Purification and Characterization of Ascorbic Acid Phosphorylating Enzyme from Pseudomonas azotocolligans(Microbiology & Fermentation Industry)
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概要
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A enzyme that catalyzed the specific formation of ascorbic acid-2-phosphate (AsA2P) from ascorbic acid (AsA) and adenosine-5'-triphosphate (ATP), was purified 3,200-fold to homogeneity from a cell extract of Pseudomonas azotocolligans. The purified enzyme appeared as a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and consisted of a single polypeptide with a molecular weight of about 30,000. Of phosphoryl donors tested, p-nitrophenylphosphate (p-NPP) and pyrophosphate (PPi) were as effective as ATP. Optimal pHs for the phosphorylating activity were around 4.0 and 5.5 when PPi and ATP were used as phosphoryl donors, respectively. The Km for AsA was 147 niM. The enzyme activity was inhibited by Cu^<2+>, but not by sulfhydryl reagents. The enzyme simultaneously had phosphatase activity at weakly acidic or neutral pH and the Km for p-NPP in the phosphatase activity was 0.38 mM. The enzyme was tentatively named "ascorbic acid phosphorlating enzyme."
- 社団法人日本農芸化学会の論文
著者
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Koizumi Satoshi
Sensor Materials Center National Institute For Materials Science
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Koizumi Satoshi
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.
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Maruyama Akihiko
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.
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Maruyama Akihiko
Fine Chemicals Biochemicals Dept. Medicals Research And Development Center Kyowa Hakko Kogyo Co. Ltd
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Maruyama Akihiko
(present Address) Fermentation Research Institute Agency Of Industrial Science And Technology
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Koizumi S
Sensor Materials Center National Institute For Materials Science
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FUJIO Tatsuro
Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd.
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Fujio T
Kyowa Hakko Kogyo Co. Ltd. Tokyo Jpn
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Fujio Tatsuro
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.
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Koizumi Satoshi
Advanced Materials Laboratory National Institute For Materials Science
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KOIZUMI Satoshi
Advanced Science Research Center, Japan Atomic Energy Research Institute
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