Short Communication Inorganic Pyrophosphatase from Spirulina maxima

An inorganic pyrophosphatase was isolated from a cyanobacterium Spirulina maxima. The properties of the enzyme such as pH optimum, substrate and metal ion specificities and the effects of inhibitors were determined. Key words: Cyanobacterium — Spirulina maxima — Inorganic pyrophosphatase. Inorganic pyrophosphatase (EC 3.6.1.1) seems to hydrolyze PPi released in various biological reactions such as those involved in the synthesis of proteins, carbohydrates, nucleic acids and fatty acids. Kornberg (1962) suggested that the hydrolysis of PPi is necessary to propel these reactions toward completion. Inorganic pyrophosphatase has been characterized for various plant materials (Simmons and Butler 1969, Popli and Singh 1977), animal tissues (Butler 1971, Morita and Yasui 1978) and microorganisms (Wong et al. 1970, Cohen et al. 1978). It has also been found in cyanobacteria, such as Anacystis nidulans (Bornefeld 1981) and Anabaena cylindrica (Sawhney and Nicholas 1976), but comparatively little is known about the properties of the cyanobacterial enzyme. This paper reports on the finding of inorganic pyrophosphatase in a filamentous cyanobacterium, Spirulina maxima, the methods used to purify it and its properties