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Literature summary for 3.1.3.8 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
Search for more literature for 3.1.3.8

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
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.
-
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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]

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

Ki Value [mM]

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