Purification and characterization of aromatic acid reductase from Nocardia asteroides JCM 3016.

DOI
  • KATO Nobuo
    Department of Biotechnology, Faculty of Engineering, Tottori University
  • JOUNG Eun-Ho
    Department of Biotechnology, Faculty of Engineering, Tottori University Present address: Institute of Biotechnology, Korea University
  • YANG Han-Chul
    Department of Biotechnology, Faculty of Engineering, Tottori University Present address: Institute of Biotechnology, Korea University
  • MASUDA Muneto
    Department of Biotechnology, Faculty of Engineering, Tottori University
  • SHIMAO Masayuki
    Department of Biotechnology, Faculty of Engineering, Tottori University
  • YANASE Hideshi
    Department of Biotechnology, Faculty of Engineering, Tottori University

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抄録

Aromatic acid reductase (aryl-aldehyde dehydrogenase, EC 1.2.1.30) was purified to electrophoretic homogeneity from Nocardia asteroides JCM 3016. The enzyme was a monomeric protein with a molecular weight of 152, 000. The enzyme absolutely required ATP, NADPH, and MgCl2 for the reduction of benzoate to benzaldehyde. In the overall reaction, benzaldehyde, AMP, and NADP+ were stoichiometrically formed from benzoate, ATP and NADPH, respectively. The purified enzyme catalyzed the reduction of benzoyl adenosine 5'-monophosphate (bzAMP), which is the intermediate formed from benzoate and ATP. The temperature dependence of the benzoate- and bzAMP-reducing activities agreed exactly, and the same Km for NADPH was obtained by the steady state kinetics of both reactions. These results suggest that the overall reduction of benzoate proceeds via bzAMP, and that the ATP-dependent adenylation of benzoate and the reduction of bzAMP are catalyzed by one enzyme. The enzyme was fairly specific for meta-substituted benzoates.

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詳細情報

  • CRID
    1390282681441795584
  • NII論文ID
    110006325429
  • NII書誌ID
    AA00515312
  • DOI
    10.1271/bbb1961.55.757
  • ISSN
    18811280
    00021369
  • 本文言語コード
    en
  • データソース種別
    • JaLC
    • Crossref
    • CiNii Articles
  • 抄録ライセンスフラグ
    使用不可

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