EC Number   |
Protein Variants |
Reference |
|---|
    3.1.3.1 | A115V |
activity in U2OS cells after 48h after transfection: 0.1% |
694196 |
| 3.1.3.1 | A116T |
mutant responsible for hypophosphatasia shows negligible alkaline phosphatase activity and a weak dominant negative effect when co-expressed with the wild-type enzyme, mutant exists as a monomer and heterogeneously associated aggregates covalently linked via disulfide bonds in contrast to wild-type enzyme which exists as a homodimer |
714341 |
| 3.1.3.1 | A16V |
in combination with P275T the mutation causes infantile hypophosphatasia, 7.2% of wild-type activity |
666373 |
| 3.1.3.1 | biotechnology |
aqueous suspendible polymer nanostructures are prepared by simple microtome processing of electrospun nylon 6 nanofibers and are used to immobilize calf intestinal ALP by either covalent or noncovalent bioconjugation chemistries. Noncovalent immobilization of ALP to the mechanically cut nanofibers using a multi-stacked, layer-by-layer approach with the cationic polymer Sapphire II results in the highest enzyme loading. In terms of the overall catalytic performance of the various immobilized ALP systems, a single-stacked layer-by-layer assembly approach resulted in the highest level of enzymatic activity (30.1%) per unit mass of nanofiber support |
693963 |
| 3.1.3.1 | C201Y |
mutation identified in patient diagnosed with perinatal hypophosphatasia. Mutants exhibit a diminished alkaline phosphatase activity in the cells, where a 66 kDa immature form is predominant with a marginal amount of a 80 kDa mature form. The 66 kDa form exists as a monomer in contrast to a dimer form of wild-type. Only a small fraction of the mutant protein reaches cell surface as the 80 kDa mature form, most of the 66 kDa form is found to be endo-beta-N-acetylglucosaminidase H sensitive and rapidly degraded in proteasome following polyubiquitination |
729280 |
| 3.1.3.1 | C489S |
mutation identified in patient diagnosed with perinatal hypophosphatasia. Mutants exhibit a diminished alkaline phosphatase activity in the cells, where a 66 kDa immature form is predominant with a marginal amount of a 80 kDa mature form |
729280 |
| 3.1.3.1 | D101A |
the mutant shows 64fold decreased catalytic efficiency compared to the wild type enzyme |
750399 |
| 3.1.3.1 | D101A/D153A |
the mutant shows 190fold decreased catalytic efficiency compared to the wild type enzyme |
750399 |
| 3.1.3.1 | D101A/D153A/E322Y |
the mutant shows 48000000fold decreased catalytic efficiency compared to the wild type enzyme |
750399 |
| 3.1.3.1 | D101A/D153A/E322Y/K328A |
the mutant shows 320000000fold decreased catalytic efficiency compared to the wild type enzyme |
750399 |
