Manganese-dependent Production, and Properties, of 5'-Nucleotidase by Alkalophilic Bacillus No. A-59(Microbiology & Fermentation Industry)
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概要
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Alkalophilic Bacillus No. A-59 produced 5'-nucleotidase (EC 3.1.3.5) extracellularly when Mn^<2+> was added to the growth medium. The enzyme formation was negligible in the medium without the addition of Mn^<2+> and the optimum Mn^<2+> concentration for the enzyme production was 10 mM. The 5'-nucleotidase was purified and its molecular weight was determined to be 78,000 by gel filtration. The optimum pH for its activity was 9.0〜9.5. The enzyme was stable in the pH range of 8.5 to 9.5, and up to 40℃. A substrate specificity study revealed that the enzyme hydrolyzed 5'-AMP strongly, several 5'-XMPs and ADP weakly, but not 3'-XMP, 2'-XMP, ATP or p-nitrophenyl phosphate. The Km value for 5'-AMP was 1.5mM. The maximum enzyme activity was obtained without divalent cations, The enzyme was inhibited by borate and arsenite ions, but not by 2mM EDTA.
- 社団法人日本農芸化学会の論文
- 1989-03-23
著者
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HORIKOSHI KOKI
The Institute of Physical and Chemical Research
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IKURA YOKO
The Institute of Physical and Chemical Research
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