3.4.21.46: complement factor D
This is an abbreviated version!
For detailed information about complement factor D, go to the full flat file.
Word Map on EC 3.4.21.46
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3.4.21.46
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angiogenesis
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angiogenic
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vessel
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metastasis
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neovascularization
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hypoxia
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artery
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hypoxia-inducible
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necrosis
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retinal
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antiangiogenic
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umbilical
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bevacizumab
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microvessels
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vein
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capillary
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factor-1
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huvecs
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vegfr-2
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collagen
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vasculature
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retinopathy
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eyes
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ovarian
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macular
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tumour
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tube
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microvascular
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mesenchymal
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anti-vegf
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lymphatic
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receptor-2
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pro-angiogenic
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bfgf
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intravitreal
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progression-free
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edema
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choroid
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metalloproteinase
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endothelium
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hypertension
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sprout
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matrigel
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paracrine
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lymph
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hif-1alpha
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mmp-9
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sunitinib
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drug development
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sorafenib
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vitreous
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medicine
- 3.4.21.46
- angiogenesis
-
angiogenic
- vessel
- metastasis
- neovascularization
- hypoxia
- artery
-
hypoxia-inducible
- necrosis
- retinal
-
antiangiogenic
-
umbilical
-
bevacizumab
-
microvessels
- vein
- capillary
- factor-1
- huvecs
- vegfr-2
- collagen
- vasculature
- retinopathy
- eyes
- ovarian
-
macular
- tumour
- tube
-
microvascular
- mesenchymal
-
anti-vegf
- lymphatic
- receptor-2
-
pro-angiogenic
- bfgf
-
intravitreal
-
progression-free
- edema
- choroid
- metalloproteinase
- endothelium
- hypertension
-
sprout
- matrigel
-
paracrine
- lymph
- hif-1alpha
- mmp-9
- sunitinib
- drug development
- sorafenib
- vitreous
- medicine
Reaction
selective cleavage of Arg-/-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor =
Synonyms
28 kDa protein, adipocyte, Adipsin, alternative complement pathway component Factor D, C3 convertase activator, C3 proactivator convertase, CFD, complement factor D/adipsin and kallikrein-like serine protease, convertase, C3 proactivator, Df, Df protein, endogenous vascular elastase, esterase, properdin factor D, factor D, factor D (complement), fD, PDGF-D, platelet-derived growth factor D, PoDAK, vascular endothelial growth factor, vascular endothelial growth factor D, VEGF-D
ECTree
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Engineering
Engineering on EC 3.4.21.46 - complement factor D
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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
C25A/P43S
has biological activity comparable to that of the native protein in Ba/F3-VEGFR-2 cells
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
C53A
R202A
R22I/C25L
has biological activity comparable to that of the native protein in Ba/F3-VEGFR-2 cells, has increased dimer to monomer ratio
R22L/C25L
has biological activity comparable to that of the native protein in Ba/F3-VEGFR-2 cells, has increased dimer to monomer ratio
S183A
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
S94Y/T214/S215W
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the triple mutant has a turnover number that is 16fold higher than that of wild type factor D
T214S/S215W
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more than 16fold incerease of the ratio of turnover number/KM-value
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putative interaction with Glu230 in factor B, cleavage of factor B reduced to 20%, activity against peptides threefold increased
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