Functional Characterization of D-Galacturonic Acid Reductase, a Key Enzyme of the Ascorbate Biosynthesis Pathway, from Euglena gracilis

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<small>D</small>-Galacturonic acid reductase, a key enzyme in ascorbate biosynthesis, was purified to homogeneity from <I>Euglena gracilis</I>. The enzyme was a monomer with a molecular mass of 38–39 kDa, as judged by SDS–PAGE and gel filtration. Apparently it utilized NADPH with a <I>K</I>m value of 62.5±4.5 μ<small>M</small> and uronic acids, such as <small>D</small>-galacturonic acid (<I>K</I>m=3.79±0.5 m<small>M</small>) and <small>D</small>-glucuronic acid (<I>K</I>m=4.67±0.6 m<small>M</small>). It failed to catalyze the reverse reaction with <small>L</small>-galactonic acid and NADP<SUP>+</SUP>. The optimal pH for the reduction of <small>D</small>-galacturonic acid was 7.2. The enzyme was activated 45.6% by 0.1 m<small>M</small> H<SUB>2</SUB>O<SUB>2</SUB>, suggesting that enzyme activity is regulated by cellular redox status. No feedback regulation of the enzyme activity by <small>L</small>-galactono-1,4-lactone or ascorbate was observed. N-terminal amino acid sequence analysis revealed that the enzyme is closely related to the malate dehydrogenase families.

収録刊行物

  • Bioscience, biotechnology, and biochemistry  

    Bioscience, biotechnology, and biochemistry 70(11), 2720-2726, 2006-11-23 

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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各種コード

  • NII論文ID(NAID)
    10018524959
  • 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
    8560526
  • 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  CJP引用  NDL  J-STAGE 
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