Cold-induced enzyme inactivation: How does cooling lead to pyridoxal phosphate-aldimine bond cleavage in tryptophanase?

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1594, Issue 2, 2002, Pages 335-340

  Erez, Tali ^a   Gdalevsky, Garik Ya ^a   Hariharan, Chithra ^a   Pines, Dina ^a   Pines, Ehud ^a   Phillips, Robert S ^b   Cohen Luria, Rivka ^a   Parola, Abraham H ^a  

^a BEN GURION UNIVERSITY OF THE NEGEV   (Israel)

^b UNIVERSITY OF GEORGIA   (United States)

Author keywords

Protein quaternary structure; Pyridoxal phosphate; Single photon spectrofluorometry; Time resolved fluorescence anisotropy; Tryptophanase; W330F mutant tryptophanase

Indexed keywords

DIMER; MUTANT PROTEIN; PYRIDOXAL 5 PHOSPHATE; TETRAMER; TRYPTOPHANASE;

ANISOTROPY; ARTICLE; CHEMICAL BOND; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; COOLING; DISSOCIATION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME INACTIVATION; ESCHERICHIA COLI; FLUORESCENCE ANALYSIS; HYDROPHOBICITY; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; SPECTROFLUOROMETRY; WILD TYPE;

ANISOTROPY; BINDING SITES; COLD; ENZYME STABILITY; MUTATION; PROTEIN CONFORMATION; PYRIDOXAL PHOSPHATE; ROTATION; SPECTROMETRY, FLUORESCENCE; TRYPTOPHANASE;

EID: 0037060470     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(01)00325-9     Document Type: Article

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