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Information on EC 3.4.21.46 - complement factor D and Organism(s) Homo sapiens and UniProt Accession P00746

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.46 complement factor D
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P00746 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
selective cleavage of Arg-/-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor
Synonyms
vascular endothelial growth factor, vegf-d, adipsin, factor d, pdgf-d, complement factor d, vascular endothelial growth factor d, platelet-derived growth factor d, endogenous vascular elastase, podak, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28 kDa protein, adipocyte
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-
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-
Adipsin
-
-
-
-
C3 convertase activator
-
-
-
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C3 proactivator convertase
-
-
-
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convertase, C3 proactivator
-
-
-
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endogenous vascular elastase
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-
-
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esterase, properdin factor D
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-
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factor D
factor D (complement)
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platelet-derived growth factor D
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vascular endothelial growth factor
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vascular endothelial growth factor D
VEGF-D
CAS REGISTRY NUMBER
COMMENTARY hide
37213-56-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
benzyloxycarbonyl-L-Lys-thiobenzyl ester + H2O
benzyloxycarbonyl-L-Lys + thiobenzoate
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Lys-thiobenzylester + H2O
?
show the reaction diagram
-
-
-
?
complement component C3bB + H2O
?
show the reaction diagram
complement factor B + H2O
?
show the reaction diagram
-
-
-
?
complement factor B + H2O
fragment Ba + fragment Bb
show the reaction diagram
-
-
-
?
Ac-Lys-Arg-4-nitroanilide + H2O
Ac-Lys-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-Gly-L-Lys methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Benzoyl-L-Arg methyl ester + H2O
Benzoyl-L-Arg + methanol
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Arg-benzyl thioester + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Lys thiobenzyl ester + H2O
benzyloxycarbonyl-Lys + phenylmethanethiol
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Lys-Arg-isobutyl thioester + H2O
?
show the reaction diagram
-
-
-
-
?
complement component C3bB + H2O
?
show the reaction diagram
-
-
-
-
?
complement factor B + H2O
?
show the reaction diagram
-
-
-
-
?
factor B + H2O
Ba + Bb
show the reaction diagram
-
-
smaller and larger cleavage subunit of factor B, respectively
-
?
factor B + H2O
Bb fragment + Ba fragment
show the reaction diagram
N-Acetyl-L-Tyr ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzoyl-Ile-Glu-Gly-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-acetyl-L-Arg methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-acetyl-L-Lys methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-tosyl-L-Lys methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Nepsilon-carbobenzoxy-L-Lys methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
p-tosyl-L-Arg methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
pro-convertase C3bB + H2O
active C3 convertase C3bBb + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
complement component C3bB + H2O
?
show the reaction diagram
complement factor B + H2O
?
show the reaction diagram
-
-
-
?
complement factor B + H2O
fragment Ba + fragment Bb
show the reaction diagram
-
-
-
?
complement component C3bB + H2O
?
show the reaction diagram
-
-
-
-
?
complement factor B + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,2S)-2-([4-[3-(aminomethyl)anilino]quinazolin-2-yl]amino)cyclohexane-1-carboxylic acid
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(2-fluoro-3-trifluoromethoxyphenyl)-amide]
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(2-fluoro-3-trifluoromethylphenyl)-amide]
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-chlorophenyl)-amide]
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-difluoromethoxyphenyl)-amide]
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-methoxyphenyl)-amide]
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-trifluoromethoxyphenyl)-amide]
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 3-[(3-bromophenyl)amide] 2-[(1-carbamoyl-1H-indol-3-yl)amide]
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 3-[(6-bromo-pyridin-2-yl)-amide] 2-[(1-carbamoyl-1H-indol-3-yl)-amide]
-
(1R,3S,5R)-2-azabicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(6-trifluoromethyl-pyridin-2-yl)-amide]
-
(1S,2S,5R)-3-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 3-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(2S)-2-([4-[3-(aminomethyl)anilino]pyrimidin-2-yl]amino)-3-methylbutanoic acid
-
(2S)-2-([4-[3-(aminomethyl)anilino]quinazolin-2-yl]amino)-3-methylbutanoic acid
-
(2S)-N2-(diphenylmethyl)-N1-(1-methyl-1H-indol-3-yl)pyrrolidine-1,2-dicarboxamide
-
(2S,4R)-4-fluoro-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxy-phenyl)-amide]
-
(2S,4R)-4-methyl-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(2S,4S)-4-amino-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(2S,4S)-4-fluoro-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(2S,4S)-4-hydroxy-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(2S,4S)-4-methyl-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxy-phenyl)-amide
-
(R)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(S)-4,4-difluoro-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(S)-piperidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(S)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(S)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-methyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
1-(2-((1R,3S,5R)-3-((6-bromopyridin-2-yl)carbamoyl)-2-azabicyclo[3.1.0]hexan-2-yl)-2-oxoethyl)-1H-indazole-3-carboxamide
-
1-(2-[(1R,3S,5R)-3-[(6-bromopyridin-2-yl)carbamoyl]-2-azabicyclo[3.1.0]hexan-2-yl]-2-oxoethyl)-1H-indazole-3-carboxamide
-
1-[2-[(1R,3S,5R)-3-[[(1R)-1-(3-chloro-2-fluorophenyl)ethyl]carbamoyl]-2-azabicyclo[3.1.0]hexan-2-yl]-2-oxoethyl]-1H-indazole-3-carboxamide
-
1-[2-[(1R,3S,5R)-3-[[(1R)-1-(3-chloro-2-fluorophenyl)ethyl]carbamoyl]-2-azabicyclo[3.1.0]hexan-2-yl]-2-oxoethyl]-1H-pyrazolo[3,4-c]pyridine-3-carboxamide
-
3'-(aminomethyl)-5-(3-methylbutanamido)-N-(1,2,3,4-tetrahydronaphthalen-1-yl)[1,1'-biphenyl]-3-carboxamide (incorrect configuration definition!)
-
3'-(aminomethyl)-N-benzyl[1,1'-biphenyl]-3-carboxamide
-
3'-(aminomethyl)-N-[(1R)-1,2,3,4-tetrahydronaphthalen-1-yl][1,1'-biphenyl]-3-carboxamide
-
3'-(aminomethyl)-N-[(1S)-1,2,3,4-tetrahydronaphthalen-1-yl][1,1'-biphenyl]-3-carboxamide
3-([3-[3-(aminomethyl)anilino]-1H-pyrazolo[3,4-d]pyrimidin-4-yl]amino)phenol
-
3-[[(2-carbamoyl-1H-indol-5-yl)oxy]methyl]benzoic acid
anti-factor D Fab fragment
an Escherichia coli-expressed, humanized Fab fragment, derived from monoclonal antibody 166-32, and designed as specific enzyme inhibitor targeting the exosite. Anti-factor D Fab fragment prevents factor D-mediated proteolytic activation of its macromolecular substrate C3bB, but not proteolysis of a small synthetic substrate, indicating that the inhibitor does not block access of the substrate to the catalytic site, binding structure and inhibitory mechanism, overview. The structures show that the AFD-binding site includes surface loops of the enzyme that form part of the enzyme's exosite. Anti-factor D Fab fragment inhibits the enzyme proteolytic function by interfering with macromolecular substrate access rather than by inhibiting the enzyme catalysis
-
isatoic anhydride
-
methyl 2-([[(2S)-2-[[3-(trifluoromethoxy)phenyl]carbamoyl]pyrrolidine-1-carbonyl]amino]methyl)benzoate
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]-2-phenylacetamide
-
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]-3-methylbutanamide
-
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]-3-phenylpropanamide
-
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]acetamide
-
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]benzamide
-
[2-([3'-[(1S)-1-amino-2-hydroxyethyl][1,1'-biphenyl]-3-yl]methoxy)phenyl]acetic acid
selective inhibitor
3,4-dichloroisocoumarin
-
mechanism-based inactivation
diisopropyl fluorophosphate
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
complement factor B
the enzyme factor D is activated by its substrate factor B through interactions outside the active site. The substrate-binding, or exosite, region displays a well defined and rigid conformation
-
matriptase
-
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.95 - 11.44
Benzyloxycarbonyl-Lys-thiobenzyl ester
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3 - 21.3
Benzyloxycarbonyl-Lys-thiobenzyl ester
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.084
(1R,2S)-2-([4-[3-(aminomethyl)anilino]quinazolin-2-yl]amino)cyclohexane-1-carboxylic acid
Homo sapiens
at pH 7.5 and 25°C
0.000012
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(2-fluoro-3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.000023
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(2-fluoro-3-trifluoromethylphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.00015
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-chlorophenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.00015
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-difluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.00032
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-methoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.00005
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.000045
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 3-[(3-bromophenyl)amide] 2-[(1-carbamoyl-1H-indol-3-yl)amide]
Homo sapiens
at pH 7.5 and 25°C
0.000006
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 3-[(6-bromo-pyridin-2-yl)-amide] 2-[(1-carbamoyl-1H-indol-3-yl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.000014
(1R,3S,5R)-2-azabicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(6-trifluoromethyl-pyridin-2-yl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.00065
(1S,2S,5R)-3-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 3-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.044
(2S)-2-([4-[3-(aminomethyl)anilino]pyrimidin-2-yl]amino)-3-methylbutanoic acid
Homo sapiens
at pH 7.5 and 25°C
0.075
(2S)-2-([4-[3-(aminomethyl)anilino]quinazolin-2-yl]amino)-3-methylbutanoic acid
Homo sapiens
at pH 7.5 and 25°C
0.0058
(2S)-N2-(diphenylmethyl)-N1-(1-methyl-1H-indol-3-yl)pyrrolidine-1,2-dicarboxamide
Homo sapiens
at pH 7.5 and 25°C
0.00005
(2S,4R)-4-fluoro-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxy-phenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.00085
(2S,4R)-4-methyl-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.0005
(2S,4S)-4-amino-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.0007
(2S,4S)-4-fluoro-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.0014
(2S,4S)-4-hydroxy-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.0003
(2S,4S)-4-methyl-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxy-phenyl)-amide
Homo sapiens
at pH 7.5 and 25°C
0.03
(R)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.00045
(S)-4,4-difluoro-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.022
(S)-piperidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.0005
(S)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.02
(S)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-methyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.000006
1-(2-[(1R,3S,5R)-3-[(6-bromopyridin-2-yl)carbamoyl]-2-azabicyclo[3.1.0]hexan-2-yl]-2-oxoethyl)-1H-indazole-3-carboxamide
Homo sapiens
at pH 7.5 and 25°C
0.000017
1-[2-[(1R,3S,5R)-3-[[(1R)-1-(3-chloro-2-fluorophenyl)ethyl]carbamoyl]-2-azabicyclo[3.1.0]hexan-2-yl]-2-oxoethyl]-1H-pyrazolo[3,4-c]pyridine-3-carboxamide
Homo sapiens
at pH 7.5 and 25°C
0.0034
3'-(aminomethyl)-5-(3-methylbutanamido)-N-(1,2,3,4-tetrahydronaphthalen-1-yl)[1,1'-biphenyl]-3-carboxamide (incorrect configuration definition!)
Homo sapiens
at pH 7.5 and 25°C
0.31
3'-(aminomethyl)-N-benzyl[1,1'-biphenyl]-3-carboxamide
Homo sapiens
at pH 7.5 and 25°C
0.098
3'-(aminomethyl)-N-[(1R)-1,2,3,4-tetrahydronaphthalen-1-yl][1,1'-biphenyl]-3-carboxamide
Homo sapiens
at pH 7.5 and 25°C
0.037 - 0.054
3'-(aminomethyl)-N-[(1S)-1,2,3,4-tetrahydronaphthalen-1-yl][1,1'-biphenyl]-3-carboxamide
0.02
3-([3-[3-(aminomethyl)anilino]-1H-pyrazolo[3,4-d]pyrimidin-4-yl]amino)phenol
Homo sapiens
at pH 7.5 and 25°C
0.014
methyl 2-([[(2S)-2-[[3-(trifluoromethoxy)phenyl]carbamoyl]pyrrolidine-1-carbonyl]amino]methyl)benzoate
0.043
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]-2-phenylacetamide
Homo sapiens
at pH 7.5 and 25°C
0.12
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]-3-methylbutanamide
Homo sapiens
at pH 7.5 and 25°C
0.14
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]-3-phenylpropanamide
Homo sapiens
at pH 7.5 and 25°C
0.69
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]acetamide
Homo sapiens
at pH 7.5 and 25°C
0.257
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]benzamide
Homo sapiens
at pH 7.5 and 25°C
0.000012
[2-([3'-[(1S)-1-amino-2-hydroxyethyl][1,1'-biphenyl]-3-yl]methoxy)phenyl]acetic acid
Homo sapiens
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1 - 7.2
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
parasitized red blood cells, pRBC, infected by Plasmodium falciparum, rosetting serum dependent for the strains FCR3S1.2 and Malayan Camp
Manually annotated by BRENDA team
-
low levels of vegf-D mRNA
Manually annotated by BRENDA team
-
PDGF-D is widely expressed in most neointimas in arteries exhibiting the chronic arteriopathy of chronic allograft nephropathy and is only weakly expressed in a small proportion of sclerotic arteries. The neointimal cells expressing PDGF-D are alpha-smooth muscle actin-expressing cells, but not infiltrating macrophages or endothelial cells
Manually annotated by BRENDA team
-
PDGF-D high-expressing breast cancer cell line SUM-149 is more invasive compared to low-expressing cell lines
Manually annotated by BRENDA team
-
normal hepatocytes synthesize factor D constitutively. The liver may be a major source of plasma factor D
Manually annotated by BRENDA team
-
low levels of vegf-D mRNA
Manually annotated by BRENDA team
-
PDGF-D is uniformly expressed in visceral epithelial cells and arteriolar wall in normal kidneys, kidneys with acute vascular rejection, and kidneys with chronic allograft nephropathy. In kidneys with acute vascular rejection, PDGF-D is expressed in arterial medial smooth muscle cells, some adventitial cells, and some neointimal cells that also have alpha-smooth muscle actin expression
Manually annotated by BRENDA team
-
low PDGF-D expressing breast cancer cell line is less invasive
Manually annotated by BRENDA team
-
PDGF-D expressing breast cancer cell lines are more invasive compared to non-expressing cell lines
Manually annotated by BRENDA team
-
low PDGF-D expressing breast cancer cell line is less invasive
Manually annotated by BRENDA team
-
low levels of vegf-D mRNA
Manually annotated by BRENDA team
-
5- to 8fold higher amounts of vegf-D mRNA as the other gastric cell lines
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
knockdown of complement factor D in senescent fibroblasts significantly reduces the increase of matrix metalloproteinase 1 in the co-cultured young fibroblasts
physiological function
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CFAD_HUMAN
253
0
27033
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
-
Westernblot
22900
-
equilibrium sedimentation
23000
-
x * 23000, SDS-PAGE
24000
-
x * 24000, SDS-PAGE
24376
-
x * 24376, calculation from nucleotide sequence
25000
-
x * 25000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
SDS-PAGE and immunoblotting. VEGF-DDeltaNDeltaC homodimer is antiparallel and has an elongated shape but is flat at the central part. It has three subunit interface cysteines C25, C44 and C53
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
profactor D
no modification
-
no potential N-glycosylation site, no carbohydrate is present in the purified protein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of profactor D
in complex with inhibitors, sitting drop vapor diffusion method, using 25% (w/v) PEGME 3350, 100 mM Bis-Tris pH 5.5 or 30% (w/v) PEG MME 2000, 0.1 M thiocyanate
in complex with inhibitors, vapor diffusion method, using 22 or 27% (w/v) PEG3350, 50 mM NaCl and 100 mM HEPES/NaOH, pH 7.5 at 20°C
purified enzyme in complex with anti-factor D Fab fragment, sitting drop vapor diffusion method, 30 mg/ml protein in 20 mM HEPES, pH 7.2, and 200 mM NaCl, is mixed with an equal volume of crystallization buffer containing 0.1 M Tris-HCl, pH 8.5, 0.2 M ammonium phosphate, 50% 2-methyl-2,4-pentanediol, and 0.01 M hexamine cobalt(III) chloride, 6 days, 4°C, X-ray diffraction structure determination and analysis at 2.4 A resolution
structure of native factor D and a complex formed with isatoic anhydride inhibitor
wild-type enzyme, mutants R202A and S81Y/T198S/S199W, and enzyme mutant S183A in ternary complex with C3bB, hanging drop vapour diffusion technique, mixing of 10 mg/ml protein solution with reservoir solution consisting of 15% w/v PEG 6000, 50 mM MES-NaOH pH 6.0, 18°C, 6 days, X-ray diffraction structure determination and analysis at 1.8 A, 2.8 A, 2.0 A, and 3.5 A resolution, respectively, molecular replacement and ensemble refinement
S183A mutant protein in complex with pro-convertase C3bB
-
structure of diisopropyl fluorophosphate-inhibited factor D
-
wild type and mutant factor D, expression in CHO cells
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
S183A
site-directed mutagenesis, structure analysis
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
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
-
putative interaction with Glu230 in factor B, cleavage of factor B reduced to 20%, activity against peptides threefold increased
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
-
catalytically inactive
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing causes approximately 30% loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, no aggregation occurs, stable
-
4°C, 0.1 M Tris-HCl, 0.2 M NaCl, 2 mM EDTA, pH 8.0, 0.02% w/v NaN3, several months, about 10% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme and inhibitor by gel filtration
recombinant soluble wild-type and mutant enzymes from HEK-293-E cells by cation exchange chromatography and gel filtration
cation-exchange chromatography,gelfiltration
-
HisTrap column chromatography
-
Sephacryl S-100 and DEAE Sepharose fast flow column chromatography, 4°C
-
VEGF-DDELTANDELTAC and the three cysteine mutants purified by metal affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
transient expression of wild-type and mutant enzymes in HEK-293-E cells from pUPE.05.05 expression vectors, the recombinant proteins are secreted
baculoviral VEGF-D or adenoviral VEGF-D expressed in the rabbit eye. VEGF-D expression shows a similar pattern in the retina and retinal pigment epithelium layer after baculoviral and adenoviral transduction. At 6 days after gene transfer, both viruses show dose-dependent increase in the expression of human VEGF-D in the vitreous humour
-
expressed in breast cancer cell lines MDA-MB-468 and MCF-7 cells
-
expressed in HEK293-E cells
-
expressed in HeLa S3 cells
-
gastric cells transiently transfected with the pGL3-based vegf-D reporter gene construct vegf-D(-2011/+110), which comprises nucleotides -2011/+110 of the human vegf-D gene
-
mutants transiently transfected into 293T cells. The native VEGF-DDELTANDELTAC and mutants expressed in a larger scale in insect cells using BVboostFG baculovirus expression system
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme gene and protein expression are increased in the dermal layer of skin specimens from aged subjects (more than70 years old), compared to young subjects (younger than 20 years old)
deguelin, a rotenoid of the flavonoid family, significantly down-regulates the expression of VEGF-D both at the mRNA and protein level in VEGF-D transfected LL/2 Lewis lung cells
-
in lung cancer cell lines, interleukin-7/interleukin-7 receptor increase the expression of VEGF-D and phosphorylation of c-Fos/c-Jun, induce c-Fos and c-Jun heterodimer formation, and enhance c-Fos/c-Jun DNA binding activity to regulate VEGF-D expression
-
overexpression of PDGF-D in PDGF-D low expressing breast cancer cell lines MDA-MB-468 and MCF-7 cells by cDNA transfection shows increased cell proliferation. PDGF-D overexpression is positively correlated with the expression of Notch-1 and Jagged-1, and the expression of mesenchymal markers (Vimentin and ZEB-2) with concomitant decreased expression of epithelial marker E-cadherin. PDGF-D over-expression leads to increased DNA binding activity of NF-kappaB
-
silencing the expression of PDGF-D by siRNA in PDGF-D high expressing MDA-MB-231 and SUM-149 cells shows decreased cell proliferation and increased apoptosis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme's exosite is a target for design of specific inhibitors for inhibition of the pathway complement activation in advanced dry age-related macular degeneration
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Harper, J.W.; Hemmi, K.; Powers, J.C.
Reaction of serine proteases with substituted isocoumarins: discovery of 3,4-dichloroisocoumarin, a new general mechanism based serine protease inhibitor
Biochemistry
24
1831-1841
1985
Homo sapiens
Manually annotated by BRENDA team
Davis III, A.E.; Alper, C.A.
Factor D of the alternative complement pathway
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
549-553
1984
Homo sapiens
-
Manually annotated by BRENDA team
Reid, K.B.M.; Johnson, D.M.A.; Gagnon, J.; Prohaska, R.
Preparation of human factor D of the alternative pathway of complement
Methods Enzymol.
80
134-143
1981
Homo sapiens
Manually annotated by BRENDA team
Davies, A.E.; Zalut, C.; Rosen, F.S.; Alper, C.A.
Human factor D of the alternative complement pathway. Physicochemical characteristics and N-terminal amino acid sequence
Biochemistry
18
5082-5087
1979
Homo sapiens
Manually annotated by BRENDA team
Lesavre, P.H.; Hugli, T.E.; Esser, A.F.; Mller-Eberhard, H.J.
The alternative pathway C3/C5 convertase: chemical basis of factor B activation
J. Immunol.
123
529-534
1979
Homo sapiens
Manually annotated by BRENDA team
Volanakis, J.E.; Schrohenloher, R.E.; Stroud, R.M.
Human factor D of the alternative complement pathway: purification and characterization
J. Immunol.
119
337-342
1977
Homo sapiens
Manually annotated by BRENDA team
Jing, H.; Macon, K.J.; Moore, D.; DeLucas, L.J.; Volanakis, J.E.; Narayana, S.V.L.
Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D
EMBO J.
18
804-814
1999
Homo sapiens (P00746)
Manually annotated by BRENDA team
Balke, N.; Holtkamp, U.; Hrl, W.H.; Tschesche, H.
Inhibition of degranulation of human polymorphonuclear leukocytes by complement factor D
FEBS Lett.
371
300-302
1995
Homo sapiens
Manually annotated by BRENDA team
Kim, S.; Narayana, S.V.L.; Volanakis, J.E.
Crystal structure of a complement factor D mutant expressing enhanced catalytic activity [published erratum appears in J Biol Chem 1995 Dec 29;270(52):31414
J. Biol. Chem.
270
24399-24405
1995
Homo sapiens
Manually annotated by BRENDA team
Cole, L.B.; Chu, N.; Kilpatrick, J.M.; Volanakis, J.E.; Narayana, S.V.L.; Babu, Y.S.
Structure of diisopropyl fluorophosphate-inhibited factor D
Acta Crystallogr. Sect. D
53
143-150
1997
Homo sapiens
Manually annotated by BRENDA team
Jing, H.; Babu, Y.S.; Moore, D.; Kilpatrick, J.M.; Liu, X.Y.; Volanakis, J.E.; Narayana, S.V.L.
Structures of native and complexed complement factor D: implications of the atypical His57 conformation and self-inhibitory loop in the regulation of specific serine protease activity
J. Mol. Biol.
282
1061-1081
1998
Homo sapiens (P00746)
Manually annotated by BRENDA team
Catana, E.; Schifferli, J.A.
Purification of human complement factor D from the peritoneal fluid of patients on chronic ambulatory peritoneal dialysis
J. Immunol. Methods
138
265-271
1991
Homo sapiens
Manually annotated by BRENDA team
Miyata, T.; Oda, O.; Inagi, R.; Sugiyama, S.; Miyama, A.; Maeda, K.; Nakashima, I.; Yamanaka, N.
Molecular and functional identification and purification of complement component factor D from urine of patients with chronic renal failure
Mol. Immunol.
27
637-644
1990
Homo sapiens
Manually annotated by BRENDA team
Volanakis, J.E.; Barnum, S.R.; Kilpatrick, J.M.
Purification and properties of human factor D
Methods Enzymol.
223
82-97
1993
Homo sapiens
Manually annotated by BRENDA team
Kitano, E.; Kitamura, H.
Synthesis of factor D by normal human hepatocytes
Int. Arch. Allergy Immunol.
122
299-302
2000
Homo sapiens
Manually annotated by BRENDA team
Sprong, T.; Roos, D.; Weemaes, C.; Neeleman, C.; Geesing, C.L.; Mollnes, T.E.; van Deuren, M.
Deficient alternative complement pathway activation due to factor D deficiency by 2 novel mutations in the complement factor D gene in a family with meningococcal infections
Blood
107
4865-4870
2006
Homo sapiens
Manually annotated by BRENDA team
Oda, O.; Nagaya, T.; Ogawa, H.
Analysis of protein absorbed by LDL column (Liposorber) with special reference to complement component factor D
Clin. Chim. Acta
342
155-160
2004
Homo sapiens
Manually annotated by BRENDA team
Harris, C.L.; Abbott, R.J.; Smith, R.A.; Morgan, B.P.; Lea, S.M.
Molecular dissection of interactions between components of the alternative pathway of complement and decay accelerating factor (CD55)
J. Biol. Chem.
280
2569-2578
2005
Homo sapiens
Manually annotated by BRENDA team
Luginbuehl, A.; Nikolic, M.; Beck, H.P.; Wahlgren, M.; Lutz, H.U.
Complement factor D, albumin, and immunoglobulin G anti-band 3 protein antibodies mimic serum in promoting rosetting of malaria-infected red blood cells
Infect. Immun.
75
1771-1777
2007
Homo sapiens (P00746)
Manually annotated by BRENDA team
Li, L.; Liu, B.; Li, X.; Yang, S.; Xiao, J.; Chen, M.; Zhang, Y.; Ma, J.
Vascular endothelial growth factor D and intratumoral lymphatics as independent prognostic factors in epithelial ovarian carcinoma
Anat. Rec. (Hoboken)
292
562-569
2009
Homo sapiens (O43915), Homo sapiens
Manually annotated by BRENDA team
Schaefer, G.; Wissmann, C.; Hertel, J.; Lunyak, V.; Hoecker, M.
Regulation of vascular endothelial growth factor D by orphan receptors hepatocyte nuclear factor-4 alpha and chicken ovalbumin upstream promoter transcription factors 1 and 2
Cancer Res.
68
457-466
2008
Homo sapiens
Manually annotated by BRENDA team
Liu, G.; Changsirikulchai, S.; Hudkins, K.L.; Banas, M.C.; Kowalewska, J.; Yang, X.; Wietecha, T.A.; Volpone, J.; Gilbertson, D.G.; Alpers, C.E.
Identification of platelet-derived growth factor D in human chronic allograft nephropathy
Hum. Pathol.
39
393-402
2008
Homo sapiens
Manually annotated by BRENDA team
Toivanen, P.I.; Nieminen, T.; Viitanen, L.; Alitalo, A.; Roschier, M.; Jauhiainen, S.; Markkanen, J.E.; Laitinen, O.H.; Airenne, T.T.; Salminen, T.A.; Johnson, M.S.; Airenne, K.J.; Ylae-Herttuala, S.
Novel vascular endothelial growth factor D (VEGF-D) variants with increased biological activity
J. Biol. Chem.
284
16037-1648
2009
Homo sapiens (O43915)
Manually annotated by BRENDA team
Kinnunen, K.; Kalesnykas, G.; Maehoenen, A.J.; Laidinen, S.; Holma, L.; Heikura, T.; Airenne, K.; Uusitalo, H.; Ylae-Herttuala, S.
Baculovirus is an efficient vector for the transduction of the eye: comparison of baculovirus- and adenovirus-mediated intravitreal vascular endothelial growth factor D gene transfer in the rabbit eye
J. Gene Med.
11
382-389
2009
Homo sapiens
Manually annotated by BRENDA team
Ahmad, A.; Wang, Z.; Kong, D.; Ali, R.; Ali, S.; Banerjee, S.; Sarkar, F.H.
Platelet-derived growth factor-D contributes to aggressiveness of breast cancer cells by up-regulating Notch and NF-kappaB signaling pathways
Breast Cancer Res. Treat.
126
15-25
2011
Homo sapiens
Manually annotated by BRENDA team
Glasgow, C.G.; Avila, N.A.; Lin, J.P.; Stylianou, M.P.; Moss, J.
Serum vascular endothelial growth factor-D levels in patients with lymphangioleiomyomatosis reflect lymphatic involvement
Chest
135
1293-1300
2009
Homo sapiens
Manually annotated by BRENDA team
Ming, J.; Zhang, Q.; Qiu, X.; Wang, E.
Interleukin 7/interleukin 7 receptor induce c-Fos/c-Jun-dependent vascular endothelial growth factor-D up-regulation: a mechanism of lymphangiogenesis in lung cancer
Eur. J. Cancer
45
866-873
2009
Homo sapiens
Manually annotated by BRENDA team
Hu, J.; Ye, H.; Fu, A; Chen, X.; Wang, Y.; Chen, X.; Ye, X.; Xiao, W.; Duan, X.; Wei, Y.; Chen, L.
Deguelin-an inhibitor to tumor lymphangiogenesis and lymphatic metastasis by down-regulation of vascular endothelial cell growth factor-D in lung tumor model
Int. J. Cancer
127
2455-2466
2010
Homo sapiens
Manually annotated by BRENDA team
Deng, J.; Liang, H.; Sun, D.; Pan, Y.; Wang, B.; Guo, Y.
Vascular endothelial growth factor-D is correlated with hepatic metastasis from gastric cancer after radical gastrectomy
Surgery
146
896-905
2009
Homo sapiens
Manually annotated by BRENDA team
Forneris, F.; Ricklin, D.; Wu, J.; Tzekou, A.; Wallace, R.; Lambris, J.; Gros, P.
Structures of C3b in complex with factors B and D give insight into complement convertase formation
Science
330
1816-1820
2010
Homo sapiens
Manually annotated by BRENDA team
Forneris, F.; Burnley, B.T.; Gros, P.
Ensemble refinement shows conformational flexibility in crystal structures of human complement factor D
Acta Crystallogr. Sect. D
70
733-743
2014
Homo sapiens (P00746), Homo sapiens
Manually annotated by BRENDA team
Katschke, K.J.; Wu, P.; Ganesan, R.; Kelley, R.F.; Mathieu, M.A.; Hass, P.E.; Murray, J.; Kirchhofer, D.; Wiesmann, C.; van Lookeren Campagne, M.
Inhibiting alternative pathway complement activation by targeting the factor D exosite
J. Biol. Chem.
287
12886-12892
2012
Macaca fascicularis, Homo sapiens (P00746), Homo sapiens
Manually annotated by BRENDA team
Vulpetti, A.; Ostermann, N.; Randl, S.; Yoon, T.; Mac Sweeney, A.; Cumin, F.; Lorthiois, E.; Ruedisser, S.; Erbel, P.; Maibaum, J.
Discovery and design of first benzylamine-based ligands binding to an unlocked conformation of the complement factor D
ACS Med. Chem. Lett.
9
490-495
2018
Homo sapiens (P00746)
Manually annotated by BRENDA team
Ezure, T.; Sugahara, M.; Amano, S.
Senescent dermal fibroblasts negatively influence fibroblast extracellular matrix-related gene expression partly via secretion of complement factor D
Biofactors
45
556-562
2019
Homo sapiens (P00746)
Manually annotated by BRENDA team
Huang, W.; Kim, H.R.
Dynamic regulation of platelet-derived growth factor D (PDGF-D) activity and extracellular spatial distribution by matriptase-mediated proteolysis
J. Biol. Chem.
290
9162-9170
2015
Homo sapiens
Manually annotated by BRENDA team
Lorthiois, E.; Anderson, K.; Vulpetti, A.; Rogel, O.; Cumin, F.; Ostermann, N.; Steinbacher, S.; Mac Sweeney, A.; Delgado, O.; Liao, S.M.; Randl, S.; Ruedisser, S.; Dussauge, S.; Fettis, K.; Kieffer, L.; de Erkenez, A.; Yang, L.; Hartwieg, C.; Argikar, U.A.; La Bonte, L.R.; Newton, R.; Kansara, V.; Flohr, S.; Hommel, U.; Jaffee, B.; Maibaum, J.
Discovery of highly potent and selective small-molecule reversible factor D inhibitors demonstrating alternative complement pathway inhibition in vivo
J. Med. Chem.
60
5717-5735
2017
Homo sapiens (P00746), Homo sapiens
Manually annotated by BRENDA team
Karki, R.G.; Powers, J.; Mainolfi, N.; Anderson, K.; Belanger, D.B.; Liu, D.; Ji, N.; Jendza, K.; Gelin, C.F.; Mac Sweeney, A.; Solovay, C.; Delgado, O.; Crowley, M.; Liao, S.M.; Argikar, U.A.; Flohr, S.; La Bonte, L.R.; Lorthiois, E.L.; Vulpetti, A.; Brown, A.; Long, D.; Prentiss, M.; Gradoux, N.; de Erkenez, A.; Cumin, F.; Adams, C.; Jaffe, B.; Mogi, M.
Design, synthesis, and preclinical characterization of selective factor D inhibitors targeting the alternative complement pathway
J. Med. Chem.
62
4656-4668
2019
Homo sapiens (P00746), Homo sapiens
Manually annotated by BRENDA team