Pyridoxal phosphate binding to wild type, W330F, and C298S mutants of Escherichia coli apotryptophanase: Unraveling the cold inactivation

FEBS Letters

Volumn 433, Issue 3, 1998, Pages 279-282

  Erez, Tali ^a   Phillips, Robert S ^b   Parola, Abraham H ^a  

^a BEN GURION UNIVERSITY OF THE NEGEV   (Israel)

^b UNIVERSITY OF GEORGIA   (United States)

Author keywords

Cold inactivation; Protein conformation and quaternary structure; Pyridoxal phosphate; Site directed mutagenesis; Stopped flow kinetics; Tryptophanase

Indexed keywords

ESCHERICHIA COLI;

APOENZYME; PYRIDOXAL 5 PHOSPHATE; RECOMBINANT PROTEIN; TRYPTOPHANASE;

ARTICLE; BINDING SITE; CHEMICAL MODEL; CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; KINETICS; METABOLISM; POINT MUTATION; SITE DIRECTED MUTAGENESIS;

APOENZYMES; BINDING SITES; ESCHERICHIA COLI; KINETICS; MODELS, CHEMICAL; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PYRIDOXAL PHOSPHATE; RECOMBINANT PROTEINS; TRYPTOPHANASE;

EID: 0032555330     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(98)00931-4     Document Type: Article

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