R. Greiner et al., Stereospecificity of myo-inositol hexakisphosphate dephosphorylation by a phytate-degrading enzyme of baker's yeast, J AGR FOOD, 49(5), 2001, pp. 2228-2233
During food processing such as baking, phytate is dephosphorylated to produ
ce degredation products, such as myo-inositol pentakis-, tetrakis-, tris-,
bis-, and monophosphates. Certain myo-inositol phosphates have been propose
d to have positive effects on human health. The position of the phosphate g
roups on the myo-inositol ring is thereby of great significance for their p
hysiological functions. Using a combination of high-performance ion chromat
ography analysis and kinetic studies the stereospecificity of mya-inositol
hexakisphosphate dephosphorylation by a phytate-degrading enzyme from baker
's yeast.(Saccharomyces cerevisiae) was established. The data demonstrate t
hat the phytate-degrading enzyme from baker's yeast dephosphorylates myo-in
ositol hexakisphosphate in a stereospecific way by sequential removal of ph
osphate groups via D-Ins(1,2,4,5,6)P-5, D-Ins-(1,2,5,6)P-4, D-Ins(1,2,6)P-3
, D-Ins(1,2,6)Pa-2 to finally Ins(2)P (notation 3/4/5/6/1). Knowledge of th
e absolute stereochemical-specificity of the baker's yeast phytase allows u
se of the enzyme to produce defined myo-inositol phosphates for kinetic and
physiological studies.