ENZYME-CATALYZED HYDROLYSIS OF PYROPHOSPHATE: EFFECT OF LANTHANUM ION

Inorganic pyrophosphatase (EC3.6.1.1) from baker's yeast was activated by 10-3-10-4 M magnesium ion to promote the P-O-P bond cleavage of pyrophosphate (diphosphate). On the contrary lanthanum ion at very lower concentrations, 10-5-10-7 M La3+, strongly inhibited the hydrolytic activity of the...

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Bibliographic Details
Published inPhosphorus Research Bulletin Vol. 6; pp. 201 - 204
Main Authors YOZA, Norimasa, NAKATANI, Ai, NAKAZATO, Tetsuya, ISHIGURO, Shin-ichi
Format Journal Article
LanguageEnglish
Published Japanese Association of Inorganic Phosphorus Chemistry 1996
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Summary:Inorganic pyrophosphatase (EC3.6.1.1) from baker's yeast was activated by 10-3-10-4 M magnesium ion to promote the P-O-P bond cleavage of pyrophosphate (diphosphate). On the contrary lanthanum ion at very lower concentrations, 10-5-10-7 M La3+, strongly inhibited the hydrolytic activity of the Mg2+ -stimulated enzyme. The kinetic processes of these activation and inhibition reactions were visualized by high-performance liquid chromatography.
ISSN:0918-4783
1882-2363
DOI:10.3363/prb1992.6.0_201