Purification and Characterization of a Novel Bifunctional Enzyme, Cyclic-Ribonucleotide Phosphomutase-5'-Phosphodiesterase, from Aspergillus niger

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概要

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• A 3', 5'-cyclicribonucleotide was enzymatically converted into a corresponding 2', 3'-cyclic-ribo-nucleotide by a culture extract of 5'-phosphodiesterase (5'-PDase ; EC 3. 1. 4. 1) hyperproductive mutant of Aspergillus niger, FS-44. Cyclic-ribonucleotide phosphomutase (cRNPMase) activity catalyzing the preceding reaction was not separated from the 5'-PDase activity during the purification steps. The enzyme was purified to the homogeneity of a single polypeptide with a molecular weight of 62,000. The purified enzyme specifically catalyzed the conversion of 3', 5'-cyclic-ribonucleotides to corresponding 2', 3'-cyclic-ribonucleotides. The decreasing order of reaction rate was as follows : adenosine 3', 5'-cyclic monophosphate > inosine 3', 5'-cyclic monophosphate > uridine 3', 5'-cyclic monophosphate > guanosine 3', 5'-cyclic monophosphate > cytidine 3', 5'-cyclic monophosphate. The enzyme did not act on 2'-AMP, 3'-AMP, or 5'-AMP. The optimum pH of cRNPMase activity was pH 3.0, while that of 5'-PDase activity was pH 5. 6. Both activities was inhibited by diisopropyl flurophosphate, Fe^<2+>, and Fe^<3+>. While 5'-PDase activity was significantly inhibited by Zn^<2+> and Cu^<2+>, cRNPMase activity was not at all. The Michaelis constant of cRNPMase was estimated to be 3. 72mM for adenosine 3', 5'-cyclic monophosphate and that of 5'-PDase was 0.96mM for adenosine 5'-p-nitrophenyl phosphate. The enzyme was a glycoprotein containing N-linked sugar chains. The isoelectric point was 4.8. This bifunctional enzyme was named cyclic-ribonucleotide phosphomutase-5'-phosphodiesterase (cRNPMase-5'-PDase).

• 社団法人日本農芸化学会の論文
• 1994-02-23

著者

• Nagata T

  National Food Res. Inst. Ministry Of Agriculture Forestry And Fisheries Ibaraki Jpn

• Chohnan Shigeru

  Research Laboratories, Yamasa Corporation

• Nagata Takashi

  Research Laboratories, Yamasa Corporation

• Midorikawa Yuichirou

  Research Laboratories, Yamasa Corporation

• Chohnan S

  Yamasa Corp. Chiba Jpn

• Chohnan Shigeru

  Research Laboratories Yamasa Corporation

• Midorikawa Yuichirou

  Research Laboratories Yamasa Corporation

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• Purification and Characterization of a Novel Bifunctional Enzyme, Cyclic-Ribonucleotide Phosphomutase-5'-Phosphodiesterase, from Aspergillus niger
• Determination of the Chemical Form of Fluorine in Tea Infusions by ^F-NMR
• Investigation of Substrate-binding Sites of Cyclic-ribonucleotide Phosphomutase-5'-phosphodiesterase Using Substrate Analogues

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