Cleavage of Escherichia coli tryptophan indole-lyase by trypsin at Lys406 affects the transmission of conformational changes associated with monovalent cation activation

European Journal of Biochemistry

Volumn 255, Issue 2, 1998, Pages 508-515

  Phillips, Robert S ^a   Doshi, Kokila J ^a  

^a UNIVERSITY OF GEORGIA   (United States)

Author keywords

Monovalent cation; Pyridoxal 5' phosphate; Stopped flow spectrophotometry; Trypsin; Tryptophan indole lyase

Indexed keywords

LYASE; TRYPTOPHAN; TRYPTOPHANASE;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME ACTIVATION; ENZYME ACTIVITY; ESCHERICHIA COLI; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MOLECULAR WEIGHT; PRIORITY JOURNAL;

EID: 0032527734     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2550508.x     Document Type: Article

References (32)

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