Disruption of an ionic network leads to accelerated thermal denaturation of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima

Journal of Molecular Biology

Volumn 274, Issue 4, 1997, Pages 676-683

  Pappenberger, Günter ^a   Schurig, Hartmut ^a   Jaenicke, Rainer ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

Electrostatic interaction; GAPDH; Kinetic thermal stability; Protein stability; Site directed mutagenesis

Indexed keywords

BACTERIAL ENZYME; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MUTANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; ENTHALPY; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME STABILITY; KINETICS; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; SPECTROSCOPY; THERMOPHILIC BACTERIUM; THERMOSTABILITY;

BACTERIA (MICROORGANISMS); THERMOTOGA MARITIMA;

EID: 0031565980     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1421     Document Type: Article

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