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Volumn 277, Issue 27, 2002, Pages 24744-24752
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Characterization of monomeric L1 metallo-β-lactamase and the role of the N-terminal extension in negative cooperativity and antibiotic hydrolysis
a
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Author keywords
[No Author keywords available]
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Indexed keywords
ANTIBIOTICS;
ENZYMES;
HYDROLYSIS;
MONOMERS;
SUBSTRATES SPECIFICITY;
BIOCHEMISTRY;
AMPICILLIN;
ANTIBIOTIC AGENT;
ASPARTIC ACID;
BETA LACTAM ANTIBIOTIC;
BETA LACTAMASE;
CEFALORIDINE;
CEFMETAZOLE;
CEFOTAXIME;
CEFOXITIN;
CEFTAZIDIME;
IMIPENEM;
MEROPENEM;
METALLO BETA LACTAMASE L1;
METHIONINE;
MUTANT PROTEIN;
NITROCEFIN;
PENICILLIN G;
TETRAMER;
UNCLASSIFIED DRUG;
AMINO ACID SUBSTITUTION;
AMINO TERMINAL SEQUENCE;
ARTICLE;
CONTROLLED STUDY;
DRUG HYDROLYSIS;
DRUG PROTEIN BINDING;
ENZYME ANALYSIS;
ENZYME SPECIFICITY;
ENZYME SUBSTRATE;
ENZYME SUBUNIT;
NONHUMAN;
PRIORITY JOURNAL;
SITE DIRECTED MUTAGENESIS;
STENOTROPHOMONAS MALTOPHILIA;
AMINO ACID SEQUENCE;
ANTI-BACTERIAL AGENTS;
BASE SEQUENCE;
BETA-LACTAMASES;
BIOTRANSFORMATION;
CRYSTALLOGRAPHY, X-RAY;
DNA PRIMERS;
KINETICS;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN SUBUNITS;
RECOMBINANT PROTEINS;
STENOTROPHOMONAS MALTOPHILIA;
SUBSTRATE SPECIFICITY;
STENOTROPHOMONAS;
STENOTROPHOMONAS MALTOPHILIA;
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EID: 0037025381
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M201524200 Document Type: Article |
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Times cited : (35)
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References (52)
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