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Literature summary extracted from

  • Oh, B.C.; Chang, B.S.; Park, K.H.; Ha, N.C.; Kim, H.K.; Oh, B.H.; Oh, T.K.
    Calcium-dependent catalytic activity of a novel phytase from Bacillus amyloliquefaciens DS11 (2001), Biochemistry, 40, 9669-9676.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.8 overexpression of a N-terminal His-tagged phytase in Escherichia coli Bacillus amyloliquefaciens
3.1.3.26 overexpression of a N-terminal His-tagged phytase in Escherichia coli Bacillus amyloliquefaciens

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.8 D258A turnover number of mutant enzyme is 20.87% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.8 D314A inactive mutant enzyme Bacillus amyloliquefaciens
3.1.3.8 D55A turnover number of mutant enzyme is 0.21% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.8 E211A inactive mutant enzyme Bacillus amyloliquefaciens
3.1.3.8 E227A turnover number of mutant enzyme is 9.29% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.8 E260A inactive mutant enzyme Bacillus amyloliquefaciens
3.1.3.8 K76E turnover number of mutant enzyme is 0.26% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.8 K76R turnover number of mutant enzyme is 0.3% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.8 R122E turnover number of mutant enzyme is 48.81% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.8 R122K turnover number of mutant enzyme is 17.11% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.8 Y159A turnover number of mutant enzyme is 0.19% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.8 Y159A turnover number of mutant enzyme is 0.37% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.8 Y159F inactive mutant enzyme Bacillus amyloliquefaciens
3.1.3.26 D258A turnover number of mutant enzyme is 20.87% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.26 D314A inactive mutant enzyme Bacillus amyloliquefaciens
3.1.3.26 D55A turnover number of mutant enzyme is 0.21% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.26 E211A inactive mutant enzyme Bacillus amyloliquefaciens
3.1.3.26 E227A turnover number of mutant enzyme is 9.29% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.26 E260A inactive mutant enzyme Bacillus amyloliquefaciens
3.1.3.26 K76E turnover number of mutant enzyme is 0.26% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.26 K76R turnover number of mutant enzyme is 0.3% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.26 R122E turnover number of mutant enzyme is 48.81% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.26 R122K turnover number of mutant enzyme is 17.11% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.26 Y159A turnover number of mutant enzyme is 0.19% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.26 Y159A turnover number of mutant enzyme is 0.37% of that of the wild-type enzyme Bacillus amyloliquefaciens
3.1.3.26 Y159F inactive mutant enzyme Bacillus amyloliquefaciens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.8 Ca2+ free, not complexed with phytate, competitive inhibitor Bacillus amyloliquefaciens
3.1.3.8 phytate free, not complexed with Ca2+, competitive inhibitor Bacillus amyloliquefaciens
3.1.3.26 Ca2+ free, not complexed with phytate, competitive inhibitor Bacillus amyloliquefaciens
3.1.3.26 phytate free, not complexed with Ca2+, competitive inhibitor Bacillus amyloliquefaciens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.8 0.138
-
 phytate wild-type enzyme Bacillus amyloliquefaciens
3.1.3.8 0.747
-
 phytate mutant enzyme E227A Bacillus amyloliquefaciens
3.1.3.8 0.914
-
 phytate mutant enzyme D55A Bacillus amyloliquefaciens
3.1.3.8 0.934
-
 phytate mutant enzyme Y159H Bacillus amyloliquefaciens
3.1.3.8 0.967
-
 phytate mutant enzyme K76E Bacillus amyloliquefaciens
3.1.3.8 2.505
-
 phytate mutant enzyme R122E Bacillus amyloliquefaciens
3.1.3.8 3.046
-
 phytate mutant enzyme R122K Bacillus amyloliquefaciens
3.1.3.8 3.542
-
 phytate mutant enzyme D258A Bacillus amyloliquefaciens
3.1.3.8 8.661
-
 phytate mutant enzyme Y159A Bacillus amyloliquefaciens
3.1.3.8 11.99
-
 phytate mutant enzyme K76R Bacillus amyloliquefaciens
3.1.3.26 0.138
-
 phytate wild-type enzyme Bacillus amyloliquefaciens
3.1.3.26 0.747
-
 phytate mutant enzyme E227A Bacillus amyloliquefaciens
3.1.3.26 0.914
-
 phytate mutant enzyme D55A Bacillus amyloliquefaciens
3.1.3.26 0.934
-
 phytate mutant enzyme Y159H Bacillus amyloliquefaciens
3.1.3.26 0.967
-
 phytate mutant enzyme K76E Bacillus amyloliquefaciens
3.1.3.26 2.505
-
 phytate mutant enzyme R122E Bacillus amyloliquefaciens
3.1.3.26 3.046
-
 phytate mutant enzyme R122K Bacillus amyloliquefaciens
3.1.3.26 3.542
-
 phytate mutant enzyme D258A Bacillus amyloliquefaciens
3.1.3.26 8.661
-
 phytate mutant enzyme Y159A Bacillus amyloliquefaciens
3.1.3.26 11.99
-
 phytate mutant enzyme K76R Bacillus amyloliquefaciens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.8 Ca2+ rapid equilibrium ordered mechanism in which binding of ca2+ to the active site is necessary for the essential activation of the enzyme. Ca2+ turns out to be also required for the substrate because the enzyme is only able to hydrolyze the calcium-phytate complex. 4 mol of Ca2+ bind to 1 mol of phytate Bacillus amyloliquefaciens
3.1.3.26 Ca2+ rapid equilibrium ordered mechanism in which binding of ca2+ to the active site is necessary for the essential activation of the enzyme. Ca2+ turns out to be also required for the substrate because the enzyme is only able to hydrolyze the calcium-phytate complex. 4 mol of Ca2+ bind to 1 mol of phytate Bacillus amyloliquefaciens

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 Bacillus amyloliquefaciens
-
 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 Bacillus amyloliquefaciens S11
-
 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 Bacillus amyloliquefaciens
-
 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 Bacillus amyloliquefaciens S11
-
 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 rapid equilibrium ordered mechanism in which binding of Ca2+ to the active site is necessary for the essential activation of the enzyme. Ca2+ turns out to be also required for the substrate because the enzyme is only able to hydrolyze the calcium-phythate complex Bacillus amyloliquefaciens ? + phosphate
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O rapid equilibrium ordered mechanism in which binding of Ca2+ to the active site is necessary for the essential activation of the enzyme. Ca2+ turns out to be also required for the substrate because the enzyme is only able to hydrolyze the calcium-phythate complex Bacillus amyloliquefaciens S11 ? + phosphate
-
 ?
3.1.3.26 myo-inositol hexakisphosphate + H2O rapid equilibrium ordered mechanism in which binding of Ca2+ to the active site is necessary for the essential activation of the enzyme. Ca2+ turns out to be also required for the substrate because the enzyme is only able to hydrolyze the calcium-phythate complex Bacillus amyloliquefaciens ? + phosphate
-
 ?
3.1.3.26 myo-inositol hexakisphosphate + H2O rapid equilibrium ordered mechanism in which binding of Ca2+ to the active site is necessary for the essential activation of the enzyme. Ca2+ turns out to be also required for the substrate because the enzyme is only able to hydrolyze the calcium-phythate complex Bacillus amyloliquefaciens S11 ? + phosphate
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.8 0.82
-
 phytate mutant enzyme K76R Bacillus amyloliquefaciens
3.1.3.8 27
-
 phytate mutant enzyme Y159H Bacillus amyloliquefaciens
3.1.3.8 117
-
 phytate mutant enzyme D55A Bacillus amyloliquefaciens
3.1.3.8 5530
-
 phytate mutant enzyme E227A Bacillus amyloliquefaciens
3.1.3.8 5532
-
 phytate mutant enzyme E227A Bacillus amyloliquefaciens
3.1.3.8 11800
-
 phytate mutant enzyme R122K Bacillus amyloliquefaciens
3.1.3.8 11810
-
 phytate mutant enzyme R122K Bacillus amyloliquefaciens
3.1.3.8 12400
-
 phytate mutant enzyme D258A Bacillus amyloliquefaciens
3.1.3.8 12430
-
 phytate mutant enzyme D258A Bacillus amyloliquefaciens
3.1.3.8 29060
-
 phytate mutant enzyme R122E Bacillus amyloliquefaciens
3.1.3.8 29100
-
 phytate mutant enzyme R122E Bacillus amyloliquefaciens
3.1.3.8 59550
-
 phytate wild-type enzyme Bacillus amyloliquefaciens
3.1.3.8 59600
-
 phytate wild-type enzyme Bacillus amyloliquefaciens
3.1.3.26 0.82
-
 phytate mutant enzyme K76R Bacillus amyloliquefaciens
3.1.3.26 27
-
 phytate mutant enzyme Y159H Bacillus amyloliquefaciens
3.1.3.26 117
-
 phytate mutant enzyme D55A Bacillus amyloliquefaciens
3.1.3.26 5530
-
 phytate mutant enzyme E227A Bacillus amyloliquefaciens
3.1.3.26 5532
-
 phytate mutant enzyme E227A Bacillus amyloliquefaciens
3.1.3.26 11800
-
 phytate mutant enzyme R122K Bacillus amyloliquefaciens
3.1.3.26 11810
-
 phytate mutant enzyme R122K Bacillus amyloliquefaciens
3.1.3.26 12400
-
 phytate mutant enzyme D258A Bacillus amyloliquefaciens
3.1.3.26 12430
-
 phytate mutant enzyme D258A Bacillus amyloliquefaciens
3.1.3.26 29060
-
 phytate mutant enzyme R122E Bacillus amyloliquefaciens
3.1.3.26 29100
-
 phytate mutant enzyme R122E Bacillus amyloliquefaciens
3.1.3.26 59550
-
 phytate wild-type enzyme Bacillus amyloliquefaciens
3.1.3.26 59600
-
 phytate wild-type enzyme Bacillus amyloliquefaciens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.3.8 0.97
-
 Ca2+ free, not complexed with phytate, competitive inhibitor Bacillus amyloliquefaciens
3.1.3.8 2.3
-
 phytate free, not complexed with Ca2+, competitive inhibitor Bacillus amyloliquefaciens
3.1.3.26 0.97
-
 Ca2+ free, not complexed with phytate, competitive inhibitor Bacillus amyloliquefaciens
3.1.3.26 2.3
-
 phytate free, not complexed with Ca2+, competitive inhibitor Bacillus amyloliquefaciens