A Novel Versatility of Catalase I as a Dioxygenase for Indole - ring - opening Dioxygenation

この論文にアクセスする

この論文をさがす

著者

    • SAGAWA Takashi
    • Department of Applied Chemistry & Biochemistry, Faculty of Engineering, Kumamoto University
    • YOMO Tetsuya
    • Department of Biotechnology, Faculty of Engineering, Osaka University
    • TSUGAWA Shin-ichi
    • Department of Applied Chemistry & Biochemistry, Faculty of Engineering, Kumamoto University
    • TAKEDA Yuka
    • Department of Applied Chemistry & Biochemistry, Faculty of Engineering, Kumamoto University
    • IHARA Hirotaka
    • Department of Applied Chemistry & Biochemistry, Faculty of Engineering, Kumamoto University
    • URABE Itaru
    • Department of Biotechnology, Faculty of Engineering, Osaka University

抄録

Catalase I (wild type) from <I>Bacillus stearothermophilus</I>, which was found to have catalase activity, catalyzed dioxygen-inserted indole-ring opening reaction of methyl <I>N</I>-acetyl L-tryptophanate as tryptophan 2,3-dioxygenase (TDO) model in the presence of Na<SUB>2</SUB>S<SUB>2</SUB>O<SUB>4</SUB>. Heme-reconstruction with protoporphyrin IX manganese(III) chloride (MnClPP) <I>via</I> annealing was examined and the reconstituted MnClPP-catalase I also revealed dioxygenolytic behaviour with higher TDO activity and higher selectivity than the catalase I (wild type).

収録刊行物

  • Chemistry letters  

    Chemistry letters 1999(4), 339-340, 1999-04-05 

    公益社団法人 日本化学会

参考文献:  8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)
    10004340995
  • NII書誌ID(NCID)
    AA00603318
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    03667022
  • データ提供元
    CJP書誌  J-STAGE 
ページトップへ