EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.1.3.8 | hanging-drop vapour diffusion method at 22°C, crystal structure determined at 1.5 A resolution. The crystal structure clearly shows a partially occupied phosphohistidine residue, the transient reaction intermediate of the enzyme, at the active site | Aspergillus fumigatus |
3.1.3.26 | hanging-drop vapour diffusion method at 22°C, crystal structure determined at 1.5 A resolution. The crystal structure clearly shows a partially occupied phosphohistidine residue, the transient reaction intermediate of the enzyme, at the active site | Aspergillus fumigatus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.8 | Aspergillus fumigatus | - |
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 | Aspergillus fumigatus | - |
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 | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.1.3.8 | glycoprotein | six predicted N-glycosylation sites are observed to be glycosylated from the experimental electron density | Aspergillus fumigatus |
3.1.3.26 | glycoprotein | six predicted N-glycosylation sites are observed to be glycosylated from the experimental electron density | Aspergillus fumigatus |