ArticlePlant communications2022
Structure of a cereal purple acid phytase provides new insights to phytate degradation in plants.
Article in Plant communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Inositol Thiophosphates as Inhibitors of Mammalian, Plant, and Fungal Phytases.ACS chemical biology · 2026Article
- Genome-wide identification, characterization and expression profiling of purple acid phosphatases under variable phosphorus regimes in lentil (Lens culinaris Medik.).BMC plant biology · 2025Article
- Phosphorus-specific, liquid chromatography inductively coupled plasma mass spectrometry for analysis of inositol phosphate and inositol pyrophosphate metabolism.The Biochemical journal · 2025Article
- Enzyme immobilization with plant-based polysaccharides through complex coacervation.Lebensmittel-Wissenschaft + [i.e. und] Technologie. Food science + technology. Science + technologie alimentaire · 2025Article
- Analysis of Inositol Phosphates, Diphosphoinositol Phosphates, and Their Analogs by HPLC on an Acid-Compatible Stationary Phase with Detection by Complexation with Ferric Ion.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Structural and functional profile of phytases across the domains of life.Current research in structural biology · 2024Review
- Selectivity in Enzymatic Phosphorus Recycling from Biopolymers: Isotope Effect, Reactivity Kinetics, and Molecular Docking with Fungal and Plant Phosphatases.Environmental science & technology · 2022Article
- Insights to the Structural Basis for the Stereospecificity of theInternational journal of molecular sciences · 2022Article
- The importance of residue-level filtering and the Top2018 best-parts dataset of high-quality protein residues.Protein science : a publication of the Protein Society · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 3 countries.
Funding
Abstract
Grain phytate, a mixed metal ion salt of inositol hexakisphosphate, accounts for 60%-80% of stored phosphorus in plants and is a potent antinutrient of non-ruminant animals including humans. Through neofunctionalization of purple acid phytases (PAPhy), some cereals such as wheat and rye have acquired particularly high mature grain phytase activity. As PAPhy activity supplies phosphate, liberates metal ions necessary for seedling emergence, and obviates antinutrient effects of phytate, its manipulation and control are targeted crop traits. Here we show the X-ray crystal structure of the b2 isoform of wheat PAPhy induced during germination. This high-resolution crystal structure suggests a model for phytate recognition that, validated by molecular dynamics simulations, implicates elements of two sequence inserts (termed PAPhy motifs) relative to a canonical metallophosphoesterase (MPE) domain in forming phytate-specific substrate specificity pockets. These motifs are well conserved in PAPhys from monocot cereals, enzymes which are characterized by high specificity for phytate. Tested by mutagenesis, residues His229 in PAPhy motif 4 and Lys410 in the MPE domain, both conserved in PAPhys, are found to strongly influence phytase activity. These results explain the observed phytase activity of cereal PAPhys and open the way to the rational engineering of phytase activity
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Registered trials
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