Mutational Study on αGln90 of Fe-Type Nitrile Hydratase from Rhodococcus sp. N771

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Nitrile hydratase (NHase) from <I>Rhodococcus</I> sp. N771 is a non-heme iron enzyme having post-translationally modified cysteine ligands, αCys112-SO<SUB>2</SUB>H and αCys114-SOH. We replaced αGln90, which is conserved in all known NHases and involved in the hydrogen-bond network around the catalytic center, with glutamic acid or asparagine. The <I>k</I><SUB>cat</SUB> of αQ90E and αQ90N mutants decreased to 24% and 5% that of wild type respectively, but the effect of mutations on <I>K</I><SUB>m</SUB> was not very significant. In both mutants, the αCys114-SOH modification appeared to be responsible for the catalysis as in native NHase. We crystallized the nitrosylated αQ90N mutant and determined its structure at a resolution of 1.43 Å. The structure was basically identical to that of native nitrosylated NHase except for the mutated site and its vicinity. The structural difference between native and αQ90N mutant NHases suggested the importance of the hydrogen bond networks between αGln90 and the iron center for the catalytic activity.

収録刊行物

  • Bioscience, biotechnology, and biochemistry  

    Bioscience, biotechnology, and biochemistry 70(4), 881-889, 2006-04-23 

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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各種コード

  • NII論文ID(NAID)
    10018532257
  • 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
    7899672
  • 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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