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Stereospecificity of myo-inositol hexakisphosphate dephosphorylation by a phytate-degrading enzyme of Escherichia coli
2000 (English)In: Journal of Biotechnology, ISSN 0168-1656, E-ISSN 1873-4863, Vol. 84, no 1, 53-62 p.Article in journal (Refereed)
Abstract [en]

Using a combination of high-performance ion chromatography analysis and kinetic studies, the stereospecificity of myo-inositol hexakisphosphate dephosphorylation by the phytate-degrading enzyme P2 of Escherichia coli was established. High-performance ion chromatography revealed that the phytate- degrading enzyme P2 of E. coli degrades myo-inositol hexakisphosphate by stepwise dephosphorylation via D/L-Ins(1,2,3,4,5)P5, D/L-Ins(2,3,4,5)P4, D/L-Ins(2,4,5)P3 or D/L-Ins(1,2,4)P3, D/L-Ins(1,2)P2 or Ins(2,5)P2 or D/L-Ins(4,5)P2 to finally Ins(2)P or Ins(5)P. Kinetic parameters for myo- inositol pentakisphosphate hydrolysis by E. coli and wheat phytase, respectively, showed that the myo-inositol pentakisphosphate intermediate produced either by the phytate-degrading enzyme of wheat or E. coli are not identical. The absolute configuration of the myo-inositol pentakisphosphate isomer produced by the E. coli enzyme was determined by taking into consideration that wheat phytase produces predominantly the D- Ins(1,2,3,5,6)P5 isomer (Lim, P.E., Tate, M.E., 1973. The phytases: II. Properties of phytase fraction F1 and F2 from wheat bran and the myo- inositol phosphates produced by fraction F2. Biochim. Biophys. Acta 302, 326-328). The data demonstrate that the phytate-degrading enzyme P2 of E. coli dephosphorylates myo-inositol hexakisphosphate in a stereospecific way by sequential removal of phosphate groups via D-Ins(1,2,3,4,5)P5, D- Ins(2,3,4,5)P4, D-Ins(2,4,5)P3, Ins(2,5)P2 to finally Ins(2)P (notation 6/1/3/4/5). (C) 2000 Elsevier Science B.V.Using a combination of high-performance ion chromatography analysis and kinetic studies, the stereospecificity of myo-inositol hexakisphosphate dephosphorylation by the phytate-degrading enzyme P2 of Escherichia coli was established. High-performance ion chromatography revealed that the phytate-degrading enzyme P2 of E. coli degrades myo-inositol hexakisphosphate by stepwise dephosphorylation via D/L-Ins(1,2,3,4,5)P5, D/L-Ins(2,3,4,5)P4, D/L-Ins(2,4,5)P3 or D/L-Ins(1,2,4)P3, D/L-Ins(1,2)P2 or Ins(2,5)P2 or D/L-Ins(4,5)P2 to finally Ins(2)P or Ins(5)P. Kinetic parameters for myo-inositol pentakisphosphate hydrolysis by E. coli and wheat phytase, respectively, showed that the myo-inositol pentakisphosphate intermediate produced either by the phytate-degrading enzyme of wheat or E. coli are not identical. The absolute configuration of the myo-inositol pentakisphosphate isomer produced by the E. coli enzyme was determined by taking into consideration that wheat phytase produces predominantly the D-Ins(1,2,3,5,6)P5 isomer. The data demonstrate that the phytate-degrading enzyme P2 of E. coli dephosphorylates myo-inositol hexakisphosphate in a stereospecific way by sequential removal of phosphate groups via D-Ins(1,2,3,4,5)P5, D-Ins(2,3,4,5)P4, D-Ins(2,4,5)P3, Ins(2,5)P2 to finally Ins(2)P (notation 6/1/3/4/5).

Place, publisher, year, edition, pages
2000. Vol. 84, no 1, 53-62 p.
Keyword [en]
Food Engineering
Keyword [sv]
Livsmedelsteknik
National Category
Food Science
Identifiers
URN: urn:nbn:se:ri:diva-8834DOI: 10.1016/S0168-1656(00)00331-XPubMedID: 11035187OAI: oai:DiVA.org:ri-8834DiVA: diva2:966707
Available from: 2016-09-08 Created: 2016-09-08Bibliographically approved

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