D-gluconate dehydrogenase, 2-keto-D-gluconate yielding, from Gluconobacter dioxyacetonicus: Purification and characterization.

• SHINAGAWA Emiko

  Departmentof Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University

• MATSUSHITA Kazunobu

  Departmentof Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University

• ADACHI Osao

  Departmentof Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University

• AMEYAMA Minoru

  Departmentof Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University

抄録

D-Gluconate dehydrogenase catalyzing the oxidation ofD-gluconate to 2-keto-D-gluconate was solubilized with Triton X-100 from the membrane of Gluconobacter dioxyacetonicus IFO 3271 and purified to an almost homogeneousstate by chromatographies on DEAE-cellulose and CMToyopearl in the presence of 0.1% Triton X-100. The enzyme had three subunits with molecular weights of 64, 000, 45, 000 and 21, 000, and contained approximately 2mol of heme per mol of the enzyme. The prosthetic group of the dehydrogenase was found to be a flavin covalently bound to the enzyme protein. The substrate specificity of the purified enzyme was very strict for D-gluconate and the apparent Michaelis constant for D-gluconate was 2.2mM.The optimum pH and temperature of the purified enzyme were 6.0 and 40°C, respectively.

収録刊行物

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 48 (6), 1517-1522, 1984

  公益社団法人 日本農芸化学会

キーワード

• General Agricultural and Biological Sciences
• General Biochemistry, Genetics and Molecular Biology

詳細情報

• CRID: 1390282681441917440
• NII論文ID: 130000026849
• DOI: 10.1271/bbb1961.48.1517
• COI: 1:CAS:528:DyaL2cXltVKhsr0%3D
• ISSN: 18811280
• ISSN: 00021369
• ISSN: http://id.crossref.org/issn/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