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The structure of Aspergillus niger phytase PhyA in complex with a phytate mimetic

Journal Article


Abstract


  • Phytases hydrolyse the phosphomonoesters of phytate (myo-inositol-1,2,3,4,5,6-hexakis phosphate) and thus find uses in plant and animal production through the mobilisation of phosphorus from this source. The structure of partially deglycosylated Aspergillus niger PhyA is presented in apo form and in complex with the potent inhibitor myo-inositol-1,2,3,4,5,6-hexakis sulfate, which by analogy with phytate provides a snapshot of the Michaelis complex. The structure explains the enzyme’s preference for the 3′-phosphate of phytate. The apo-and inhibitor-bound forms are similar and no induced–fit mechanism operates. Furthermore the enzyme structure is apparently unaffected by the presence of glycosides on the surface. The new structures of A. niger PhyA are discussed in the context of protein engineering studies aimed at modulating pH preference and stability.

Publication Date


  • 2010

Citation


  • Oakley, A. J. (2010). The structure of Aspergillus niger phytase PhyA in complex with a phytate mimetic. Biochemical and Biophysical Research Communications, 397 (4), 745-749.

Scopus Eid


  • 2-s2.0-77954384305

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/5178

Number Of Pages


  • 4

Start Page


  • 745

End Page


  • 749

Volume


  • 397

Issue


  • 4

Place Of Publication


  • http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description#description

Abstract


  • Phytases hydrolyse the phosphomonoesters of phytate (myo-inositol-1,2,3,4,5,6-hexakis phosphate) and thus find uses in plant and animal production through the mobilisation of phosphorus from this source. The structure of partially deglycosylated Aspergillus niger PhyA is presented in apo form and in complex with the potent inhibitor myo-inositol-1,2,3,4,5,6-hexakis sulfate, which by analogy with phytate provides a snapshot of the Michaelis complex. The structure explains the enzyme’s preference for the 3′-phosphate of phytate. The apo-and inhibitor-bound forms are similar and no induced–fit mechanism operates. Furthermore the enzyme structure is apparently unaffected by the presence of glycosides on the surface. The new structures of A. niger PhyA are discussed in the context of protein engineering studies aimed at modulating pH preference and stability.

Publication Date


  • 2010

Citation


  • Oakley, A. J. (2010). The structure of Aspergillus niger phytase PhyA in complex with a phytate mimetic. Biochemical and Biophysical Research Communications, 397 (4), 745-749.

Scopus Eid


  • 2-s2.0-77954384305

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/5178

Number Of Pages


  • 4

Start Page


  • 745

End Page


  • 749

Volume


  • 397

Issue


  • 4

Place Of Publication


  • http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description#description