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Volumn 40, Issue 6, 2001, Pages 1640-1650

Familial mutations and zinc stoichiometry determine the rate-limiting step of nitrocefin hydrolysis by metallo-β-lactamase from Bacteroides fragilis

(3) Fast, W a Wang, Z a Benkovic, S J a

a PENNSYLVANIA STATE UNIVERSITY (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BETA LACTAMASE; METALLO BETA LACTAMASE; NITROCEFIN; UNCLASSIFIED DRUG; ZINC;

ANTIBIOTIC RESISTANCE; ARTICLE; BACTERIAL MUTATION; BACTEROIDES FRAGILIS; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME SPECIFICITY; HYDROLYSIS; METAL BINDING; MOLECULAR EVOLUTION; NONHUMAN; PRIORITY JOURNAL; STOICHIOMETRY;

AMINO ACID SUBSTITUTION; ARGININE; BACILLUS CEREUS; BACTEROIDES FRAGILIS; BETA-LACTAMASES; CATALYSIS; CEPHALOSPORINS; COBALT; CYSTEINE; DIALYSIS; HYDROLYSIS; INDICATORS AND REAGENTS; KINETICS; METALLOPROTEINS; MULTIGENE FAMILY; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; RESORCINOLS; SPECTROPHOTOMETRY, ATOMIC; ZINC;

BACILLUS CEREUS; BACTERIA (MICROORGANISMS); BACTEROIDES FRAGILIS;

EID: 0035852802 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi001860v Document Type: Article

Times cited : (76)

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