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