Kinetics of Turnover of Cefotaxime by the Enterobacter cloacae P99 and GC1 β-Lactamases: Two Free Enzyme Forms of the P99 β-Lactamase Detected by a Combination of Pre- and Post-Steady State Kinetics

Biochemistry

Volumn 43, Issue 9, 2004, Pages 2664-2672

  Kumar, Sanjai ^a   Adediran, S A ^a   Nukaga, Michiyoshi ^b   Pratt, R F ^a  

^a WESLEYAN UNIVERSITY   (United States)

^b UNIVERSITY OF CONNECTICUT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOCHEMISTRY; CATALYST ACTIVITY; CONFORMATIONS; ENZYME INHIBITION; HYDROLYSIS;

HYDROLYSIS RESISTANCE; SIDE CHAINS;

ENZYME KINETICS;

AMMONIUM SULFATE; BETA LACTAMASE; CEFALOTIN; CEFOTAXIME; DEPSIPEPTIDE; DIHYDROTHIAZINE; P99 BETA LACTAMASE; THIAZINE DERIVATIVE; UNCLASSIFIED DRUG;

ANTIBIOTIC RESISTANCE; ARTICLE; CATALYSIS; DRUG BINDING; DRUG HYDROLYSIS; DRUG STRUCTURE; ENTEROBACTER CLOACAE; ENZYME ACTIVITY; NONHUMAN; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; REACTION ANALYSIS; STEADY STATE; TURNOVER TIME;

ACYLATION; BETA-LACTAMASES; CATALYSIS; CEFOTAXIME; CEFUROXIME; CEPHALOTHIN; ENTEROBACTER CLOACAE; HYDROLYSIS; KINETICS; MODELS, CHEMICAL; PROTEIN BINDING; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ENTEROBACTER CLOACAE; NEGIBACTERIA;

EID: 1542267769     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi030212j     Document Type: Article

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