Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.1.3.8 (
phytase
)
1,997
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Biological recycling of inorganic phosphorus (P
i
) from organic phosphorus (P
o
) compounds by
phosphatase
-type enzymes, including phytases, is an important contributor to the pool of bioavailable P to plants and microorganisms. However, studies of mixed-substrate reactions with these enzymes are lacking. Here, we explore the reactivity of a
phytase
extract from the fungus
Aspergillus niger
toward a heterogeneous mixture containing, in addition to phytate, different structures of environmentally relevant P
o
compounds such as ribonucleotides and sugar phosphates. Using a high-resolution liquid chromatography-mass spectrometry method to monitor simultaneously the parent P
o
compounds and their by-products, we captured sequential substrate-specific evolution of P
i
from the mixture, with faster hydrolysis of multiphosphorylated compounds (phytate, diphosphorylated sugars, and di- and tri-phosphorylated ribonucleotides) than hydrolysis of monophosphorylated compounds (monophosphorylated sugars and monophosphorylated ribonucleotides). The interaction mechanisms and energies revealed by molecular docking simulations of each P
o
compound within the enzyme's active site explained the substrate hierarchy observed experimentally. Specifically, the favorable orientation for binding of the negatively charged phosphate moieties with respect to the positive potential surface of the active site was important. Collectively, our findings provide mechanistic insights about the broad but hierarchical role of
phytase
-type enzymes in P
i
recycling from the heterogeneous assembly of P
o
compounds in agricultural soils or wastes.
...
PMID:Hierarchical Reactivity of Enzyme-Mediated Phosphorus Recycling from Organic Mixtures by
Aspergillus niger
Phytase. 3330 54
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