Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "A tale of two mechanisms"

Biochemistry

Volumn 46, Issue 37, 2007, Pages 10517-10527

  Liu, Dali ^a   Pozharski, Edwin ^b   Lepore, Bryan W ^a,c   Fu, Mengmeng ^d   Silverman, Richard B ^d   Petsko, Gregory A ^a   Ringe, Dagmar ^a  

^a BRANDEIS UNIVERSITY   (United States)

^b UNIVERSITY OF MARYLAND   (United States)

^c Program in Bioorganic Chemistry   (United States)

^d NORTHWESTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COCRYSTALLIZATION; INACTIVATORS; PROTEIN STRUCTURE; STRUCTURAL MODELS;

ACTIVATION ANALYSIS; CRYSTALLIZATION KINETICS; ESCHERICHIA COLI; MOLECULAR MODELING; MOLECULAR STRUCTURE; PH;

ENZYME ACTIVITY;

4 AMINO 4,5 DIHYDRO 2 THIOPHENECARBOXYLIC ACID; ASPARTATE AMINOTRANSFERASE; LYSINE; PYRIDOXAL 5 PHOSPHATE; UNCLASSIFIED DRUG;

ARTICLE; COMPLEX FORMATION; COVALENT BOND; CRYSTALLIZATION; DENSITY; ENZYME ACTIVE SITE; ENZYME INACTIVATION; ESCHERICHIA COLI; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN STRUCTURE;

ASPARTATE AMINOTRANSFERASES; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENZYME ACTIVATION; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; PROTEIN STRUCTURE, SECONDARY; PYRIDOXAL PHOSPHATE; STATIC ELECTRICITY; THIOPHENES;

ESCHERICHIA COLI;

EID: 34548678883     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700663n     Document Type: Article

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