Lysyl-tRNA synthetase from Bacillus stearothermophilus: The Trp314 residue is shielded in a non-polar environment and is responsible for the fluorescence changes observed in the amino acid activation reaction

Journal of Molecular Biology

Volumn 325, Issue 4, 2003, Pages 677-695

  Takita, Teisuke ^a   Nakagoshi, Makoto ^a   Inouye, Kuniyo ^a   Tonomura, Ben'ichiro ^b  

^a KYOTO UNIVERSITY   (Japan)

^b KINKI UNIVERSITY   (Japan)

Author keywords

Class IIb synthetase; Fluorescence; Lysyl tRNA synthetase; States of Trp residue(s); UV absorption difference spectra

Indexed keywords

ADENOSINE TRIPHOSPHATE; ENZYME; LYSINE; LYSINE TRANSFER RNA LIGASE; PHENYLALANINE; TRYPTOPHAN;

AMINO ACID COMPOSITION; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CATALYSIS; ENZYME ACTIVITY; FLUORESCENCE; FLUOROMETRY; GEOBACILLUS STEAROTHERMOPHILUS; MICROENVIRONMENT; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; ULTRAVIOLET SPECTROSCOPY; WILD TYPE;

GEOBACILLUS STEAROTHERMOPHILUS;

EID: 0037462877     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01238-X     Document Type: Article

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