EC Number   |
Protein Variants |
Reference |
|---|
   3.4.21.69 | D167F/D172G |
at saturating Ca2+ concentrations, the activation rates of the mutant and wild-type protein C by the thrombin-TM complex are comparable, but the mutant requires four-fold higher Ca2+ concentrations than wild-type APC to achieve half-maximal activation rates. When only thrombin is present, Ca2+ is not able to influence the activation of the D167F/D172G mutant, though Ca2+ effectively inhibits activation of wild-type protein C by thrombin |
718418 |
| 3.4.21.69 | D222E |
mutation of the Arg-Gly-Asp sequence abolishes both integrin binding and inhibition of neutrophil migration |
696948 |
| 3.4.21.69 | D35T/D36A |
site-directed mutagenesis, the mutant shows slightly increased factor Va proteolysis compared to the wild-type enzyme, the activation by protein S is reduced |
683627 |
| 3.4.21.69 | D36A/L38D/A39V |
site-directed mutagenesis, substitution of APC amino acid residues within the C-terminal end of the gamma-carboxyglutamic acid (Gla) domain with those of prothrombin result in an APC variant (APC-36A/L38D/A39V) with diminished capacity to inhibit thrombin generation. FVa degradation by this APC variant is normal in the absence of protein S, but completely defective when FVa degradation is dependent upon protein S cofactor activity |
752736 |
| 3.4.21.69 | D36A/L38D/A39V |
site-directed mutagenesis, the mutant shows no activation by protein S |
683627 |
| 3.4.21.69 | E149A |
the cytoprotective effects of the APC mutant are severely diminished, despite a normal cleavage of PAR-1 and normal binding to EPCR. E149A-APC expresses only 6% of the anti-apoptotic activity of wild-type APC in a staurosporine-induced apoptosis model in endothelial cells and was unable to down-regulate IL-6 release in lipopolysaccharide treated U937 monocytes |
718418 |
| 3.4.21.69 | E167A |
site-directed mutagenesis, the surface loop residue mutation eliminates the cytoprotective signaling properties of APC without affecting its anticoagulant activity, inability of E167A to exhibit significant protective activity in response to TNF-alpha-induced inflammatory events in endothelial cells |
683652 |
| 3.4.21.69 | E16D |
site-directed mutagenesis, the mutation causes aberrant Ca2+ binding and Gla domain misfolding |
683627 |
| 3.4.21.69 | E170A |
site-directed mutagenesis, the surface loop residue mutation eliminates the cytoprotective signaling properties of APC without affecting its anticoagulant activity, inability of E170A to exhibit significant protective activity in response to TNF-alpha-induced inflammatory events in endothelial cells |
683652 |
| 3.4.21.69 | E20A/V34M |
the mutation is associated with thrombotic complications, despite the fact that carriers of these mutations have normal protein C antigen levels and APC amidolytic activity |
718418 |
