Molecular Cloning and Characterization of D-Xylose Isomerase from A Novel Actinobacteria, Thermobifida fusca MBL 10003

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  • Kasumi Takafumi
    Laboratory of Enzymology and Molecular Biology, Department of Chemistry and Life Science, Nihon University
  • Mori Sumiko
    Biomolecular Engineering Laboratory, National Food Research Institute
  • Kaneko Satoshi
    Biomolecular Engineering Laboratory, National Food Research Institute
  • Koyama Yoshiyuki
    Laboratory of Enzymology and Molecular Biology, Department of Chemistry and Life Science, Nihon University

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  • Molecular Cloning and Characterization of D-Xylose Isomerase from A Novel Actinobacteria, <I>Thermobifida fusca </I>MBL 10003

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D-xylose isomerase was cloned and characterized from a newly isolated actinobacteria strain, Thermobifisa fusca MBL 10003. There was only one base difference between the xylose isomerase genes from T. fusca XY, a cellulosic bacteria, and T. fusca MBL10003. The structural gene (xylA) is predicted to encode a polypeptide of 387 amino acids with an estimated molecular mass of 43,900. The deduced amino acid sequence of the gene showed high identity with homologous enzymes from the species of Streptomyces, Actinoplanes and Arthrobacter. The optimal temperature and pH were 75°C and 10, respectively. The enzyme was stable between 70 and 75°C, and between pH 4 and 12. Unlike other known xylose isomerases, the T. fusca enzyme had very similar Km values for xylose and glucose, 264 and 274 mM, respectively. In contrast, kcat and, therefore, kcat/Km for xylose was approximately 18-fold larger than that for glucose. It required divalent metal ions for activity. Of these, Mg2+ was the most effective activator, and Co2+ functioned as a co-activator of Mg2+.

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