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Degradation of Phytate by the 6-Phytase from Hafnia alvei: A Combined Structural and Solution Study

DOI: 10.1371/journal.pone.0065062 DOI Help
PMID: 23741456 PMID Help

Authors: Antonio Ariza (Department of Chemistry, University of York) , Olga Moroz (University of York) , Elena Blagova (Structural Biology Laboratory, University of York, U.K.) , Johan Turkenburg (University of York) , Jitka Waterman (Department of Chemistry, University of York) , Shirley Roberts (University of York) , Jesper Vind (Novozymes A/S, Bagsværd) , Carsten Sjøholm (Novozymes A/S, Bagsværd) , Søren F. Lassen (Novozymes A/S, Bagsværd) , Leonardo De Maria (Novozymes A/S, Bagsværd) , Vibe Glitsoe (Novozymes A/S, Bagsværd) , Lars K. Skov (Novozymes A/S, Bagsværd) , Keith Wilson (University of York)
Co-authored by industrial partner: Yes

Type: Journal Paper
Journal: Plos One , VOL 8 (5) , PAGES 11766-11774

State: Published (Approved)
Published: May 2013

Open Access Open Access

Abstract: Phytases hydrolyse phytate (myo-inositol hexakisphosphate), the principal form of phosphate stored in plant seeds to produce phosphate and lower phosphorylated myo-inositols. They are used extensively in the feed industry, and have been characterised biochemically and structurally with a number of structures in the PDB. They are divided into four distinct families: histidine acid phosphatases (HAP), β-propeller phytases, cysteine phosphatases and purple acid phosphatases and also split into three enzyme classes, the 3-, 5- and 6-phytases, depending on the position of the first phosphate in the inositol ring to be removed. We report identification, cloning, purification and 3D structures of 6-phytases from two bacteria, Hafnia alvei and Yersinia kristensenii, together with their pH optima, thermal stability, and degradation profiles for phytate. An important result is the structure of the H. alvei enzyme in complex with the substrate analogue myo-inositol hexakissulphate. In contrast to the only previous structure of a ligand-bound 6-phytase, where the 3-phosphate was unexpectedly in the catalytic site, in the H. alvei complex the expected scissile 6-phosphate (sulphate in the inhibitor) is placed in the catalytic site.

Journal Keywords: Amino; Binding; Catalytic; Hafnia; Hydrolysis; Models; Molecular; Phylogeny; Phytic; Protein; Sequence; Substrate Specificity

Subject Areas: Food Science, Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography

Other Facilities: ID23–1 of the European Synchrotron Radiation Facility (ESRF, Grenoble)

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