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	
3.4.21.46	C44A	does not bind to the soluble receptor VEGFR-2/IgGFc	698902	
3.4.21.46	C53A	does not bind the soluble receptors VEGFR-2/IgGFc and VEGFR-3/IgGFc	698902	
3.4.21.46	C53A	does not bind to the soluble receptor VEGFR-2/IgGFc	698902	
3.4.21.46	G51C	can not induce cell survival, has increased dimer to monomer ratio	698902	
3.4.21.46	H133A	catalytically inactive	718398	
3.4.21.46	P43S	can not induce cell survival	698902	
3.4.21.46	R115C	activity like wild type	718398	
3.4.21.46	R157A	catalytically inactive	718398	
3.4.21.46	R202A	putative interaction with Glu230 in factor B, cleavage of factor B reduced to 20%, activity against peptides threefold increased	718398	
3.4.21.46	R202A	site-directed mutagenesis, the mutation R202A removes the Arg202-Asp177 salt bridge, the mutant variant has enhanced activity towards artificial peptides compared to the wild-type enzyme and simultaneously displays active and inactive conformations of the active site. Ensemble refinement reveals pronounced disorder in the exosite loops for this enzyme variant, reminiscent of thrombin in the absence of the stabilizing Na+ ion, structure analysis	731071	
3.4.21.46	R22I	can not induce cell survival	698902	
3.4.21.46	R22I/C25L	has biological activity comparable to that of the native protein in Ba/F3-VEGFR-2 cells, has increased dimer to monomer ratio	698902	
3.4.21.46	R22L	can not induce cell survival	698902	
3.4.21.46	R22L/C25L	has biological activity comparable to that of the native protein in Ba/F3-VEGFR-2 cells, has increased dimer to monomer ratio	698902	
3.4.21.46	S183A	catalytically inactive	718398	
3.4.21.46	S183A	site-directed mutagenesis, structure analysis	731071	
3.4.21.46	S81Y/T198S/S199W	site-directed mutagenesis, the mutation causes steric hindrance of Trp199 resulting in pronounced rearrangement of the proteinase active-site region, structure analysis	731071	
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	V203D	very low activity	718398