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Literature summary extracted from

  • Shin, S.; Ha, N.C.; Oh, B.C.; Oh, T.K.; Oh, B.H.
    Enzyme mechanism and catalytic property of beta propeller phytase (2001), Structure, 9, 851-858.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.3.8 agriculture enzyme is used in animal feed to reduce phosphate pollution Bacillus subtilis
3.1.3.8 biotechnology the complete hydrolysis of phytate by the enzyme, which is proposed on the basis of its capability to cleave any phosphate group of phytate, is a highly desired property for the biotechnological application of the enzyme Bacillus subtilis
3.1.3.26 agriculture enzyme is used in animal feed to reduce phosphate pollution Bacillus subtilis
3.1.3.26 biotechnology the complete hydrolysis of phytate by the enzyme, which is proposed on the basis of its capability to cleave any phosphate group of phytate, is a highly desired property for the biotechnological application of the enzyme Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.8 the crystal structure of the enzyme in complex with phosphate reveals that two phosphates and four calcium ions are tightly bound at the active site Bacillus subtilis
3.1.3.26 the crystal structure of the enzyme in complex with phosphate reveals that two phosphates and four calcium ions are tightly bound at the active site Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.8 F- uncompetitive Bacillus subtilis
3.1.3.26 F- uncompetitive Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.8 Ca2+ the crystal structure of the enzyme in complex with inorganic phosphate reveals that two phosphates and four calcium ions are tightly bound at the active site Bacillus subtilis
3.1.3.26 Ca2+ the crystal structure of the enzyme in complex with inorganic phosphate reveals that two phosphates and four calcium ions are tightly bound at the active site Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 Bacillus subtilis
-
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 subtilis
-
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 the enzyme is able to hydrolyze any of the six phosphate groups of phytate. The reaction is likely to proceed through a direct attack of the metal-bridging water molecule on the phosphorous atom of a substrate and the subsequent stabilization of the pentavalent transition state by the bound calcium ions Bacillus subtilis ? + phosphate
-
?
3.1.3.26 myo-inositol hexakisphosphate + H2O the enzyme is able to hydrolyze any of the six phosphate groups of phytate. The reaction is likely to proceed through a direct attack of the metal-bridging water molecule on the phosphorous atom of a substrate and the subsequent stabilization of the pentavalent transition state by the bound calcium ions Bacillus subtilis ? + phosphate
-
?