Relocation of the catalytic carboxylate group in class A β-lactamase: The structure and function of the mutant enzyme Glu166→Gln:Asn170→Asp

Protein Engineering

Volumn 12, Issue 7, 1999, Pages 573-579

  Chen, Celia C H ^a   Herzberg, Osnat ^a  

^a UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE   (United States)

Author keywords

Site directed mutagenesis; X ray structure; lactam kinetics; lactamase

Indexed keywords

AMMONIUM SULFATE; ASPARTIC ACID; BACTERIAL ENZYME; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CARBOXYLIC ACID DERIVATIVE; GLUTAMIC ACID; GLYCINE; MUTANT PROTEIN; NITROCEFIN; PENICILLIN G;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DEACYLATION; DRUG HYDROLYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME KINETICS; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; X RAY CRYSTALLOGRAPHY;

EID: 0032804318     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/12.7.573     Document Type: Article

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