Sequencing and Expression of the L-Phenylalanine Oxidase Gene from Pseudomonas sp. P-501. Proteolytic Activation of the Proenzyme

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  • Suzuki Haruo
    Division of Biosciences, Graduate School of Fundamental Life Science Kitasato University Department of Biosciences, School of Science, Kitasato University
  • Higashi Yuhki
    Division of Biosciences, Graduate School of Fundamental Life Science Kitasato University
  • Asano Mai
    Division of Biosciences, Graduate School of Fundamental Life Science Kitasato University
  • Suguro Masaya
    Division of Biosciences, Graduate School of Fundamental Life Science Kitasato University
  • Kigawa Masayuki
    Department of Biosciences, School of Science, Kitasato University
  • Maeda Masahiro
    Department of Biosciences, School of Science, Kitasato University
  • Katayama Satoshi
    Department of Biosciences, School of Science, Kitasato University
  • Mukouyama Etsuko B.
    Department of Biosciences, School of Science, Kitasato University
  • Uchiyama Koji
    Laboratory of Embryology, Kitasato University

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  • Sequencing and Expression of the L-Phenylalanine Oxidase Gene from <i>Pseudomonas</i> sp. P-501. Proteolytic Activation of the Proenzyme

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The nucleotide sequence encoding L-phenylalanine oxidase (deaminating and decarboxylating) (PAO) from Pseudomonas sp. P-501 was determined. The open reading frame is arranged in the order of prosequence, α subunit, dipeptide and β subunit from the 5'- to 3'-end. Expression of the gene in Escherichia coli showed that without the prosequence, PAO is produced in small quantity as a soluble form with no visible absorption, but with the prosequence (proPAO), PAO is highly expressed and yellow. The purified proPAO contained one mol of FAD per mol of proPAO polypeptide, but had no catalytic activity. Treatment of proPAO with a mixture of Pronase and trypsin converted the noncatalytic proPAO to the catalytic form, and the Pronase-trypsintreated proPAO showed kinetic and spectral properties comparable to the native enzyme. These results suggest that in Pseudomonas, PAO is expressed as a proenzyme that is processed by proteolysis to the active form.

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