Structural Basis of Activity against Aztreonam and Extended Spectrum Cephalosporins for Two Carbapenem-Hydrolyzing Class D β-Lactamases from Acinetobacter baumannii

Biochemistry

Volumn 54, Issue 10, 2015, Pages 1976-1987

  Mitchell, Joshua M ^a   Clasman, Jozlyn R ^a   June, Cynthia M ^a   Kaitany, Kip Chumba J ^a   LaFleur, James R ^a   Taracila, Magdalena A ^b,c   Klinger, Neil V ^a   Bonomo, Robert A ^b,c   Wymore, Troy ^d   Szarecka, Agnieszka ^a   Powers, Rachel A ^a   Leonard, David A ^a  

^a GRAND VALLEY STATE UNIVERSITY   (United States)

^b CASE WESTERN RESERVE UNIVERSITY   (United States)

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

^d OAK RIDGE NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CHAINS; ENZYMES; HYDROLYSIS;

ANTIBIOTIC RESISTANCE; BINDING AFFINITIES; CAUSATIVE AGENTS; EXTENDED-SPECTRUM CEPHALOSPORINS; HYDROLYTIC ACTIVITIES; STEADY-STATE KINETICS; STRUCTURAL BASIS; SUBSTRATE PROFILE;

ANTIBIOTICS;

AZTREONAM; BACTERIAL ENZYME; BETA LACTAMASE; CARBAPENEM; CEFOTAXIME; CEFTAZIDIME; CEFTRIAXONE; CEPHALOSPORIN DERIVATIVE; DORIPENEM; HYDROLASE; OXACILLIN; BACTERIAL PROTEIN;

ACINETOBACTER BAUMANNII; ACYLATION; ANTIBIOTIC RESISTANCE; ARTICLE; BACTERIAL MUTATION; BACTERIAL STRAIN; BINDING AFFINITY; CHEMICAL BOND; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CONVERGENT EVOLUTION; CRYSTAL STRUCTURE; DEACYLATION; DENSITY; DRUG HYDROLYSIS; ENZYME ACTIVITY; ENZYME STRUCTURE; HYDROGEN BOND; LIGAND BINDING; MELTING POINT; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; PROTEIN STABILITY; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; STEADY STATE; THERMODYNAMICS; TURNOVER TIME; CHEMISTRY; ENZYMOLOGY; HYDROLYSIS; KINETICS; PROTEIN SECONDARY STRUCTURE;

ACINETOBACTER; ACINETOBACTER BAUMANNII;

ACINETOBACTER BAUMANNII; AZTREONAM; BACTERIAL PROTEINS; BETA-LACTAMASES; CEPHALOSPORINS; HYDROLYSIS; KINETICS; PROTEIN STRUCTURE, SECONDARY;

EID: 84925278264     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi501547k     Document Type: Article

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