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hexamer
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6 * 37000, gel filtration of the enzyme in a 6 M guanidine hydrochloride solution
homohexamer
6 * 64000, SDS-PAGE
?
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x * 54600, native enzyme, x * 39200, recombinant enzyme expressed in Lactobacillus casei, SDS-PAGE
?
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x * 76000, SDS-PAGE before deglycosylation
?
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x * 49000, SDS-PAGE after deglycosylation
?
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x * 48270, calculation from nucleotide sequence
?
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x * 66000, 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, SDS-PAGE
?
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x * 60000, glycosylated enzyme, SDS-PAGE, x * 47000, deglycosylated enzyme, SDS-PAGE
?
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x * 108000, SDS-PAGE
-
?
x * 41000, about, recombinant His6-tagged enzyme, SDS-PAGE
?
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x * 41000, about, recombinant His6-tagged enzyme, SDS-PAGE
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?
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x * 40000, SDS-PAGE
-
?
x * 39000, deglycosylated recombinant enzyme, SDS-PAGE
?
x * 45000, Pichia pastoris-expressed Phy168 after deglycosylation, SDS-PAGE
?
x * 60000, recombinant thioredoxin-tagged enzyme, SDS-PAGE, x * 42000, recombinant nontagged enzyme, SDS-PAGE
?
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x * 45000, Pichia pastoris-expressed Phy168 after deglycosylation, SDS-PAGE
-
?
-
x * 46000, SDS-PAGE
-
?
-
x * 60000, recombinant thioredoxin-tagged enzyme, SDS-PAGE, x * 42000, recombinant nontagged enzyme, SDS-PAGE
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?
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x * 46000, SDS-PAGE
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?
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x * 41800, calculated
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?
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x * 43000, SDS-PAGE
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?
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x * 39000, deglycosylated recombinant enzyme, SDS-PAGE
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?
x * 68000, recombinant enzyme, SDS-PAGE
?
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x * 68000, recombinant enzyme, SDS-PAGE
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?
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x * 47000, SDS-PAGE
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?
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x * 53000, SDS-PAGE, wild-type
?
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x * 64000, SDS-PAGE
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?
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x * 42000, SDS-PAGE
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?
x * 51000, SDS-PAGE, x * 51900, calculated
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x * 51000, SDS-PAGE, x * 51900, calculated
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?
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x * 43250, SDS_PAGE
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?
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x * 43000, SDS-PAGE
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?
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x * 45300, calculated
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x * 45000, mature protein, calculated
?
x * 65000, SDS-PAGE, x * 50481, sequence calculation
?
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x * 65000, SDS-PAGE
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?
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x * 65000, SDS-PAGE, x * 50481, sequence calculation
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?
x * 63000, recombinant His-tagged enzyme, SDS-PAGE, x * 47750, sequence calculation
?
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x * 40000, about, SDS-PAGE
?
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x * 40000, about, SDS-PAGE
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?
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x * 68852, calculated
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x * 68852, calculated
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?
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x * 45000, SDS-PAGE
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?
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x * 35400, extracellular enzyme, SDS-PAGE
?
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x * 45000, isozymes RO1 and RO2, SDS-PAGE
?
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x * 63000, about, sequence calculation
?
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x * 63000, about, sequence calculation
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?
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x * 46000, SDS-PAGE
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?
x * 46000, recombinant His6-tagged phytase PhyH49, SDS-PAGE
?
x * 66000, recombinant His6-tagged phytase PhyB49, SDS-PAGE
?
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x * 46000, recombinant His6-tagged phytase PhyH49, SDS-PAGE
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?
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x * 66000, recombinant His6-tagged phytase PhyB49, SDS-PAGE
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?
x * 59000-65000, recombinant glycosylated enzyme from Pichia pastoris, SDS-PAGE, x * 45000, recombinant deglycosylated enzyme from Pichia pastoris, SDS-PAGE
?
x * 45795, sequence calcualtion, x * 48000, SDS-PAGE
?
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x * 45795, sequence calcualtion, x * 48000, SDS-PAGE
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?
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x * 70000, recombinant enzyme, SDS-PAGE
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x * 70000, recombinant enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE
?
x * 53000, sequence calculation, x * 55000, recombinant His-tagged enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE
?
x * 90000, native enzyme, SDS-PAGE
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x * 90000, native enzyme, SDS-PAGE
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?
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x * 53000, sequence calculation, x * 55000, recombinant His-tagged enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE
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?
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x * 90000, native enzyme, SDS-PAGE
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?
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x * 53000, sequence calculation, x * 55000, recombinant His-tagged enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE
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?
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x * 90000, native enzyme, SDS-PAGE
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?
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x * 53000, sequence calculation, x * 55000, recombinant His-tagged enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE
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?
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x * 60530, calculated
?
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x * 45741, mass spectrometry
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x * 45000, recombinant wild-type enzyme, SDS-PAGE
?
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x * 46000, SDS-PAGE, x * 45900, calculated
?
-
x * 45900, calculated for mature protein, x * 48000, SDS-PAGE
?
x * 46000, SDS-PAGE, x * 45200, calculated
?
x * 46000, SDS-PAGE, x * 46100, calculated
dimer
2 * 80000, native PAGE
dimer
-
2 * 80000, native PAGE
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dimer
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2 * 70000-72000, SDS-PAGE
homodimer
2 * 53800, about, isozyme LlALP1, sequence calculation
homodimer
2 * 56200, about, isozyme LlALP2, sequence calculation
monomer
-
1 * 53000, SDS-PAGE and native PAGE
monomer
-
1 * 53000, SDS-PAGE and native PAGE
-
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 85000-100000, SDS-PAGE
monomer
-
1 * 85000, SDS-PAGE
monomer
-
1 * 65500, SDS-PAGE
monomer
-
1 * 85000-100000, SDS-PAGE
-
monomer
-
1 * 65500, SDS-PAGE
-
monomer
-
1 * 76000, SDS-PAGE
monomer
-
1 * 72360, batch 1, SDS-PAGE
monomer
-
1 * 60770, batch 2, SDS-PAGE
monomer
-
1 * 48276, calculation from nucleotide sequence
monomer
1 * 49034-49360, calculation from nucleotide sequence
monomer
1 * 66430, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
monomer
1 * 74530, Aspergillus niger CB, SDS-PAGE
monomer
1 * 66360, Aspergillus niger Naturphos, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE after deglycosylation
monomer
-
x * 48800, calculation from nucleotide sequence
monomer
-
1 * 90000-100000, SDS-PAGE
monomer
1 * 48658-48973, Aspergillus niger CB, calculation from nucleotide sequence
monomer
1 * 48423, Aspergillus niger Naturphos, calculation from nucleotide sequence
monomer
-
1 * 84000, SDS-PAGE
monomer
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1 * 74530, Aspergillus niger CB, SDS-PAGE
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monomer
-
1 * 66360, Aspergillus niger Naturphos, SDS-PAGE
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monomer
-
1 * 48658-48973, Aspergillus niger CB, calculation from nucleotide sequence
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monomer
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1 * 48423, Aspergillus niger Naturphos, calculation from nucleotide sequence
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monomer
-
1 * 74530, Aspergillus niger CB, SDS-PAGE
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monomer
-
1 * 66360, Aspergillus niger Naturphos, SDS-PAGE
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monomer
-
1 * 48658-48973, Aspergillus niger CB, calculation from nucleotide sequence
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monomer
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1 * 48423, Aspergillus niger Naturphos, calculation from nucleotide sequence
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monomer
-
1 * 55000, SDS-PAGE after deglycosylation
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monomer
1 * 80000, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
-
monomer
-
1 * 60550, Aspergillus terreus 9A1, SDS-PAGE
monomer
-
1 * 82110, Aspergillus terreus CBS, SDS-PAGE
monomer
-
1 * 48570-49166, Aspergillus terreus CBS, calculation from nucleotide sequence
monomer
-
1 * 48159, Aspergillus terreus 9A1, calculation from nucleotide sequence
monomer
-
1 * 60550, Aspergillus terreus 9A1, SDS-PAGE
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monomer
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1 * 82110, Aspergillus terreus CBS, SDS-PAGE
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monomer
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1 * 48570-49166, Aspergillus terreus CBS, calculation from nucleotide sequence
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monomer
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1 * 48159, Aspergillus terreus 9A1, calculation from nucleotide sequence
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monomer
-
1 * 60550, Aspergillus terreus 9A1, SDS-PAGE
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monomer
-
1 * 82110, Aspergillus terreus CBS, SDS-PAGE
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monomer
-
1 * 48570-49166, Aspergillus terreus CBS, calculation from nucleotide sequence
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monomer
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1 * 48159, Aspergillus terreus 9A1, calculation from nucleotide sequence
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monomer
-
1 * 44000, SDS-PAGE
monomer
-
1 * 44000, SDS-PAGE
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monomer
-
1 * 44000, SDS-PAGE
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monomer
1 * 43000, SDS-PAGE, 1 * 46000, about, sequence calculation
monomer
-
1 * 43000, SDS-PAGE, 1 * 46000, about, sequence calculation
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monomer
-
1 * 71000, SDS-PAGE
monomer
KM873028
1 * 52000, recombinant enzyme, SDS-PAGE
monomer
-
1 * 62000, SDS-PAGE
monomer
-
1 * 45846, calculation from nucleotide sequence
monomer
-
1 * 47270, SDS-PAGE
monomer
1 * 66000, deglycosylated recombinant enzyme, SDS-PAGE
monomer
-
1 * 92900, gel filtration
monomer
-
1 * 92900, gel filtration
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monomer
-
1 * 57000, phytase LP11 and LP12, SDS-PAGE
monomer
-
1 * 64000, phytase LP2, SDS-PAGE
monomer
1 * 61090, sequence calculation, 1 * 61089, mass spectrometry, 1 * 60000, SDS-PAGE
monomer
-
1 * 61090, sequence calculation, 1 * 61089, mass spectrometry, 1 * 60000, SDS-PAGE
-
monomer
-
1 * 56000, gel filtration
monomer
-
1 * 42000, SDS-PAGE
monomer
1 * 48000, native enzyme, SDS-PAGE
monomer
-
x * 40000, SDS-PAGE
monomer
-
1 * 120000, SDS-PAGE
monomer
1 * 49775, calculation from nucleotide sequence
monomer
1 * 128400, SDS-PAGE
monomer
1 * 50524, calculation from nucleotide sequence
monomer
1 * 62890, SDS-PAGE
monomer
1 * 66000, deglycosylated recombinant enzyme, SDS-PAGE
monomer
-
1 * 66000, deglycosylated recombinant enzyme, SDS-PAGE
-
monomer
-
1 * 42000, recombinant His-tagged enzyme, SDS-PAGE
monomer
-
1 * 14000, SDS-PAGE
monomer
1 * 66000, deglycosylated recombinant enzyme, SDS-PAGE
additional information
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peptide mass fingerprinting, MALDI-TOF mass spectrometry
additional information
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peptide mass fingerprinting, MALDI-TOF mass spectrometry
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additional information
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a broad protein band of 85000-100000 Da is observed after SDS-PAGE
additional information
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SDS-PAGE gives two broad bands in the regions 73000 Da and 100000 Da
additional information
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a broad proptein band of 85000-100000 Da is observed after SDS-PAGE
additional information
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structural model of the wild type and mutant enzymes, overview
additional information
three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
additional information
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three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
additional information
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structural model of the wild type and mutant enzymes, overview
-
additional information
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three-dimensional structure analysis of wild-type phytase and mutants P212H, T255E, S238D, G377T, and D461N
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additional information
molecular model of phytase constructed by homology modeling method, overview
additional information
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molecular model of phytase constructed by homology modeling method, overview
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additional information
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the dual-domain beta-propeller phytase PhyH from Bacillus sp. HJB17 contains an incomplete N-terminal beta-propeller phytase domain, PhyH-DI, residues 41-318, and a typical beta-propeller phytase domain, PhyH-DII, residues 319-644, at the C-terminus. Modelling of the three-dimensional structures of domains PhyH-DI and PhyH-DII, PhyH-DI is predicted to have a five-blade propeller structure and PhyH-DII a six-blade beta-propeller containing five four-stranded sheets and one five-stranded sheet
additional information
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the dual-domain beta-propeller phytase PhyH from Bacillus sp. HJB17 contains an incomplete N-terminal beta-propeller phytase domain, PhyH-DI, residues 41-318, and a typical beta-propeller phytase domain, PhyH-DII, residues 319-644, at the C-terminus. Modelling of the three-dimensional structures of domains PhyH-DI and PhyH-DII, PhyH-DI is predicted to have a five-blade propeller structure and PhyH-DII a six-blade beta-propeller containing five four-stranded sheets and one five-stranded sheet
-
additional information
the enzyme contains an N-terminal incomplete domain, residues 29-297, i.e. domain N, and a typical beta-propeller phytase domain at the C terminus
additional information
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the enzyme contains an N-terminal incomplete domain, residues 29-297, i.e. domain N, and a typical beta-propeller phytase domain at the C terminus
-
additional information
the ASR1 phytase polypeptide chain is organized into an alpha and an alpha,beta domain, and the active site is located in a positively charged cleft between the domains
additional information
AppAS contains three potential sites of N-glycosylation, a putative signal peptide of 22 amino acids at N-terminal end and 8 cysteine residues among which 99-130, 200-210, 404-413 are the most possible disulfide bond pairs. The calculated molecular mass of the protein with and without the signal sequence are about 47 and 45 kDa, respectively
additional information
the recombinant enzyme StPhy is composed of 26.65% alpha-helices, 5.26% beta-sheets and 68.09% random coils at pH 5.0 and 60°C. The three-dimensional structure of rStPhy displays characteristic signature sequences, RHGXRXP and HD, of HAP phytases, three-dimensional modeling, overview. Tryptophan residues surrounded by negative charges play a key role in maintaining structural integrity of rStPhy
additional information
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three-dimensional structural model, overview
additional information
amino acid sequence analysis and molecular modeling, overview
additional information
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amino acid sequence analysis and molecular modeling, overview