Purification and properties of myo-inositol-1-phosphate dehydrogenase from germinating mung bean seeds

Ghosh, B. ; De, B. P. ; Biswas, B. B. (1984) Purification and properties of myo-inositol-1-phosphate dehydrogenase from germinating mung bean seeds Archives of Biochemistry and Biophysics, 228 (1). pp. 309-319. ISSN 0003-9861

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000398...

Related URL: http://dx.doi.org/10.1016/0003-9861(84)90072-9

Abstract

A novel enzyme, myo-inositol-1-phosphate dehydrogenase, which catalyzes the conversion of myo-inositol 1-phosphate to ribulose 5-phosphate has been purified 84-fold from mung bean seedling employing several common techniques. The molecular weight of this purified enzyme has been recorded as 88,500 by Sephadex G-200 column chromatography, and in sodium dodecyl sulfate-polyacrylamide gel electrophoresis one protein band containing three subunits of Mr 32,000 each was discernible. Km values for NAD+ and myo-inositol 1-phosphate have been recorded as 2.8 × 10-4 and 5.0 × 10-4M , respectively. Production of NADH in myo-inositol-1-phosphate dehydrogenase reaction has also been evidenced by measurement of NADH fluorescence. Dehydrogenation and decarboxylation of myo-inositol 1-phosphate are mediated by the same enzyme. In fact, the rate of dehydrogenation corroborates with that of decarboxylation. Stoichiometry of this reaction suggests that for the production of 1 mol of ribulose 5-phosphate 2 mol of NAD+ are reduced.

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