE; KINETICS; LIGANDS; MICROBIAL SENSITIVITY TESTS; MODELS, MOLECULAR; MUTAGENESIS; PROTEIN BINDING; RECOMBINANT PROTEINS; WATER; ZINC;

EID: 84868028191     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01276-12     Document Type: Article

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