Literature summary for 3.1.3.8 extracted from

Ullah, A.H.; Sethumadhavan, K.; Mullaney, E.J.
Monitoring of unfolding and refolding in fungal phytase (phyA) by dynamic light scattering (2005), Biochem. Biophys. Res. Commun., 327, 993-998.

Organism

Organism	UniProt	Comment	Textmining
Aspergillus ficuum	-	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.	-

Renatured (Commentary)

Renatured (Comment)	Organism
phytase is unfolded by guanidinium chloride and then refolded by removing the denaturant by dialysis. The unfolded phytase when diluted in assay medium refolds as a function of timr at 25°C and 37°C, but not at higher temperature. 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 ficuum

Renatured (Comment)

Organism

phytase is unfolded by guanidinium chloride and then refolded by removing the denaturant by dialysis. The unfolded phytase when diluted in assay medium refolds as a function of timr at 25°C and 37°C, but not at higher temperature. 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 ficuum

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Release 2023.1 (January 2023)