title: Degradation of myo-inositol hexakisphosphate by a phytate-degrading enzyme from Pantoea agglomerans.
abstract: High-pressure liquid chromatography (HPLC) analysis established myo-inositol pentakisphosphate as the final product of phytate dephosphorylation by the phytate-degrading enzyme from Pantoea agglomerans. Neither product inhibition by phosphate nor inactivation of the Pantoea enzyme during the incubation period were responsible for the limited phytate hydrolysis as shown by addition of phytate-degrading enzyme and phytate, respectively, after the observed stop of enzymatic phytate degradation. In additon, the Pantoea enzyme did not possess activity toward the purified myo-inositol pentakisphosphate. Using a combination of High-Performance Ion Chromatography (HPIC) analysis and kinetic studies, the nature of the generated myo-inositol pentakisphosphate was established. The data demonstrate that the phytate-degrading enzyme from Pantoea agglomerans dephosphorylates myo-inositol hexakisphosphate in a stereospecific way to finally D-myo-inositol(1,2,4,5,6)pentakisphosphate.
authors.affiliation: Centre for Molecular Biology, Federal Research Centre for Nutrition and Food, Haid-und-Neu-Strasse 9, D-76131 Karlsruhe, Germany. ralf.greiner@bfe.uni-karlsruhe.de
authors.forename: Ralf
authors.initials: R
authors.lastname: Greiner
mesh_terms: D010832:6-Phytase / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D004926:Escherichia coli / Q000201:enzymology; D029968:Escherichia coli Proteins / Q000378:metabolism; D007295:Inositol Phosphates / Q000096:biosynthesis; D007700:Kinetics; D008956:Models, Chemical; D020636:Pantoea / Q000201:enzymology*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D010833:Phytic Acid / Q000378:metabolism*
chemical_list: D029968:Escherichia coli Proteins; D007295:Inositol Phosphates; C013571:inositol pentaphosphate; D010833:Phytic Acid; C062887:agp protein, E coli; D010744:Phosphoric Monoester Hydrolases; D010832:6-Phytase