Substrate Specificity of Aminopeptidase from the Mid-gut Gland of the Scallop (<i>Patinopecten yessoensis</i>)

  • UMETSU Hironori
    Graduate School of Environmental Science, Aomori University Institute of Bioscience and Biotechnology, Aomori University
  • ARAI Mito
    Graduate School of Environmental Science, Aomori University
  • OTA Toshinori
    Institute of Bioscience and Biotechnology, Aomori University
  • ABE Kaoru
    Aomori Industrial Research Center
  • UCHIZAWA Hidemitsu
    Aomori Industrial Research Center
  • SASAKI Kazuo
    Institute of Bioscience and Biotechnology, Aomori University

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タイトル別名
  • Substrate Specificity of Aminopeptidase from the Mid-gut Gland of the Scallop (Patinopecten yessoensis)

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An action for various peptides and a kinetic study for amino acid p-nitroanilides (pNAs) and 4-methylcoumaryl-7-amides (MCAs) were performed with purified aminopeptidase from the mid-gut of the scallop. The enzyme preferred dipeptides having Ala, Met, and Phe in the amino-terminal or the penultimate position from the amino-termini. The catalytic efficiencies, kcatKm values for Ala-pNA and MCA were the highest in the tested substrates, and those for pNA and MCA substrates having Met or Phe were the next highest. The enzyme was found to be a new alanine-specific aminopeptidase.

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