The catalytic efficiency (kcat/Km) of the class A β-lactamase Toho-1 correlates with the thermal stability of its catalytic intermediate analog

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1804, Issue 4, 2010, Pages 684-691

  Nitanai, Yasushi ^a   Shimamura, Tatsuro ^a   Uchiyama, Takuro ^a   Ishii, Yoshikazu ^b   Takehira, Michiyo ^a   Yutani, Katsuhide ^a   Matsuzawa, Hiroshi ^c   Miyano, Masashi ^a  

^a Harima Institute ^*  (Japan)

^b University of Tokyo   (Japan)

^c AOMORI UNIVERSITY   (Japan)

Author keywords

lactam antibiotics; Acyl intermediate; CTX M type lactamase; Differential scanning calorimetry; Thermal stability; Toho 1

Indexed keywords

AMOXICILLIN; AMPICILLIN; AZTREONAM; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CEFALEXIN; CEFALOTIN; CEFCAPENE; CEFEPIME; CEFOTAXIME; CEFOTIAM; CEFSULODIN; CEFTAZIDIME; CEFUROXIME; PENICILLIN G; TOHO 1 PROTEIN; UNCLASSIFIED DRUG; BETA LACTAMASE TOHO 1, E COLI; BETA-LACTAMASE TOHO-1, E COLI; ESCHERICHIA COLI PROTEIN; MUTANT PROTEIN; RECOMBINANT PROTEIN;

ARTICLE; CATALYSIS; DEACYLATION; DENATURATION; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVITY; ENZYME STABILITY; HYDROLYSIS; HYDROLYSIS KINETICS; PRIORITY JOURNAL; TEMPERATURE; THERMOSTABILITY; ACYLATION; AMINO ACID SUBSTITUTION; CHEMISTRY; DRUG DESIGN; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; KINETICS; METABOLISM; SITE DIRECTED MUTAGENESIS; THERMODYNAMICS;

ACYLATION; AMINO ACID SUBSTITUTION; AZTREONAM; BETA-LACTAMASES; CALORIMETRY, DIFFERENTIAL SCANNING; CATALYSIS; CEFTAZIDIME; DRUG DESIGN; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 76849096440     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.10.023     Document Type: Article

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