Some properties of inorganic pyrophosphatase from Bacillus subtilis

Inorganic pyrophosphatase (pyrophosphate phosphohydrolase, EC 3.6.1.1; PPase) from Bacillus subtilis was purified to a homogeneous state electrophoretically when analysed by SDS-PAGE. The enzyme consists of six identical subunits; the molecular weight of the native enzyme estimated by gel filtration...

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Published inThe international journal of biochemistry & cell biology Vol. 29; no. 2; pp. 303 - 310
Main Authors Shimizu, Tomomi, Imai, Mizuhiro, Araki, Shin, Kishida, Kei, Terasawa, Yasushi, Hachimori, Akira
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier Ltd 01.02.1997
Subjects
Bacillus subtilis
Bacillus subtilis - enzymology
Energy Metabolism
Inorganic pyrophosphatase
Pyrophosphatases - analysis
Pyrophosphatases - metabolism
Thermostability
Thermostability
PPase, inorganic pyrophosphatase
Inorganic pyrophosphatase
Bacillus subtilis
PPi, inorganic pyrophosphate
PAGE, polyacrylamide gel electrophoresis
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Summary:Inorganic pyrophosphatase (pyrophosphate phosphohydrolase, EC 3.6.1.1; PPase) from Bacillus subtilis was purified to a homogeneous state electrophoretically when analysed by SDS-PAGE. The enzyme consists of six identical subunits; the molecular weight of the native enzyme estimated by gel filtration was approx. 120 000, and denaturing polyacrylamide gel electrophoresis gave a single band corresponding to 24 000. The enzyme absolutely required a divalent cation for its activity. Mg 2+ was most effective, showing two steps of concentration-dependent activation. Mg 2+ could be partially replaced by Mn 2+ and Co 2+. The enzyme was thermostable in the presence of Mg 2+, and no loss of activity was observed on the incubation at 55°C for an hour.
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ISSN:1357-2725
1878-5875
DOI:10.1016/S1357-2725(96)00088-X