Phytase
FunctionPhytase or purple acid phosphatase or acidphosphatase (PHYT) catalyzes the hydrolysis of phytate (myo-inositol hexakisphosphate) to myo-inositol and inorganic phosphate [1]. PHYT are a subclass of the histidine acid phosphatase[2]. Phytate is the main phosphorus storage system in plant seeds. Phytate is indigestible by monogastric animals and humans[3]. RelevancePHYT is found in plant material and is used to increase the nutritional quality of grains, legumes, seeds and corn. PHYT is used as a dietary supplement in broiler nutrition[4]. Studies show that supplementing PHYT can reduce the need for calcium phosphate and increase digestive health. Structural highlightsThe 3D structure of shows the extensive contacts of the phosphoryl groups of the substrate binding in the [5]. Positively charged residues are colored in magenta; water molecules are shown as red spheres. 3D structures of phytase
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ReferencesReferences
- ↑ Mitchell DB, Vogel K, Weimann BJ, Pasamontes L, van Loon AP. The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila. Microbiology. 1997 Jan;143 ( Pt 1):245-52. PMID:9025298
- ↑ Mitchell DB, Vogel K, Weimann BJ, Pasamontes L, van Loon AP. The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila. Microbiology. 1997 Jan;143 ( Pt 1):245-52. PMID:9025298
- ↑ Kim OH, Booth CJ, Choi HS, Lee J, Kang J, Hur J, Jung WJ, Jung YS, Choi HJ, Kim H, Auh JH, Kim JW, Cha JY, Lee YJ, Lee CS, Choi C, Jung YJ, Yang JY, Im SS, Lee DH, Cho SW, Kim YB, Park KS, Park YJ, Oh BC. High-phytate/low-calcium diet is a risk factor for crystal nephropathies, renal phosphate wasting, and bone loss. Elife. 2020 Apr 9;9. pii: 52709. doi: 10.7554/eLife.52709. PMID:32271147 doi:http://dx.doi.org/10.7554/eLife.52709
- ↑ Gonzalez-Uarquin F, Kenez A, Rodehutscord M, Huber K. Dietary phytase and myo-inositol supplementation are associated with distinct plasma metabolome profile in broiler chickens. Animal. 2020 Mar;14(3):549-559. doi: 10.1017/S1751731119002337. Epub 2019 Oct 15. PMID:31610823 doi:http://dx.doi.org/10.1017/S1751731119002337
- ↑ Gruninger RJ, Dobing S, Smith AD, Bruder LM, Selinger LB, Wieden HJ, Mosimann SC. Substrate binding in protein-tyrosine phosphatase-like inositol polyphosphatases. J Biol Chem. 2012 Mar 23;287(13):9722-30. doi: 10.1074/jbc.M111.309872. Epub 2011, Dec 2. PMID:22139834 doi:http://dx.doi.org/10.1074/jbc.M111.309872