Evidence for the existence of a novel enzyme system. myo-inositol-1-phosphate dehydrogenase in Phaseolus aureus

De, B. P. ; Biswas, B. B. (1979) Evidence for the existence of a novel enzyme system. myo-inositol-1-phosphate dehydrogenase in Phaseolus aureus Journal of Biological Chemistry, 254 . pp. 8717-8719. ISSN 0021-9258

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Official URL: http://www.jbc.org/content/254/18/8717.short

Abstract

A novel enzyme system, myo-inositol-1-phosphate dehydrogenase, has been isolated from germinating mung bean seeds. The dehydrogenation and cleavage of myo-inositol 1-phosphate by this enzyme leads to the synthesis of a pentose phosphate which appears to be ribulose 5-phosphate. The pH optimum of the enzyme is 8.6; NAD+ is required as coenzyme and no other nucleotides can replace NAD+. Mono- or divalent cations are not essential for the enzyme activity. Stoichiometry of the reaction suggests that 2 mol of NAD+ are reduced per mol of ribulose-5-P generated.

Item Type:Article
Source:Copyright of this article belongs to American Society for Biochemistry and Molecular Biology.
ID Code:3543
Deposited On:12 Oct 2010 04:17
Last Modified:16 May 2016 14:19

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