βQ114N and βT110V mutations reveal a critically important role of the substrate α-carboxylate site in the reaction specificity of tryptophan synthase

Biochemistry

Volumn 46, Issue 49, 2007, Pages 14100-14116

  Blumenstein, Lars ^a   Domratcheva, Tatiana ^a   Niks, Dimitri ^b   Ngo, Huu ^b   Seidel, Ralf ^c   Dunn, Michael F ^b   Schlichting, Ilme ^a  

^a MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING SITES; CATALYST ACTIVITY; MOLECULAR INTERACTIONS; MUTAGENESIS; PROTEINS; SUBSTRATES;

ALLOSTERIC SIGNALS; CARBOXYLATE SITE; TRYPTOPHAN SYNTHASE;

ENZYME ACTIVITY;

CARBOXYLIC ACID; CARBOXYLIC ACID DERIVATIVE; MUTANT PROTEIN; PYRIDOXAL 5 PHOSPHATE; TRYPTOPHAN SYNTHASE; INDOLE DERIVATIVE; SERINE;

ABSORPTION; ALLOSTERISM; ARTICLE; CHEMICAL REACTION; CHEMICAL STRUCTURE; ENZYME SPECIFICITY; LIGAND BINDING; MUTATION; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN STRUCTURE; STEADY STATE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; AMINO ACID SUBSTITUTION; CIRCULAR DICHROISM; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; PROTEIN CONFORMATION; SALMONELLA TYPHIMURIUM; ULTRAVIOLET SPECTROPHOTOMETRY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SUBSTITUTION; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; INDOLES; KINETICS; MODELS, MOLECULAR; PROTEIN CONFORMATION; SALMONELLA TYPHIMURIUM; SERINE; SPECTROPHOTOMETRY, ULTRAVIOLET; TRYPTOPHAN SYNTHASE;

EID: 37049025637     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7008568     Document Type: Article

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