The Drug-Resistant Variant P167S Expands the Substrate Profile of CTX-M β-Lactamases for Oxyimino-Cephalosporin Antibiotics by Enlarging the Active Site upon Acylation

Biochemistry

Volumn 56, Issue 27, 2017, Pages 3443-3453

  Patel, Meha P ^a   Hu, Liya ^a   Stojanoski, Vlatko ^a   Sankaran, Banumathi ^b   Prasad, B V Venkataram ^a   Palzkill, Timothy ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLATION; ANTIBIOTICS; CRYSTALLOGRAPHY; HYDROLYSIS; X RAY CRYSTALLOGRAPHY;

ACYL-ENZYME COMPLEX; AMINOTHIAZOLE; CEPHALOSPORIN ANTIBIOTICS; CONFORMATIONAL CHANGE; DRUG-RESISTANT BACTERIA; ENZYME-SUBSTRATE COMPLEXES; MUTANT ENZYMES; SUBSTRATE PROFILE;

ENZYMES;

AMINOTHIAZOLE; BETA LACTAMASE CTX M; CEPHALOSPORIN; GLUTAMIC ACID; OXYIMINO CEPHALOSPORIN; PROLINE; SERINE; THIAZOLE; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; APOENZYME; BETA LACTAMASE; BETA-LACTAMASE CTX-M-14; BETA-LACTAMASE CTX-M-14, E COLI; CEFTAZIDIME; CEPHALOSPORIN DERIVATIVE; ESCHERICHIA COLI PROTEIN; LIGAND; OXIME; RECOMBINANT PROTEIN;

ACYLATION; AMINO ACID SUBSTITUTION; ANTIBIOTIC RESISTANCE; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; COVALENT BOND; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME METABOLISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; GENE MUTATION; HYDROGEN BOND; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY; CHEMISTRY; DRUG EFFECTS; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; METABOLISM; MOLECULAR MODEL; MULTIDRUG RESISTANCE; POINT MUTATION; PROTEIN CONFORMATION; SITE DIRECTED MUTAGENESIS;

ACYLATION; AMINO ACID SUBSTITUTION; ANTI-BACTERIAL AGENTS; APOENZYMES; BETA-LACTAMASES; CATALYTIC DOMAIN; CEFTAZIDIME; CEPHALOSPORINS; CRYSTALLOGRAPHY, X-RAY; DRUG RESISTANCE, MULTIPLE, BACTERIAL; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROLYSIS; LIGANDS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIMES; POINT MUTATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 85023166908     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.7b00176     Document Type: Article

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