5-phytase
| 5-phytase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.3.72 | ||||||||
| CAS number | Template:CAS | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, a 5-phytase (EC 3.1.3.72) is an enzyme that catalyzes the chemical reaction
- myo-inositol hexakisphosphate + H2O
1L-myo-inositol 1,2,3,4,6-pentakisphosphate + phosphate
Thus, the two substrates of this enzyme are myo-inositol hexakisphosphate and H2O, whereas its two products are 1L-myo-inositol 1,2,3,4,6-pentakisphosphate and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is myo-inositol-hexakisphosphate 5-phosphohydrolase.
Prevalence
Of the hundreds of phytase enzymes that have been characterized in the literature, only two have been characterized as 5-phytases.[1] A histidine acid phosphatases purified from lily pollen[2] and a protein tyrosine phosphatase-like phytase from Selenomonas ruminantium subsp. lactilytica[1] were both found to have specificity for the 5-phosphate position of myo-inositol hexakisphosphate.
Structural studies
As of late 2007, only the phytase purified from lily pollen had its structure solved, with PDB accession codes 1U24, 1U25, 1U26, 2B4O, 2B4P, and 2B4U.
References
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