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Literature summary extracted from

  • Wang, X.Y.; Meng, F.G.; Zhou, H.M.
    The role of disulfide bonds in the conformational stability and catalytic activity of phytase (2004), Biochem. Cell Biol., 82, 329-334.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.1.3.8 denaturation in urea, in presence of 2 mM dithiothreitol, the inactivation and unfolding are greatly enhanced at the same concentration of denaturant, the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified Aspergillus niger
3.1.3.26 denaturation in urea, in presence of 2 mM dithiothreitol, the inactivation and unfolding are greatly enhanced at the same concentration of denaturant, the enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified Aspergillus niger

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.8 Urea in presence of 2 mM dithiothreitol, the inactivation and unfolding are greatly enhanced at the same concentration of denaturant. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified Aspergillus niger
3.1.3.26 Urea in presence of 2 mM dithiothreitol, the inactivation and unfolding are greatly enhanced at the same concentration of denaturant. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate has not been identified Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 Aspergillus niger
-
 The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-
3.1.3.26 Aspergillus niger
-
 The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.
-