Purification and some properties of D-glucono-.GAMMA.-lactone dehydrogenase D-erythorbic acid producing enzyme of Penicillium cyaneo-fulvum.
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- TAKAHASHI Takeshi
- Department of Agricultural Chemistry, Tokyo Noko University
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- YAMASHITA Haruo
- Department of Agricultural Chemistry, Tokyo Noko University Res. Lab., Teikoku Hormone Mfg., Co.
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- KATO Eihachiro
- Department of Agricultural Chemistry, Tokyo Noko University Dept. of Agri. Chem., Meiji Univ.
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- MITSUMOTO Moritaka
- Department of Agricultural Chemistry, Tokyo Noko University Chiba Serum Instit.
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- MURAKAWA Shigeo
- Department of Agricultural Chemistry, Tokyo Noko University
書誌事項
- タイトル別名
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- D-Erythorbic Acid Producing Enzyme of <i>Penicillium cyaneo-fulvum</i>
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説明
D-Glucono-γ-lactone dehydrogenase is an enzyme dehydrogenating D-glucono-γ-lactone to D-erythorbic acid (D-araboascorbic acid, isovitamin C). D-Erythorbic acid was obtained as a cultural metabolite of penicillia. The enzyme of P. notatum was so labile that detailed studies were difficult. The enzyme of P. cyaneo-fulvum was relatively stable, however, and could be purified about 100-fold in specific activity to give a single protein. The enzyme has similar properties to L-gulono-γ-lactone oxidase (EC 1. 1. 3. 8), an L-ascorbic acid producing enzyme in animals, and to L-galactone-γ-lactone dehydrogenase (EC 1. 3. 2. 3), an L-ascorbic acid producing enzyme in plants. Molecular weight estimated by gel filtration is about 150, 000. The substrate of the enzyme seemed to be only D-glucono-γ-lactone. Km value for the substrate was 1.7±0.2×10-3M. Fe3+, Fe2+, Cu2+, Hg2+ and Ag+ inhibited the enzyme activity, but PCMB did not. Opt. pH for the enzyme reaction was 5.6_??_6.0, and the activity was completely lost on keeping at 55°C for 30min at the opt. pH. The prosthetic group seemed to be a flavin, but was difficult to identify by normal procedures. It is considered that the prosthetic group is a flavin covalently bound to the enzyme protein, as in L-gulono-γ-lactone oxidase. Phenazine methosulfate and dichlorophenolindophenol acted as a role as hydrogen acceptors, although their activity was very low compared with free oxygen. It is considered that this enzyme is a “dehydrogenase.”
収録刊行物
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 40 (1), 121-129, 1976
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206472164352
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- NII論文ID
- 130003525135
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- COI
- 1:CAS:528:DyaE28XhtVWgsLo%3D
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- ISSN
- 18811280
- 00021369
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- 本文言語コード
- en
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- データソース種別
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- JaLC
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