EC Number   |
Protein Variants |
Reference |
|---|
   3.4.21.45 | A222G |
secretion of mutant protein significantly lower compared to wild-type when expressed in human embryonic kidney cells. Mutant cleaves the alpha'-chains of complement factor C4b and C3b as efficiently as wild-type in solution. Compared to wild-type mutant A22G shows impaired cleavage of complement factor C3b on the surface of sheep erythrocytes. Mutant cleaves C3b alpha'chain on the surface of endothelial cells (HUVEV-cells) as efficiently as wild-type |
708380 |
| 3.4.21.45 | C196S |
naturally occuring mutation, causes a failure in secretion of the enzyme |
732231 |
| 3.4.21.45 | C237Y |
mutation affects secretion, is expressed in smaller amounts as the wild-type. Does not degrade C4b and C3b as efficiently as the wild-type |
697732 |
| 3.4.21.45 | C25F |
mutant is as efficiently expressed in human embryonic kidney cells as wild-type, mutant protein is not secreted. Mutant is sensitive to EndoH digestion, indicating that it does not reach the late Golgi compartment and is retained in the endoplasmic reticulum |
708380 |
| 3.4.21.45 | D104S |
site-directed mutagenesis, altered kinetics compared to the wild-type |
732047 |
| 3.4.21.45 | D207N/Q219A |
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) and Vmax similar to wild-type |
708380 |
| 3.4.21.45 | D207N/Q219A/M220A/K221Q |
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) and Vmax similar to wild-type |
708380 |
| 3.4.21.45 | D26N/K27Q/F29A/Q31A |
Km (tert-butyloxycarbonyl-Asp(benzyl)-Pro-Arg-7-amido-4-methylcoumarin) similar to wild-type, Vmax significantly increased compared to wild-type. Compared to wild-type mutant shows strongly impaired activity in degradation of fluid-phase complement factor C4b or C3b and in the degradation of surface-bound C3b deposited on sheep erythrocytes |
708380 |
| 3.4.21.45 | D385N/K387S |
site-directed mutagenesis, altered kinetics compared to the wild-type |
732047 |
| 3.4.21.45 | D420N/N422T |
site-directed mutagenesis, the mutation in the serine protease domain decreases the binding of the enzyme to substrate analogue C3met |
732047 |
