Literature summary for 3.1.3.26 extracted from

Mullaney, E.J.; Daly, C.B.; Kim, T.; Porres, J.M.; Lei, X.G.; Sethumadhavan, K.; Ullah, A.H.
Site-directed mutagenesis of Aspergillus niger NRRL 3135 phytase at residue 300 to enhance catalysis at pH 4.0 (2002), Biochem. Biophys. Res. Commun., 297, 1016-1020.

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Protein Variants

Protein Variants	Comment	Organism
K300D	specific activity of the mutant enzyme is substantially lowered. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.71	Aspergillus niger
K300E	mutation results in an increase of the hydrolysis of phythic acid of 56% and 19% at pH 4.0 and pH 5.0 at 37°C respectively. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.74	Aspergillus niger
K300R	specific activity of the mutant enzyme is substantially lowered. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.81	Aspergillus niger
K300T	specific activity of the mutant enzyme is substantially lowered. The ratio of activity at pH 6 to activity at pH 4 that is 3.29 for the wild-type enzyme is lowered to 1.68	Aspergillus niger

Organism

Organism	UniProt	Comment	Textmining
Aspergillus niger	-	NRRL 3135. 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.	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
myo-inositol hexakisphosphate + H2O	-	Aspergillus niger	? + phosphate	-	?

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Release 2023.1 (January 2023)