Cooperative effect of two surface amino acid mutations (Q252L and E170K) in glucose dehydrogenase from Bacillus megaterium IWG3 on stabilization of its oligomeric state

Applied and Environmental Microbiology

Volumn 71, Issue 6, 2005, Pages 3285-3293

  Baik, Sang Ho ^a,c   Michel, Fabrice ^b   Aghajari, Nushin ^b   Haser, Richard ^b   Harayama, Shigeaki ^a,c  

^a MARINE BIOTECHNOLOGY INSTITUTE   (Japan)

^b INSTITUT DE BIOLOGIE ET CHIMIE DES PROTÉINES   (France)

^c NATIONAL INSTITUTE OF TECHNOLOGY AND EVALUATION   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHROMATOGRAPHIC ANALYSIS; CRYSTAL STRUCTURE; FILTRATION; GLUCOSE; HYDROPHOBICITY; OLIGOMERS; PH EFFECTS; SODIUM CHLORIDE; SUBSTITUTION REACTIONS;

GLUCOSE DEHYDROGENASE (GLCDH); HARBORING; HYDROPHOBIC CAVITY; PACILLUS MEGATERIUM;

ENZYMES;

GLUCOSE DEHYDROGENASE; PROTEIN SUBUNIT;

BACTERIUM;

ALKALINITY; AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS MEGATERIUM; BACTERIAL GENE; CRYSTAL STRUCTURE; DIMERIZATION; E170K GENE; FUSION GENE; GEL CHROMATOGRAPHY; GENE MUTATION; HYDROPHOBICITY; NONHUMAN; Q252L GENE; THERMODYNAMICS; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACILLUS MEGATERIUM; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENZYME STABILITY; GLUCOSE DEHYDROGENASES; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT;

BACILLUS MEGATERIUM;

EID: 20444417370     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.6.3285-3293.2005     Document Type: Article

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