Studies on Utilization of Enzymes Produced by Actinomycetes Part XII

IWASA Takashi, SUGIMOTO Hiroshi, HARADA Michio, YOKOTSUKA Tamotsu

doi:10.1271/nogeikagaku1924.41.8_386

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放線菌酵素の利用に関する研究(第12報)
ホウセンキンコウソノリヨウニカンスルケンキュウ 12 ホウセンキン Streptomyces sp.No.41 ノセイサンスル 51-ヌクレオチダーゼニツイテ
Purification and Some Properties of 5'-Nucleotidase from Streptomyces sp. No. 41
放線菌Streptomyces sp. No. 41の生産する5'-ヌクレオチダーゼについて

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Abstract

A 5'-nucleotidase was purified from Streptomyces sp. No. 41 and some of its properties were studied. 1) The enzyme exhibited maximal activity at pH 7.0_??_7.3, and was stable between pH 6 and 8. It was completely inactivated at 55°C for 10min. 2) The enzyme activity was enhanced by Ca²⁺, Sr²⁺ and Mg²⁺, notably Ca²⁺, and inhibited by Ag⁺, Hg²⁺, Cu²⁺, Ni²⁺, and Zn²⁺. Reducing agents and thiol reagents had no effects on the enzyme activity, whereas I₂, N-bromosuccinimide, EDTA and o-phenanthroline showed significant inhibition. Nucleosides also had some inhibitory effects, among which pyrimidine nucleosides inhibited the enzyme activity to a greater extent than purine nucleosides did. 3) The enzyme catalyzed only the hydrolysis of 5'-mononucleotides, but did not hydrolyze FMN and hydrolyzed NMN to only slight extent (3% or less of the 5'-AMP hydrolysis). Of the 5'-nucleotides tested, 5'-IMP was hydrolyzed at a faster rate than the other 5'-ribo- and deoxyribonucleotides. 4) Michaelis constant for 5'-AMP was 3.0× 10^-5M, and for 5'-IMP 7.9×10^-5M.

Journal

Nippon Nōgeikagaku Kaishi

Nippon Nōgeikagaku Kaishi 41 (8), 386-392, 1967

Japan Society for Bioscience, Biotechnology, and Agrochemistry

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