The different inhibition mechanisms of OXA-1 and OXA-24 β-lactamases are determined by the stability of active site carboxylated lysine

Journal of Biological Chemistry

Volumn 289, Issue 9, 2014, Pages 6152-6164

  Che, Tao ^a   Bethel, Christopher R ^c   Pusztai Carey, Marianne ^a   Bonomo, Robert A ^a,b,c   Carey, Paul R ^a  

^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)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BIOCHEMICAL STUDIES; CATALYTIC EFFICIENCIES; GENERAL BASE; HYDROLYZED PRODUCTS; INHIBITION MECHANISMS; REACTION MECHANISM; WATER MOLECULE;

AMINO ACIDS; CARBOXYLATION; MOLECULES;

ENZYMES;

BETA LACTAMASE; BETA LACTAMASE OXA 1; BETA LACTAMASE OXA 24; CARBAPENEM DERIVATIVE; LYSINE; PIPERACILLIN; TAZOBACTAM; UNCLASSIFIED DRUG;

ANTIBIOTIC RESISTANCE; ANTIBIOTIC SENSITIVITY; ARTICLE; CONTROLLED STUDY; DECARBOXYLATION; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SYNTHESIS; MINIMUM INHIBITORY CONCENTRATION; PRIORITY JOURNAL; PROTEIN EXPRESSION; STRUCTURE ANALYSIS;

CARBOXYLATED LYSINE; CRYSTALLOGRAPHY; ENZYME MECHANISMS; OXA-1; OXA-24; PENEMS; PHYSICAL METHODS; RAMAN SPECTROSCOPY; UV SPECTROSCOPY;

ACINETOBACTER BAUMANNII; ANTI-BACTERIAL AGENTS; BETA-LACTAMASES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; ENZYME INHIBITORS; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; LYSINE; THIENAMYCINS;

EID: 84896855686     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.533562     Document Type: Article

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