Phytase: Difference between revisions
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== Function == | == Function == | ||
'''Phytase''' (PHYT) catalyzes the hydrolysis of phytate (myo-inositol hexakisphosphate) to myo-inositol and inorganic phosphate <ref>PMID:9025298</ref>. PHYT are a subclass of the histidine acid phosphatase<ref>PMID:9025298</ref>. Phytate is the main phosphorus storage system in plant seeds. Phytate is indigestible by monogastric animals and humans<ref>PMID:32271147</ref>. | '''Phytase''' or '''purple acid phosphatase''' or '''acidphosphatase''' (PHYT) catalyzes the hydrolysis of phytate (myo-inositol hexakisphosphate) to myo-inositol and inorganic phosphate <ref>PMID:9025298</ref>. PHYT are a subclass of the histidine acid phosphatase<ref>PMID:9025298</ref>. Phytate is the main phosphorus storage system in plant seeds. Phytate is indigestible by monogastric animals and humans<ref>PMID:32271147</ref>. | ||
== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
The 3D structure of <scene name='91/917455/Cv/6'>the complex between phytase and myo-inositol hexakisphosphate</scene> shows the extensive contacts of the phosphoryl groups of the substrate binding in the <scene name='91/917455/Cv/8'>highly basic binding pocket</scene><ref>PMID:22139834</ref>. Positively charged residues are colored in magenta; water molecules are shown red spheres. | The 3D structure of <scene name='91/917455/Cv/6'>the complex between phytase and myo-inositol hexakisphosphate</scene> shows the extensive contacts of the phosphoryl groups of the substrate binding in the <scene name='91/917455/Cv/8'>highly basic binding pocket</scene><ref>PMID:22139834</ref>. Positively charged residues are colored in magenta; water molecules are shown as red spheres. | ||
==3D structures of phytase== | ==3D structures of phytase== | ||