Literature DB >> 225311

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

B P De, B B Biswas.   

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.

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Year:  1979        PMID: 225311

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  3 in total

Review 1.  The plant phosphoinositide system.

Authors:  B K Drøbak
Journal:  Biochem J       Date:  1992-12-15       Impact factor: 3.857

2.  Chloroplast as a Locale of L-myo-Inositol-1-Phosphate Synthase.

Authors:  J Adhikari; A L Majumder; T J Bhaduri; S Dasgupta; A L Majumder
Journal:  Plant Physiol       Date:  1987-11       Impact factor: 8.340

3.  Redistribution of Tritium during Germination of Grain Harvested from myo-[2-H]Inositol- and scyllo-[R-H]Inositol-Labeled Wheat.

Authors:  K Sasaki; F A Loewus
Journal:  Plant Physiol       Date:  1982-01       Impact factor: 8.340

  3 in total

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