Bivalent cations and amino-acid composition contribute to the thermostability of Bacillus licheniformis xylose isomerase

European Journal of Biochemistry

Volumn 268, Issue 23, 2001, Pages 6291-6301

  Vieille, Claire ^a   Epting, Kevin L ^b   Kelly, Robert M ^b   Zeikus, J Gregory ^a  

^a Michigan State University   (United States)

^b North Carolina State University   (United States)

Author keywords

Bacillus licheniformis; Metal binding; Thermostability; Xylose isomerase

Indexed keywords

AMINO ACID; AMYLASE; APOENZYME; CATION; COBALT; DIVALENT CATION; GLUCOSE; MAGNESIUM ION; RECOMBINANT ENZYME; XYLOSE; XYLOSE ISOMERASE;

AMINO ACID COMPOSITION; ARTICLE; BACILLUS LICHENIFORMIS; BACTERIAL GROWTH; BINDING SITE; CONTROLLED STUDY; ENZYME STABILITY; ESCHERICHIA COLI; GENE SEQUENCE; KINETICS; MELTING POINT; MICROORGANISM; NONHUMAN; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; TEMPERATURE; THERMOSTABILITY;

ALDOSE-KETOSE ISOMERASES; AMINO ACIDS; BACILLUS; BINDING SITES; CATIONS, DIVALENT; CLONING, MOLECULAR; ENZYME STABILITY; GENES, BACTERIAL; HYDROGEN-ION CONCENTRATION; KINETICS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; TEMPERATURE; THERMODYNAMICS;

EID: 0035214616     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.0014-2956.2001.02587.x     Document Type: Article

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