Regulation of tryptophan synthase by temperature, monovalent cations, and an allosteric ligand. Evidence from arrhenius plots, absorption spectra, and primary kinetic isotope effects

Biochemistry

Volumn 39, Issue 16, 2000, Pages 4692-4703

  Fan, Ying Xin ^a,b   McPhie, Peter ^a   Miles, Edith Wilson ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b AMERICAN RED CROSS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

TRYPTOPHAN SYNTHASE;

ARTICLE; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME REGULATION; ENZYME STABILITY; ESCHERICHIA COLI; HYDROPHOBICITY; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; SALMONELLA TYPHIMURIUM;

ALLOSTERIC REGULATION; ALLOSTERIC SITE; CATALYSIS; CATIONS, MONOVALENT; CESIUM; CHLORIDES; DEUTERIUM; ENZYME ACTIVATION; GLYCEROPHOSPHATES; GUANIDINE; KINETICS; LIGANDS; PROTEIN CONFORMATION; SALMONELLA TYPHIMURIUM; SERINE; SODIUM CHLORIDE; SPECTRUM ANALYSIS; TEMPERATURE; THERMODYNAMICS; TRYPTOPHAN SYNTHASE;

ARRHENIUS; ESCHERICHIA COLI; SALMONELLA TYPHIMURIUM; TYPHIMURIUM;

EID: 0034712647     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9921586     Document Type: Article

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