Characterization and mutagenesis of the recombinant N-acetylneuraminate lyase from Clostridium perfringens: Insights into the reaction mechanism

European Journal of Biochemistry

Volumn 268, Issue 13, 2001, Pages 3831-3839

  Krüger, Dorothea ^a   Schauer, Roland ^a   Traving, Christina ^a  

^a UNIVERSITY OF KIEL   (Germany)

Author keywords

Clostridium perfringens; Mutagenesis; N acetylneuraminic acid; Reaction mechanism; Sialate pyruvate lyase

Indexed keywords

ASPARTIC ACID; BACTERIAL ENZYME; GLUTAMIC ACID; HYBRID PROTEIN; HYDROXYL GROUP; LYSINE; METAL CHELATE; N ACETYLNEURAMINATE LYASE; SCHIFF BASE; TYROSINE; UNCLASSIFIED DRUG;

ANION EXCHANGE CHROMATOGRAPHY; ARTICLE; CATALYSIS; CLOSTRIDIUM PERFRINGENS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME PURIFICATION; GENE EXPRESSION; KINETICS; NONHUMAN; PH; PRIORITY JOURNAL; PROTON TRANSPORT; REACTION ANALYSIS; SITE DIRECTED MUTAGENESIS; TEMPERATURE;

AMINO ACID SUBSTITUTION; CLONING, MOLECULAR; CLOSTRIDIUM PERFRINGENS; ENZYME STABILITY; ESCHERICHIA COLI; HEAT; HYDROGEN-ION CONCENTRATION; KINETICS; MUTAGENESIS, SITE-DIRECTED; OXO-ACID-LYASES; RECOMBINANT PROTEINS; THERMODYNAMICS;

EID: 0034819577     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2001.02297.x     Document Type: Article

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