Evidence for the existence of a novel enzyme system. myo-Inositol-1-phosphate dehydrogenase in Phaseolus aureus.
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.
D007295:Inositol Phosphates; D007700:Kinetics; D009243:NAD; D010944:Plants / Q000201:enzymology*; D012274:Ribulosephosphates; D013401:Sugar Alcohol Dehydrogenases / Q000378:metabolism*
D007295:Inositol Phosphates; D012274:Ribulosephosphates; D009243:NAD; D013401:Sugar Alcohol Dehydrogenases; C021823:myo-inositol-1-phosphate dehydrogenase