Binding of bivalent ions to actinomycete mannanase is accompanied by conformational change and is a key factor in its thermal stability

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1834, Issue 1, 2013, Pages 301-307

  Kumagai, Yuya ^a   Kawakami, Kayoko ^a   Uraji, Misugi ^a   Hatanaka, Tadashi ^a  

^a Research Institute for Biological Science OKAYAMA   (Japan)

Author keywords

Actinomycete; Calcium; Conformational change; Glycoside hydrolase family 5; Mannanase; Thermal stability

Indexed keywords

BETA MANNOSIDASE; CALCIUM ION; COBALT; EDETIC ACID; ION; IRON; MAGNESIUM ION; MANGANESE; MANNAN; MANNANASE 2; MANNANASE 2DC; MANNANASE DC; MUTANT PROTEIN; SODIUM CHLORIDE; UNCLASSIFIED DRUG; ZINC ION;

ARTICLE; BINDING SITE; CARBOHYDRATE BINDING MODULE; CATALYSIS; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; ISOTHERMAL TITRATION CALORIMETRY; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; STOICHIOMETRY; STREPTOMYCES; STREPTOMYCES LIVIDANS; STREPTOMYCES THERMOLUTEUS; THERMOSTABILITY; WILD TYPE;

BACTERIAL PROTEINS; CATIONS, DIVALENT; ENZYME STABILITY; GLYCOSIDE HYDROLASES; PROTEIN STRUCTURE, TERTIARY; STREPTOMYCES;

STREPTOMYCES; STREPTOMYCES LIVIDANS;

EID: 84871716315     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.08.011     Document Type: Article

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