Molecular Cloning and Characterization of an Enzyme Hydrolyzing p-Nitrophenyl α-D-Glucoside from Bacillus stearothermophilus SA0301

この論文にアクセスする

この論文をさがす

著者

抄録

<I>Bacillus stearothermophilus</I> SA0301 produces an extracellular oligo-1,6-glucosidase (bsO16G) that also hydrolyzes <I>p</I>-nitrophenyl α-<small>D</small>-glucoside (Tonozuka <I>et al.</I>, <I>J. Appl. Glycosci.</I>, <B>45</B>, 397–400 (1998)). We cloned a gene for an enzyme hydrolyzing <I>p</I>-nitrophenyl α-<small>D</small>-glucoside, which was different from the one mentioned above, from <I>B. stearothermophilus</I> SA0301. The <I>k</I><SUB>0</SUB>⁄<I>K</I><SUB>m</SUB> values of bsO16G for isomaltotriose and isomaltose were 13.2 and 1.39 s<SUP>−1</SUP>·m<small>M</small><SUP>−1</SUP> respectively, while the newly cloned enzyme did not hydrolyze isomaltotriose, and the <I>k</I><SUB>0</SUB>⁄<I>K</I><SUB>m</SUB> value for isomaltose was 0.81 s<SUP>−1</SUP>·m<small>M</small><SUP>−1</SUP>. The primary structure of the cloned enzyme more closely resembled those of trehalose-6-phosphate hydrolases than those of oligo-1,6-glucosidases, and the cloned enzyme hydrolyzed trehalose 6-phosphate. An open reading frame encoding a protein homologous to the trehalose-specific IIBC component of the phopshotransferase system was also found upstream of the gene for this enzyme.

収録刊行物

  • Bioscience, biotechnology, and biochemistry  

    Bioscience, biotechnology, and biochemistry 70(2), 495-499, 2006-02-23 

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

参考文献:  19件

参考文献を見るにはログインが必要です。ユーザIDをお持ちでない方は新規登録してください。

各種コード

  • NII論文ID(NAID)
    10018534552
  • NII書誌ID(NCID)
    AA10824164
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    09168451
  • NDL 記事登録ID
    7833568
  • NDL 雑誌分類
    ZR7(科学技術--農林水産--農産) // ZR2(科学技術--生物学--生化学) // ZP1(科学技術--化学・化学工業)
  • NDL 請求記号
    Z53-G223
  • データ提供元
    CJP書誌  NDL  J-STAGE 
ページトップへ