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Literature summary 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.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.8 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
3.1.3.8 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
3.1.3.8 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
3.1.3.8 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
3.1.3.26 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
3.1.3.26 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
3.1.3.26 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
3.1.3.26 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

EC Number Organism UniProt Comment Textmining
3.1.3.8 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.
-
3.1.3.26 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)

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