Heterologous expression, purification, and characterization of an α-mannosidase belonging to glycoside hydrolase family 99 of Shewanella amazonensis

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  • MATSUDA Kana
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology
  • KURAKATA Yuma
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology
  • MIYAZAKI Takatsugu
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology
  • MATSUO Ichiro
    Department of Chemistry and Chemical Biology, Gunma University
  • ITO Yukishige
    RIKEN Advanced Science Institute ERATO, Japan Science and Technology Agency (JST)
  • NISHIKAWA Atsushi
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology
  • TONOZUKA Takashi
    Department of Applied Biological Science, Tokyo University of Agriculture and Technology

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タイトル別名
  • Heterologous Expression, Purification, and Characterization of an .ALPHA.-Mannosidase Belonging to Glycoside Hydrolase Family 99 of Shewanella amazonensis
  • Heterologous expression purification and characterization of an a mannosidase belonging to glycoside hydrolase family 99 of Shewanella amazonensis
  • Heterologous Expression, Purification, and Characterization of an α-Mannosidase Belonging to Glycoside Hydrolase Family 99 of<i>Shewanella amazonensis</i>

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抄録

Shewanella amazonensis α-mannosidase (Sama99), a member of glycoside hydrolase family 99, was expressed in Escherichia coli. The purified Sama99 hydrolyzed pyridylamino (PA)-sugars, Glc1Man9GlcNAc2-PA, and Glc3Man9GlcNAc2-PA, and the product was probably a pyridylamino-decasaccharide in both cases. The mode of action of Sama99 was found to be essentially identical to that of rat endo-α-1,2-mannosidase, but the specificity of Sama99 was low.

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