Gene Expression and Characterization of a Third Type of Dye-Linked L-Proline Dehydrogenase from the Aerobic Hyperthermophilic Archaeon, Aeropyrum pernix

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A third novel type of dye-linked <small>L</small>-proline dehydrogenase (LPDH) has recently been found in the hyperthermophilic archaeon, <I>Pyrobaculum calidifontis</I>, by Satomura <I>et al.</I> The gene encoding the enzyme homologue was identified in the aerobic hyperthermophilic archaeon, <I>Aeropyrum pernix</I>. The gene was successfully expressed in <I>Escherichia coli</I>, and the product was purified to homogeneity and characterized. The expressed enzyme was highly thermostable LPDH having a molecular mass of about 88 kDa and a homodimeric structure. The preferred substrate for the enzyme was <small>L</small>-proline with 2,6-dichloroindophenol (DCIP) as the electron acceptor. However, the enzyme did not utilize ferricyanide as the electron acceptor, in contrast to all other known LPDHs. The electrochemical determination of <small>L</small>-proline at concentrations from 0 to 0.7 m<small>M</small> was achieved by using <I>A. pernix</I> LPDH. A phylogenetic analysis revealed <I>A. pernix</I> LPDH to be clustered with the third type of LPDHs, and to be clearly separated from the clusters of previously known heterooligomeric LPDHs.

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  • Bioscience, biotechnology, and biochemistry

    Bioscience, biotechnology, and biochemistry 76(3), 589-593, 2012-03-23

    公益社団法人 日本農芸化学会

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各種コード

  • NII論文ID(NAID)
    10030750977
  • NII書誌ID(NCID)
    AA10824164
  • 本文言語コード
    ENG
  • 資料種別
    NOT
  • ISSN
    09168451
  • NDL 記事登録ID
    023553913
  • NDL 請求記号
    Z53-G223
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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