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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

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

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.46 complement factor D

Engineering

Engineering on EC 3.4.21.46 - complement factor D

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
C25I
is mainly in a presumably covalently bound dimeric form
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
C25V
is mainly in a presumably covalently bound dimeric form
C44A
does not bind to the soluble receptor VEGFR-2/IgGFc
G51C
can not induce cell survival, has increased dimer to monomer ratio
H133A
-
catalytically inactive
P43S
can not induce cell survival
R115C
-
activity like wild type
R157A
-
catalytically inactive
R202A
R22I
can not induce cell survival
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
can not induce cell survival
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
-
6fold increase in turnover number
S94Y/T214/S215W
-
the triple mutant has a turnover number that is 16fold higher than that of wild type factor D
T214S/S215W
-
more than 16fold incerease of the ratio of turnover number/KM-value
T638G
-
factor D deficient mutant
T640C
-
factor D deficient mutant
V203D
-
very low activity