Mg2+-free Bacillus stearothermophilus tryptophanyl-tRNA synthetase retains a major fraction of the overall rate enhancement for tryptophan activation

Journal of the American Chemical Society

Volumn 130, Issue 4, 2008, Pages 1488-1494

  Weinreb, Violetta ^a   Carter Jr , Charles W ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BINDING ENERGY; CATALYST ACTIVITY; CONCENTRATION (PROCESS); METAL IONS; RNA;

BACILLUS STEAROTHERMOPHILUS; BINDING AFFINITY; DIVALENT METAL IONS; NONLINEAR MODELS;

ENZYME ACTIVITY;

AMINO ACID TRANSFER RNA LIGASE; EDETIC ACID; MAGNESIUM ION; TRYPTOPHAN; ADENOSINE TRIPHOSPHATE; ION; LIGAND; MAGNESIUM; TRYPTOPHAN TRANSFER RNA LIGASE;

ARTICLE; BINDING AFFINITY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME MECHANISM; GEOBACILLUS STEAROTHERMOPHILUS; METAL BINDING; MOLECULAR INTERACTION; MOLECULAR MODEL; NONHUMAN; BIOCHEMISTRY; CATALYSIS; CHEMICAL MODEL; CHEMISTRY; ENZYMOLOGY; KINETICS; METABOLISM; METHODOLOGY; PHOSPHORYLATION; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

ADENOSINE TRIPHOSPHATE; BACILLUS STEAROTHERMOPHILUS; BIOCHEMISTRY; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; EDETIC ACID; IONS; KINETICS; LIGANDS; MAGNESIUM; MODELS, CHEMICAL; PHOSPHORYLATION; THERMODYNAMICS; TRYPTOPHAN; TRYPTOPHAN-TRNA LIGASE;

EID: 38649111324     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja076557x     Document Type: Article

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