Large scale dynamics of the michaelis complex in Bacillus stearothermophilus lactate dehydrogenase revealed by a single-tryptophan mutant study

Biochemistry

Volumn 52, Issue 11, 2013, Pages 1886-1892

  Nie, Beining ^a   Deng, Hua ^a   Desamero, Ruel ^b   Callender, Robert ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b CITY UNIVERSITY OF NEW YORK   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE RESIDUES; BACILLUS STEAROTHERMOPHILUS; CATALYTIC MECHANISMS; LACTATE DEHYDROGENASE; LARGE-SCALE DYNAMICS; MICHAELIS COMPLEX; STRUCTURAL CHANGE; TEMPERATURE JUMP;

BACTERIOLOGY; CATALYSIS; PROTEINS; QUANTUM CHEMISTRY;

AMINO ACIDS;

LACTATE DEHYDROGENASE; OXAMIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; TRYPTOPHAN;

ARTICLE; CATALYST; ENERGY TRANSFER; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE; GEOBACILLUS STEAROTHERMOPHILUS; LARGE SCALE PRODUCTION; MICHAELIS CONSTANT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; QUANTUM YIELD; TEMPERATURE;

CATALYTIC DOMAIN; GEOBACILLUS STEAROTHERMOPHILUS; KINETICS; L-LACTATE DEHYDROGENASE; MODELS, MOLECULAR; NAD; OXAMIC ACID; POINT MUTATION; PROTEIN CONFORMATION; TEMPERATURE; TRYPTOPHAN;

GEOBACILLUS STEAROTHERMOPHILUS;

EID: 84875408991     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3017125     Document Type: Article

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