Structural basis for different substrate profiles of two closely related class D β-lactamases and their inhibition by halogens

Biochemistry

Volumn 54, Issue 21, 2015, Pages 3370-3380

  Stojanoski, Vlatko ^a   Chow, Dar Chone ^a   Fryszczyn, Bartlomiej ^a   Hu, Liya ^a   Nordmann, Patrice ^b   Poirel, Laurent ^b   Sankaran, Banumathi ^c   Prasad, B V Venkataram ^a   Palzkill, Timothy ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b University of Fribourg   (Switzerland)

^c LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANTIBIOTICS; CARBOXYLATION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME INHIBITION; ENZYMES; HYDROLYSIS; SEWAGE TREATMENT PLANTS; X RAY CRYSTALLOGRAPHY;

CONFORMATIONAL CHANGE; DIFFERENT SUBSTRATES; INHIBITION ASSAYS; KINETIC ANALYSIS; STRUCTURAL DIFFERENCES; SUBSTRATE PROFILE; SUBSTRATE SPECIFICITY; SUBSTRATE-BINDING SITES;

SUBSTRATES;

BETA LACTAMASE; CARBAPENEM DERIVATIVE; CEFTAZIDIME; HALOGEN; IODIDE; OXA 163 ENZYME; OXA 48 ENZYME; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; CEPHALOSPORIN DERIVATIVE; ENZYME INHIBITOR; OXACILLINASE;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DECARBOXYLATION; ENZYME INHIBITION; ENZYME INHIBITION ASSAY; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; MOLECULAR MODEL; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY; CHEMISTRY; ENTEROBACTER CLOACAE; ENTEROBACTERIACEAE INFECTION; ENZYME ACTIVE SITE; ENZYMOLOGY; HUMAN; KLEBSIELLA INFECTION; KLEBSIELLA PNEUMONIAE; METABOLISM; MICROBIOLOGY; MOLECULAR DOCKING; PROTEIN CONFORMATION;

ANTI-BACTERIAL AGENTS; BETA-LACTAMASES; CARBAPENEMS; CATALYTIC DOMAIN; CEFTAZIDIME; CEPHALOSPORINS; ENTEROBACTER CLOACAE; ENTEROBACTERIACEAE INFECTIONS; ENZYME INHIBITORS; HUMANS; IODIDES; KLEBSIELLA INFECTIONS; KLEBSIELLA PNEUMONIAE; MOLECULAR DOCKING SIMULATION; PROTEIN CONFORMATION;

EID: 84930613804     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00298     Document Type: Article

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