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Pathway of phytate dephosphorylation by beta-propeller phytases of different origins

R. Greiner ; B. L. Lim ; C. W. Cheng ; Nils-Gunnar Carlsson (Institutionen för kemi- och bioteknik, Livsmedelsvetenskap)
Canadian Journal of Microbiology (0008-4166). Vol. 53 (2007), 4, p. 488-495.
[Artikel, refereegranskad vetenskaplig]

Using a combination of high-performance ion chromatography analysis and kinetic studies, the pathway of myomositol hexakisphosphate dephosphorylation by the beta-propeller phytase of Shewanella oneidensis was established, which was then compared with that of Bacillus subtilis 168, Bacillus amyloliquefaciens ATCC 15841, and B. amyloliquefaciens 45 beta-propeller phytases. The data demonstrate that all of these beta-propeller phytases dephosphorylate myo-inositol hexakisphosphate in a stereospecific way by sequential removal of phosphate groups via D-Ins(1,2,4,5,6)P-5, In,(2,4,5,6)P-4 to finally Ins(2,4,6)P-3. Thus, the beta-propeller phytases prefer the hydrolysis of every second phosphate over that of adjacent ones. This finding does not support previous phytate degradation models proposed by J. Kerovuo, J. Rouvinen, and F. Hatzack (2000. Biochem. J. 352: 623-628) and R. Greiner, A. Farouk, M. Larsson Alminger, and N.G. Carlsson (2002. Can. J. Microbiol. 48: 986-994), but seems to fit with the structural model given by S. Shin, N.C. Ha, B.C. Oh, T.K. Oh, and B.H. Oh (2001. Structure, 9: 851-858).

Nyckelord: Bacillus spp., beta-propeller phytase, myo-inositol phosphate isomers, phytate degradation, Shewanella oneidensis, MYOINOSITOL HEXAKISPHOSPHATE DEPHOSPHORYLATION, DEGRADING ENZYME, KLEBSIELLA-TERRIGENA, PHOSPHATE ISOMERS, ESCHERICHIA-COLI, BACILLUS, STEREOSPECIFICITY, PURIFICATION, MECHANISM



Denna post skapades 2008-12-10.
CPL Pubid: 80967

 

Institutioner (Chalmers)

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

Ämnesområden

Kemiteknik

Chalmers infrastruktur