Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures

Journal of Biological Chemistry

Volumn 274, Issue 27, 1999, Pages 19181-19187

  Alvarez, Marco ^a   Wouters, Johan ^b   Maes, Dominique ^c   Mainfroid, Véronique ^a   Rentier Delrue, Françoise ^a   Wyns, Lode ^c   Depiereux, Eric ^b   Martial, Joseph A ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

^b UNIVERSITY OF NAMUR   (Belgium)

^c VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; GLYCINE; GLYCOLIC ACID DERIVATIVE; HISTIDINE; LYSINE; MUTANT PROTEIN; TRIOSEPHOSPHATE ISOMERASE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DEAMINATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STABILITY; GEOBACILLUS STEAROTHERMOPHILUS; HEAT TOLERANCE; HIGH TEMPERATURE; MOLECULAR DYNAMICS; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; ADAPTATION; CHEMICAL STRUCTURE; HEAT; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

GEOBACILLUS STEAROTHERMOPHILUS; POSIBACTERIA; THERMOTOGA MARITIMA;

ADAPTATION, PHYSIOLOGICAL; ASPARAGINE; BACILLUS STEAROTHERMOPHILUS; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; GLYCINE; HEAT; LYSINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; TRIOSE-PHOSPHATE ISOMERASE;

EID: 0033516339     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.27.19181     Document Type: Article

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