Influence of an anion-binding site in the stabilization of halophilic malate dehydrogenase from Haloarcula marismortui

Biochimie

Volumn 89, Issue 8, 2007, Pages 981-987

  Madern, Dominique ^a   Ebel, Christine ^a  

^a CEA GRENOBLE   (France)

Author keywords

Halophilic; Ion binding; Malate dehydrogenase; Protein solvent; Stability

Indexed keywords

ANION; BACTERIAL ENZYME; CHLORIDE; DIMER; FLUORIDE ION; MALATE DEHYDROGENASE; MUTANT PROTEIN; OLIGOMER; POTASSIUM CHLORIDE; SODIUM CHLORIDE; TETRAMER;

ADAPTATION; ARTICLE; BINDING SITE; ENZYME STABILITY; ENZYME SUBUNIT; GENE MUTATION; HALOARCULA MARISMORTUI; HALOPHYTE; SALT TOLERANCE; SITE DIRECTED MUTAGENESIS;

ANIONS; BINDING SITES; DIMERIZATION; DOSE-RESPONSE RELATIONSHIP, DRUG; FLUORIDES; HALOARCULA MARISMORTUI; MALATE DEHYDROGENASE; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MUTATION; POTASSIUM CHLORIDE; POTASSIUM COMPOUNDS; PROTEIN SUBUNITS;

HALOARCULA MARISMORTUI;

EID: 34447268243     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2007.03.008     Document Type: Article

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