EC Number   |
Reaction |
Reference |
|---|
    3.1.3.1 | a phosphate monoester + H2O = an alcohol + phosphate |
Arg166 contributes to catalysis through binding interactions and through additional transition state stabilization that may arise from complementarity of the guanidinum group to the geometry of the trigonal bipyramidal transition state |
690980 |
| 3.1.3.1 | a phosphate monoester + H2O = an alcohol + phosphate |
double in-line displacement mechanism involving two-metal ion catalysis |
94615 |
| 3.1.3.1 | a phosphate monoester + H2O = an alcohol + phosphate |
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate |
-, 649164, 649342, 649366, 649496, 650744, 650752, 650793, 650882, 651016, 651199, 651349, 651385, 651458, 651568, 652408, 652666, 652689, 652838, 652952, 652967, 653130, 653452, 653584, 653756, 653964, 653965, 654004, 654022 |
| 3.1.3.1 | a phosphate monoester + H2O = an alcohol + phosphate |
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, active site structure, highly conserved in evolution of alkaline phosphatases |
652219 |
| 3.1.3.1 | a phosphate monoester + H2O = an alcohol + phosphate |
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, active site structure, mechanism |
652882 |
| 3.1.3.1 | a phosphate monoester + H2O = an alcohol + phosphate |
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, catalytically active His153 and His328 |
653130 |
| 3.1.3.1 | a phosphate monoester + H2O = an alcohol + phosphate |
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, substrate binding and active site structure |
653801 |
