EC Number   |
Protein Variants |
Reference  |
|---|
   3.4.21.46 | S94Y |
6fold increase in turnover number |
36587 |
| 3.4.21.46 | S94Y/T214/S215W |
the triple mutant has a turnover number that is 16fold higher than that of wild type factor D |
36587 |
| 3.4.21.46 | T214S/S215W |
more than 16fold incerease of the ratio of turnover number/KM-value |
36587 |
| 3.4.21.46 | T638G |
factor D deficient mutant |
668074 |
| 3.4.21.46 | T640C |
factor D deficient mutant |
668074 |
| 3.4.21.46 | C25A |
has increased activity compared to the native VEGF-DDELTANDELTAC. Efficiently binds to the soluble receptor VEGFR-2/IgGFc. The C25A mutant behaves mainly as a monomeric protein on SDS-PAGE under reducing conditions but as a dimeric protein under non-reducing conditions. It induces VEGFR-2 Tyr-1175 phosphorylation |
698902 |
| 3.4.21.46 | C25A/P43S |
has biological activity comparable to that of the native protein in Ba/F3-VEGFR-2 cells |
698902 |
| 3.4.21.46 | C25I |
is mainly in a presumably covalently bound dimeric form |
698902 |
| 3.4.21.46 | C25L |
has increased activity compared to the native VEGF-DDELTANDELTAC, the C25L mutant is the most active mutant and is mainly in a presumably covalently bound dimeric form, has highest affinity to bind soluble receptor VEGFR-2/IgGFc. It induces VEGFR-2 Tyr-1175 phosphorylation |
698902 |
| 3.4.21.46 | C25V |
is mainly in a presumably covalently bound dimeric form |
698902 |
