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Literature summary extracted from

  • Wyss, M.; Pasamontes, L.; Friedlein, A.; Remy, R.; Tessier, M.; Kronenberger, A.; Middendorf, A.; Lehmann, M.; Schoebelen, L.; Röthlisberger, U.; Kusznir, E.; Wahl, G.; Muller, F.; Lahm, H.W.; Vogel, K.; van Loon, A.P.G.M.
    Biophysical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolase): molecular size, glycosylation pattern, and engineering of proteolytic resistance (1999), Appl. Environ. Microbiol., 65, 359-366.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.8 expression in Aspergillus niger, Saccharomyces cerevisiae or Hansenula polymorpha Aspergillus fumigatus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.8 K186G/R187Q mutant protein with reduced susceptibility to proteolysis Aspergillus nidulans
3.1.3.8 R151L mutation has no effect on specific activity Aspergillus fumigatus
3.1.3.8 R151L/S152N mutant protein with reduced susceptibility to proteolysis Aspergillus fumigatus
3.1.3.8 S152N mutant protein with reduced susceptibility to proteolysis Aspergillus fumigatus
3.1.3.8 S152N mutation has no effect on specific activity Aspergillus fumigatus

General Stability

EC Number General Stability Organism
3.1.3.8 when expressed in Aspergillus niger, several fungal phytases are susceptible to limited proteolysis by proteases present in culture supernatant Aspergillus terreus
3.1.3.8 when expressed in Aspergillus niger, several fungal phytases are susceptible to limited proteolysis by proteases present in culture supernatant Aspergillus fumigatus
3.1.3.8 when expressed in Aspergillus niger, several fungal phytases are susceptible to limited proteolysis by proteases present in culture supernatant Aspergillus niger
3.1.3.8 when expressed in Aspergillus niger, several fungal phytases are susceptible to limited proteolysis by proteases present in culture supernatant Thermothelomyces heterothallicus
3.1.3.8 when expressed in Aspergillus niger, several fungal phytases are susceptible to limited proteolysis by proteases present in culture supernatant Thermomyces dupontii
3.1.3.8 when expressed in Aspergillus niger, several fungal phytases are susceptible to limited proteolysis by proteases present in culture supernatant Aspergillus nidulans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.8 39190
-
gel filtration Escherichia coli
3.1.3.8 45846
-
1 * 45846, calculation from nucleotide sequence Escherichia coli
3.1.3.8 47060
-
analytical ultracentrifugation Escherichia coli
3.1.3.8 47270
-
1 * 47270, SDS-PAGE Escherichia coli
3.1.3.8 48159
-
1 * 48159, Aspergillus terreus 9A1, calculation from nucleotide sequence Aspergillus terreus
3.1.3.8 48276
-
1 * 48276, calculation from nucleotide sequence Aspergillus fumigatus
3.1.3.8 48423
-
1 * 48423, Aspergillus niger Naturphos, calculation from nucleotide sequence Aspergillus niger
3.1.3.8 49775
-
1 * 49775, calculation from nucleotide sequence Thermomyces dupontii
3.1.3.8 50524
-
1 * 50524, calculation from nucleotide sequence Thermothelomyces heterothallicus
3.1.3.8 60550
-
1 * 60550, Aspergillus terreus 9A1, SDS-PAGE Aspergillus terreus
3.1.3.8 60740
-
analytical ultracentrifugation Aspergillus nidulans
3.1.3.8 60770
-
1 * 60770, batch 2, SDS-PAGE Aspergillus fumigatus
3.1.3.8 62890
-
1 * 62890, SDS-PAGE Thermothelomyces heterothallicus
3.1.3.8 64890
-
Aspergillus niger Natuphos, analytical ultracentrifugation Aspergillus niger
3.1.3.8 66150
-
analytical ultracentrifugation Thermothelomyces heterothallicus
3.1.3.8 66360
-
1 * 66360, Aspergillus niger Naturphos, SDS-PAGE Aspergillus niger
3.1.3.8 66430
-
1 * 66430, SDS-PAGE Aspergillus nidulans
3.1.3.8 70380
-
Aspergillus terreus 9A1, analytical ultracentrifugation Aspergillus terreus
3.1.3.8 70740
-
analytical ultracentrifugation Aspergillus fumigatus
3.1.3.8 71020
-
Aspergillus niger CB, analytical ultracentrifugation Aspergillus niger
3.1.3.8 72360
-
1 * 72360, batch 1, SDS-PAGE Aspergillus fumigatus
3.1.3.8 73800
-
gel filtration Thermothelomyces heterothallicus
3.1.3.8 74530
-
1 * 74530, Aspergillus niger CB, SDS-PAGE Aspergillus niger
3.1.3.8 77850
-
batch 1, gel filtration Aspergillus nidulans
3.1.3.8 78030
-
Aspergillus terreus CBS, analytical ultracentrifugation Aspergillus terreus
3.1.3.8 79900
-
Aspergillus terreus 9A1, gel filtration Aspergillus terreus
3.1.3.8 82110
-
1 * 82110, Aspergillus terreus CBS, SDS-PAGE Aspergillus terreus
3.1.3.8 82360
-
Aspergillus niger Natuphos, SDS-PAGE Aspergillus niger
3.1.3.8 86940
-
batch 2, gel filtration Aspergillus nidulans
3.1.3.8 90500
-
gel filtration Aspergillus fumigatus
3.1.3.8 103000
-
Aspergillus niger CB, gel filtration Aspergillus niger
3.1.3.8 115100
-
Aspergillus terreus CBS, gel filtration Aspergillus terreus
3.1.3.8 128400
-
1 * 128400, SDS-PAGE Thermomyces dupontii
3.1.3.8 136100
-
analytical ultracentrifugation Thermomyces dupontii

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 Aspergillus fumigatus
-
-
-
3.1.3.8 Aspergillus nidulans O00093
-
-
3.1.3.8 Aspergillus niger P34752
-
-
3.1.3.8 Aspergillus niger CB P34752
-
-
3.1.3.8 Aspergillus niger Naturphos P34752
-
-
3.1.3.8 Aspergillus terreus
-
-
-
3.1.3.8 Aspergillus terreus 9A1
-
-
-
3.1.3.8 Aspergillus terreus CBS
-
-
-
3.1.3.8 Escherichia coli
-
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.
-
3.1.3.8 Thermomyces dupontii O00096
-
-
3.1.3.8 Thermothelomyces heterothallicus O00107 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.
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.3.8 no modification no glycosylation Escherichia coli
3.1.3.8 side-chain modification extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts Aspergillus terreus
3.1.3.8 side-chain modification extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts Aspergillus fumigatus
3.1.3.8 side-chain modification extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts Aspergillus niger
3.1.3.8 side-chain modification extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts Thermothelomyces heterothallicus
3.1.3.8 side-chain modification extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts Thermomyces dupontii
3.1.3.8 side-chain modification extent of glycosylation is moderate when the fungal phytases are expressed in filamentous fungi, they are excessive when the phytases are expressed in yeasts Aspergillus nidulans
3.1.3.8 side-chain modification glycosylation sites: Asn residues 27, 105, 207, 230, 339 and 376 are glycosylated in all of the peptides analyzed. Asn59 and Asn120 are both glycosylated in only one of the peptides examined. No glycosylation at Asn352 and Asn338. The incomplete glycosylation of Asn residues 59 and 120 may be one of the reasons for the MW heterogeneity of Aspergillus niger phytase Aspergillus niger
3.1.3.8 side-chain modification glycosylation is moderate in Aspergillus niger, it is excessive and highly variable in Hansenula polymorpha and Saccharomyces cerevisiae Aspergillus fumigatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
Escherichia coli 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
Aspergillus terreus 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
Aspergillus fumigatus 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
Aspergillus niger 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
Thermothelomyces heterothallicus 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
Thermomyces dupontii 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
Aspergillus nidulans 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
Aspergillus niger Naturphos 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
Aspergillus terreus 9A1 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
Aspergillus niger CB 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
Aspergillus terreus CBS 1-L-myo-inositol 1,2,4,5,6-pentakisphosphate + myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
3.1.3.8 monomer 1 * 49034-49360, calculation from nucleotide sequence Aspergillus nidulans
3.1.3.8 monomer 1 * 49775, calculation from nucleotide sequence Thermomyces dupontii
3.1.3.8 monomer 1 * 60550, Aspergillus terreus 9A1, SDS-PAGE Aspergillus terreus
3.1.3.8 monomer 1 * 50524, calculation from nucleotide sequence Thermothelomyces heterothallicus
3.1.3.8 monomer 1 * 74530, Aspergillus niger CB, SDS-PAGE Aspergillus niger
3.1.3.8 monomer 1 * 62890, SDS-PAGE Thermothelomyces heterothallicus
3.1.3.8 monomer 1 * 66360, Aspergillus niger Naturphos, SDS-PAGE Aspergillus niger
3.1.3.8 monomer 1 * 72360, batch 1, SDS-PAGE Aspergillus fumigatus
3.1.3.8 monomer 1 * 66430, SDS-PAGE Aspergillus nidulans
3.1.3.8 monomer 1 * 60770, batch 2, SDS-PAGE Aspergillus fumigatus
3.1.3.8 monomer 1 * 128400, SDS-PAGE Thermomyces dupontii
3.1.3.8 monomer 1 * 82110, Aspergillus terreus CBS, SDS-PAGE Aspergillus terreus
3.1.3.8 monomer 1 * 45846, calculation from nucleotide sequence Escherichia coli
3.1.3.8 monomer 1 * 47270, SDS-PAGE Escherichia coli
3.1.3.8 monomer 1 * 48658-48973, Aspergillus niger CB, calculation from nucleotide sequence Aspergillus niger
3.1.3.8 monomer 1 * 48423, Aspergillus niger Naturphos, calculation from nucleotide sequence Aspergillus niger
3.1.3.8 monomer 1 * 48570-49166, Aspergillus terreus CBS, calculation from nucleotide sequence Aspergillus terreus
3.1.3.8 monomer 1 * 48276, calculation from nucleotide sequence Aspergillus fumigatus
3.1.3.8 monomer 1 * 48159, Aspergillus terreus 9A1, calculation from nucleotide sequence Aspergillus terreus