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myo-Inositol phosphate isomers generated by the action of a phytate-degrading enzyme from Klebsiella terrigena on phytate

R Greiner ; Nils-Gunnar Carlsson (Institutionen för kemi- och bioteknik, Livsmedelsvetenskap)
Canadian Journal of Microbiology (0008-4166). Vol. 52 (2006), 8, p. 759-768.
[Artikel, refereegranskad vetenskaplig]

For the first time a dual pathway for dephosphorylation of myo-inositol hexakisphosphate by a histidine acid phytase was established. The phytate-degrading enzyme of Klebsiella terrigena degrades myo-inositol hexakisphosphate by stepwise dephosphorylation, preferably 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)P-2 and alternatively via D-Ins(1,2,4,5,6)P-5, Ins(2,4,5,6)P-4, D-Ins(2,4,5)P-3, D-Ins(2,4)P-2 to finally Ins(2)P. It was estimated that more than 98% of phytate hydrolysis occurs via D-Ins(1,2,4,5,6)P-5. Therefore, the phytate-degrading enzyme from K. terrigena has to be considered a 3-phytase (EC 3.1.3.8). A second dual pathway of minor importance could be proposed that is in accordance with the results obtained by analysis of the dephosphorylation products formed by the action of the phytate-degrading enzyme of K. terrigena on myo-inositol hexakisphosphate. It proceeds preferably via D-Ins(1,2,3,5,6)P-5, D-Ins(1,2,3,6)P-4, Ins(1,2,3)P-3, D-Ins(2,3)P-2 and alternatively via D-Ins(1,2,3,5,6)P-5, D-Ins(2,3,5,6)P-4, D-Ins(2,3,5)P-3, D-Ins(2,3)P-2 to finally Ins(2)P. D-Ins(2,3,5,6)P-4, D-Ins(2,3,5)P-3, and D-Ins(2,4)P-2 were reported for the first time as intermediates of enzymatic phytate dephosphorylation. A role of the phytate-degrading enzyme from K. terrigena in phytate breakdown could not be ruled out. Because of its cytoplasmatic localization and the suggestions for substrate recognition, D-Ins(1,3,4,5,6)P-5 might be the natural substrate of this enzyme and, therefore, may play a role in microbial pathogenesis or cellular myo-inositol phosphate metabolism.Key words: myo-inositol phosphate isomers, phytate-degrading enzyme, phytate, phytase, Klebsiella terrigena.



Denna post skapades 2007-01-31. Senast ändrad 2012-03-06.
CPL Pubid: 26177

 

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Institutioner (Chalmers)

Institutionen för kemi- och bioteknik, Livsmedelsvetenskap (2005-2014)

Ämnesområden

Livsmedelsvetenskap

Chalmers infrastruktur