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Information on EC 3.4.21.21 - coagulation factor VIIa and Organism(s) Homo sapiens and UniProt Accession P08709

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     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.21 coagulation factor VIIa
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P08709 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-/-Ile bond in factor X to form factor Xa
Synonyms
factor vii, rfviia, fvii, fviia, factor viia, activated factor vii, recombinant factor viia, coagulation factor vii, fviic, novoseven, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
blood coagulation factor VIIa
-
serine protease factor VIIa
-
TF-FVIIa
factor VIIa in complex with tissue factor
activated blood coagulation factor VII
-
-
-
-
activated coagulation factor VII
-
-
activated factor VII
-
-
blood-coagulation factor VII, activated
-
-
-
-
blood-coagulation factor VIIa
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-
-
-
coagulation factor VII
-
-
coagulation factor VII(a)
-
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coagulation FVII
-
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Eptacog alfa
-
-
-
-
Factor VII
-
-
factor VIIa-sTF
-
-
factor VIIa-TF
-
-
FIIa
-
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free factor VIIa
-
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FVIIa-sTF
-
FVIIa in complex with soluble tissue factor
FVIIc
-
-
human factor VIIa + TF
-
-
NovoSeven
-
commercial preparation
procoagulant protein factor VII
-
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recombinant factor VIIa
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recombinant factor-activated VII
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rFVII
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Serum prothrombin conversion accelerator
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-
-
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soluble tissue factor/factor VIIa complex
-
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sTF/VIIa
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TF/VIIa
-
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tissue factor/factor VIIa
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-
tissue factor/factor VIIa complex
-
-
vitamin K dependent clotting factor
-
-
additional information
-
the enzyme is a member of the trypsin family of serine proteases
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Phosphorylation
-
phosphorylation of signal transducers and activators of transcription
CAS REGISTRY NUMBER
COMMENTARY hide
65312-43-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
show the reaction diagram
factor IX + H2O
factor IXa + ?
show the reaction diagram
-
-
-
?
factor X + H2O
factor Xa
show the reaction diagram
-
-
-
?
Factor X + H2O
Factor Xa + ?
show the reaction diagram
-
-
-
?
N-methylsulfonyl-D-Phe-Gly-Arg-4-nitroanilide + H2O
N-methylsulfonyl-D-Phe-Gly-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
?
N-methylsulfonyl-D-phenyl-D-glycyl-D-arginyl-4-nitroanilide + H2O
N-methylsulfonyl-D-phenyl-D-glycyl-D-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
?
4-methylumbelliferyl 4-guanidinobenzoate + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Ile-Glu-gamma-methoxyglutamyl-Gly-Arg-p-nitroanilide + H2O
benzoyl-Ile-Glu-gamma-methoxyglutamyl-Gly-Arg + p-nitroaniline
show the reaction diagram
-
i.e. S2222, 2% of the activity with N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide, plasma-derived wild-type enzyme
-
-
?
benzyloxycarbonyl-D-Arg-Gly-Arg + H2O
?
show the reaction diagram
-
i.e. S2765, 6% of the activity with N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide, plasma-derived wild-type enzyme
-
-
?
benzyloxycarbonyl-D-Arg-Gly-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
chromogenic S-2765
-
-
?
benzyloxycarbonyl-D-arginyl-D-glycyl-D-arginine-p-nitroanilide + H2O
p-nitroaniline + benzyloxycarbonyl-D-arginyl-D-glycyl-D-arginine
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-D-arginyl-glycyl-arginine-p-nitroanilide + H2O
benzyloxycarbonyl-D-arginyl-glycyl-arginine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-D-arginyl-glycyl-L-arginyl-p-nitroanilide + H2O
benzyloxycarbonyl-D-arginyl-glycyl-L-arginine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
chromozym t-PA + H2O
?
show the reaction diagram
-
-
-
-
?
Chromozym tissue plasminogen activator + H2O
?
show the reaction diagram
-
i.e. N-methylsulfonyl-D-Phe-Gly-Arg-4-nitranilide acetate
-
-
?
D-cyclohexylglycyl-L-2-aminobutyryl-L-arginyl-4-nitroanilide + H2O
D-cyclohexylglycyl-L-2-aminobutyryl-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
show the reaction diagram
D-Ile-Pro-Arg-p-nitroanilide + H2O
D-Ile-Pro-Arg + p-nitroaniline
show the reaction diagram
D-Ile-Pro-Arg-p-nitroanilide + H2O
p-nitroaniline + D-Ile-Pro-Arg
show the reaction diagram
-
-
-
-
?
D-isoleucyl-L-prolyl-L-arginine-p-nitroanilide + H2O
D-isoleucyl-L-prolyl-L-arginine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Phe-pipecolyl-Arg-p-nitroanilide + H2O
D-Phe-pipecolyl-Arg + p-nitroaniline
show the reaction diagram
D-phenylalanyl-L-pipecolyl-L-arginine-p-nitroanilide + H2O
D-phenylalanyl-L-pipecolyl-L-arginine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Pro-Phe-Arg-p-nitroanilide + H2O
D-Pro-Phe-Arg + p-nitroaniline
show the reaction diagram
-
i.e. S2302, 12% of the activity with N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide, plasma-derived wild-type enzyme
-
-
?
Eph tyrosine kinase receptor EphA2 + H2O
?
show the reaction diagram
-
cleavage site at the Arg159-His160 bond
-
-
?
Eph tyrosine kinase receptor EphB2 + H2O
?
show the reaction diagram
-
cleavage site at the Arg159-His160 bond
-
-
?
factor IX + H2O
?
show the reaction diagram
-
-
-
-
?
factor IX + H2O
activated factor IX + ?
show the reaction diagram
-
-
-
-
?
factor IX + H2O
factor IXa + ?
show the reaction diagram
factor VIII + H2O
factor VIIIa + ?
show the reaction diagram
-
FVIII activity increases about 4-fold within 30 s in the presence of FVIIa/tissue factor. The heavy chain of FVIII is proteolyzed at Arg336. Arg740 and Arg372
-
-
?
factor X + H2O
?
show the reaction diagram
-
-
-
-
?
factor X + H2O
activated factor X
show the reaction diagram
-
-
-
-
?
factor X + H2O
activated factor X + ?
show the reaction diagram
factor X + H2O
factor Xa
show the reaction diagram
-
-
-
-
?
Factor X + H2O
Factor Xa + ?
show the reaction diagram
H-D-isoleucyl-L-prolyl-arginine-p-nitroanilide + H2O
H-D-isoleucyl-L-prolyl-arginine + p-nitroaniline
show the reaction diagram
-
i.e. S-2288
-
-
?
Ile-Pro-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
methanesulfonyl-D-cyclohexylalanyl-butyl-arginine p-nitroanilide + H2O
methanesulfonyl-D-cyclohexylalanyl-butyl-arginine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-P3-P2-Lys-7-amido-4-carbamoylmethylcoumarin + H2O
?
show the reaction diagram
-
P2: Val or Thr, P3: Gln, Arg, Asn or Pro
-
-
?
N-methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide + H2O
N-methoxycarbonyl-D-Nle-Gly-Arg + p-nitroaniline
show the reaction diagram
-
i.e. chromozym X, 11% of the activity with N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide, plasma-derived wild-type enzyme
-
-
?
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide + H2O
N-methylsulfonyl-D-Phe-Gly-Arg + p-nitroaniline
show the reaction diagram
phosphoinositide + H2O
inositol phosphate + diacylglycerol
show the reaction diagram
-
-
-
-
?
protease-activated receptor 2 + H2O
?
show the reaction diagram
pyroGlu-Pro-Arg-p-nitroanilide + H2O
p-nitroaniline + pyroGlu-Pro-Arg
show the reaction diagram
-
-
-
-
?
pyroglutamyl-Gly-Arg-p-nitroanilide + H2O
pyroglutamyl-Gly-Arg + p-nitroaniline
show the reaction diagram
-
i.e. S2444, 2% of the activity with N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide, plasma-derived wild-type enzyme
-
-
?
pyroglutamyl-Phe-Lys-p-nitroanilide + H2O
pyroglutamyl-D-Phe-Gly-Arg + p-nitroaniline
show the reaction diagram
-
i.e. S2403, 1.4% of the activity with N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide, plasma-derived wild-type enzyme
-
-
?
pyroglutamyl-Pro-Arg-p-nitroanilide + H2O
pyroglutamyl-Pro-Arg + p-nitroaniline
show the reaction diagram
-
i.e. S2366, 38% of the activity with N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide, plasma-derived wild-type enzyme
-
-
?
S-2288 + H2O
?
show the reaction diagram
-
-
-
-
?
S2288 + H2O
D-Ile-Pro-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
signal transducer and activator of transcription 5 + ?
activated signal transducer and activator of transcription 5 + ?
show the reaction diagram
-
STAT5
-
-
?
spectrozyme fVIIa + H2O
?
show the reaction diagram
-
-
-
-
?
spectrozyme Fxa + H2O
?
show the reaction diagram
-
chromogenic substrate
-
-
?
thrombinogen + H2O
thrombin + ?
show the reaction diagram
tissue factor + H2O
?
show the reaction diagram
-
-
-
-
?
Trp-Ala-Thr-Arg-7-amido-4-carbamoylmethylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Z-D-arginyl-glycyl-arginine-p-nitroanilide + H2O
Z-D-arginyl-glycyl-arginine + p-nitroaniline
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
factor IX + H2O
factor IXa + ?
show the reaction diagram
-
-
-
?
Factor X + H2O
Factor Xa + ?
show the reaction diagram
-
-
-
?
Eph tyrosine kinase receptor EphA2 + H2O
?
show the reaction diagram
-
cleavage site at the Arg159-His160 bond
-
-
?
Eph tyrosine kinase receptor EphB2 + H2O
?
show the reaction diagram
-
cleavage site at the Arg159-His160 bond
-
-
?
factor IX + H2O
?
show the reaction diagram
-
-
-
-
?
factor IX + H2O
factor IXa + ?
show the reaction diagram
factor VIII + H2O
factor VIIIa + ?
show the reaction diagram
-
FVIII activity increases about 4-fold within 30 s in the presence of FVIIa/tissue factor. The heavy chain of FVIII is proteolyzed at Arg336. Arg740 and Arg372
-
-
?
factor X + H2O
activated factor X + ?
show the reaction diagram
-
the enzyme initiates blood clotting after interacting with its cofactor tissue factor. The product of the reaction, activated factor X, is also the most efficient activator of zymogen factor VII
-
-
?
factor X + H2O
factor Xa
show the reaction diagram
-
-
-
-
?
Factor X + H2O
Factor Xa + ?
show the reaction diagram
protease-activated receptor 2 + H2O
?
show the reaction diagram
spectrozyme fVIIa + H2O
?
show the reaction diagram
-
-
-
-
?
thrombinogen + H2O
thrombin + ?
show the reaction diagram
tissue factor + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
vitamin K
additional information
complex formation with the essential protein cofactor tissue factor
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
Mg2+ potentiates the activation of factor X and factor IX by factor VIIa
additional information
-
Mg2+ alone does not significantly influence the rate of factor X activation by the enzyme. The presence of tissue factor is required for Mg2+ to enhance the rate of factor X activation by the enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-(3-[(R)-2-[(S)-1-(4-carbamimidoyl-benzylcarbamoyl)-3-carbamoylpropylcarbamoyl]-2-ethanesulfonylamino-ethyl]-1H-indol-5-yloxymethyl)-benzoic acid
-
4-aminobenzamidine
-
5-(4-carboxybutoxy)-N-(ethylsulfonyl)-D-tryptophyl-N1-(4-carbamimidoylbenzyl)-D-glutamamide
-
5-[(3-carboxybenzyl)oxy]-N-(ethylsulfonyl)-D-tryptophyl-N1-(4-carbamimidoylbenzyl)-D-glutamamide
-
acetyl-ALCDDPRVDRWYCQFVEG-NH2
i.e. E-76
benzamidine
-
D-Phe-Phe-Arg chloromethylketone
-
D-Phe-Phe-Arg methyl ketone
-
D-prolyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
-
H-D-Phe-Phe-Arg-chloromethylketone
-
N-(ethylsulfonyl)-1-methyl-D-tryptophyl-N1-(4-carbamimidoylbenzyl)-D-glutamamide
-
N-(ethylsulfonyl)-5-hydroxy-D-tryptophyl-N1-(4-carbamimidoylbenzyl)-D-glutamamide
-
N-(ethylsulfonyl)-5-methoxy-D-tryptophyl-N1-(4-carbamimidoylbenzyl)-D-glutamamide
-
N-(ethylsulfonyl)-D-tryptophyl-N1-(4-carbamimidoylbenzyl)-L-glutamamide
-
R-4-[2-(3-aminobenzenesulfonylamino)-1-(3,5-diethoxy-2-fluorophenyl)-2-oxoethylamino]-2-hydroxy-benzamidine
incubation with enzyme in 100 mM Hepes, pH 7.8, 140 mM NaCl, 0.1% (v/v) polyethylene glycol 8000, 0.02% (v/v) Tween 80, 5 mM CaCl2 for 40 min at room temperature
(2R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(18),6(21),7,9,16,19-hexaene-3,12-dione
-
-
(2R)-2-[(1-aminoisoquinolin-6-yl)amino]-7-(propane-2-sulfonyl)-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(18),6(21),7,9,16,19-hexaene-3,12-dione
-
-
(2R,15R)-2-[(1-amino-4-fluoroisoquinolin-6-yl)amino]-7-(cyclopropanesulfonyl)-4,15,17-trimethyl-13-oxa-4,11-diazatricyclo-[14.2.2.16,10]henicosa-1(18),6,8,10(21),16,19-hexaene-3,12-dione
-
highly potent, selective inhibitor
(2R,15R)-2-[(1-amino-7-fluoroisoquinolin-6-yl)amino]-7-(cyclopropanesulfonyl)-4,15,17-trimethyl-13-oxa-4,11-diazatricyclo-[14.2.2.16,10]henicosa-1(18),6,8,10(21),16,19-hexaene-3,12-dione
-
-
(2R,15R)-2-[(1-amino-8-fluoroisoquinolin-6-yl)amino]-7-(cyclopropanesulfonyl)-4,15,17- trimethyl-13-oxa-4,11-diazatricyclo-[14.2.2.16,10]henicosa-1(18),6,8,10(21),16,19-hexaene-3,12-dione
-
-
(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,15,17-trimethyl-13-oxa-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(18),6,8,10-(21),16,19-hexaene-3,12-dione
-
-
(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,15,17-trimethyl-3,12-dioxo-13-oxa-4,11- diazatricyclo[14.2.2.16,10]henicosa-1-(18),6,8,10(21),16,19-hexaene-7-carboxamide
-
-
(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,15,17-trimethyl-7-(trifluoromethoxy)-13-oxa-4,11-diazatricyclo[14.2.2.16,10]-henicosa-1(18),6,8,10(21),16,19-hexaene-3,12-dione
-
-
(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,15,20-trimethyl-7-(1-methyl-1H-pyrazol-5-yl)-13-oxa-4,11-diazatricyclo-[14.2.2.16,10]henicosa-1(18),6,8,10(21),16,19-hexaene-3,12-dione
-
-
(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-7-(cyclopropanesulfonyl)-4,15,20-trimethyl-13-oxa-4,11-diazatricyclo[14.2.2.16,10]-henicosa-1(18),6,8,10(21),16,19-hexaene-3,12-dione
-
-
(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-N,N,4,15,17-pentamethyl-3,12-dioxo-13-oxa-4,11-diazatricyclo[14.2.2.16,10]-henicosa-1(18),6,8,10(21),16,19-hexaene-7-carboxamide
-
-
(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-N,N-diethyl-4,15,17-trimethyl-3,12-dioxo-13-oxa-4,11-diazatricyclo[14.2.2.16,10]-henicosa-1(18),6,8,10(21),16,19-hexaene-7-carboxamide
-
-
(2S)-2-[(1-aminoisoquinolin-6-yl)amino]-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(18),6(21),7,9,16,19-hexaene-3,12-dione
-
-
(R)-2-(1-aminoisoquinolin-6-ylamino)-7-ethanesulfonyl-20-methyl-4,11-diaza-tricyclo[14.2.2.16,10]henicosa-1(19),6,8,10-(21),16(20),17-hexaene-3,12-dione
-
-
(R)-2-(1-aminoisoquinolin-6-ylamino)-7-ethanesulfonyl-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(19),6,8,10(21),16-(20),17-hexaene-3,12-dione
-
-
2-(1-aminoisoquinolin-6-ylamino)-16-oxa-4,11-diazatricyclo-[15.2.2.16,10]docosa-1(20),6,8,10(22),17(21),18-hexaene-3,12-dione trifluoroacetic acid
-
-
2-(3'-amino-3-fluoro-4-(isopropylamino)-1,1'-biphenyl-2-yl)-N-(4-(amino(imino)methyl)benzyl)acetamide
-
IC50: 340 nM
2-(3'-amino-4-(benzylamino)-3-fluoro-1,1'-biphenyl-2-yl)-N-(4-(amino(imino)methyl)benzyl)acetamide
-
IC50: 500 nM
2-(3-allylamino-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl)-N-(4-carbamimidoyl-benzyl)-acetamide
-
pH 8.0, IC50: 700 nM
2-(3-benzylamino-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl)-N-(4-carbamimidoyl-benzyl)-acetamide
-
pH 8.0, IC50: 770 nM
2-(3-benzylsulfanyl-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl)-N-(4-carbamimidoyl-benzyl)-acetamide
-
pH 8.0, IC50: 0.0064 mM
2-(3-butylamino-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl)-N-(4-carbamimidoyl-benzyl)-acetamide
-
pH 8.0, IC50: 0.0032 mM
2-[(1-aminoisoquinolin-6-yl)amino]-4,11-diazatricyclo[13.2.2.16,10]icosa-1(17),6(20),7,9,15,18-hexaene-3,12-dione
-
-
2-[(1-aminoisoquinolin-6-yl)amino]-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(18),6(21),7,9,16,19-hexaene-3,12-dione
-
-
2-[(1-aminoisoquinolin-6-yl)amino]-4,11-diazatricyclo[15.2.2.16,10]docosa-1(19),6(22),7,9,17,20-hexaene-3,12-dione
-
-
2-[3-(2-amino-ethylamino)-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
-
pH 8.0, IC50: 0.0021 mM
2-[3-(3-amino-propylamino)-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
-
pH 8.0, IC50: 890 nM
2-[3-(4-amino-butylamino)-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
-
pH 8.0, IC50: 980 nM
2-[3-(4-tert-butyl-cyclohexylamino)-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
-
pH 8.0, IC50: 0.003 mM
2-[3-(adamantan-1-ylamino)-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
-
pH 8.0, IC50: 0.013 mM
2-[6-(3-acetylamino-phenyl)-5-chloro-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
-
pH 8.0, IC50: 0.00161 mM
2-[6-(3-amino-phenyl)-5-chloro-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
-
pH 8.0, IC50: 70 nM
2-[6-(3-amino-phenyl)-5-chloro-3-cyclobutylamino-2-oxo-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
-
pH 8.0, IC50: 20 nM
2-[6-(3-amino-phenyl)-5-chloro-3-isopropylamino-2-oxo-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
-
pH 8.0, IC50: 20 nM
2-[6-(3-bromo-phenyl)-5-chloro-3-cyclobutylamino-2-oxo-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
-
pH 8.0, IC50: 0.0042 mM
3-amino-5-(1-(1-((4-(amino(imino)methyl)benzyl)-amino)-2-oxoethyl)-5-(isopropylamino)-6-oxo-1,6-dihydropyridin-2-yl)benzoic acid
-
IC50: 118 nM
3-amino-5-[1-[2-([4-[amino(imino)methyl]benzyl]amino)-2-oxoethyl]-3-chloro-5-(isopropylamino)-6-oxo-1,6-dihydropyrazin-2-yl]benzoic acid
-
pH 8.0, IC50: 16 nM, potent and highly selective inhibitor, selectivity versus factor Xa and thrombin
3-methyl-2-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-pentanoic acid [4-guanidino-1-(thiazole-2-carbonyl)-butyl]-amide
-
IC50: 300 nM, reversible, covalent
3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 0.00145 mM, reversible, covalent
3-[1-[(4-carbamimidoyl-benzylcarbamoyl)-methyl]-3-chloro-5-isopropylamino-6-oxo-1,6-dihydro-pyrazin-2-yl]-benzoic acid
-
pH 8.0, IC50: 360 nM
3-[1-[(4-carbamimidoyl-benzylcarbamoyl)-methyl]-3-chloro-5-isopropylamino-6-oxo-1,6-dihydro-pyrazin-2-yl]-benzoic acid methyl ester
-
pH 8.0, IC50: 780 nM
4,4-dimethyl-2-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-pentanoic acid [4-guanidino-1-(thiazole-2-carbonyl)-butyl]-amide
-
IC50: 700 nM, reversible, covalent
4-((R)-7-ethanesulfonyl-3,12-dioxo-4,11-diaza-tricyclo-[14.2.2.16,10]henicosa-1(19),6,8,10(21),16(20),17-hexaen-2-ylamino)benzamidine trifluoroacetic acid
-
-
4-aminobenzamidine
-
-
4-[5-(4-fluorophenyl)-2-[4-(methylsulfonyl)phenyl]-1H-imidazol-4-yl]pyridine
-
-
6-dimethylamino-2-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-hexanoic acid [4-guanidino-1-(thiazole-2-carbonyl)-butyl]-amide
-
IC50: 0.00282 mM, reversible, covalent
active-site-inhibited factor Xa
-
80 nM: 60% inhibition
-
alpha1-proteinase inhibitor variant M358R
-
-
-
anti-gC antibody
-
20% inhibition
-
anti-TF antibody
-
40% inhibition
-
antithrombin
-
antithrombin III
-
Bovine pancreatic trypsin inhibitor
-
mutant enzyme K192E is poorly inhibited, mutant enzyme K192Q is inhibited more than the wild-type enzyme
-
combination of the gC- and TF-specific antibodies
-
65% inhibition
-
D-Phe-Phe-Arg chloromethyl ketone
-
-
D-Phe-Phe-Arg-chloromethyl ketone
-
-
diethyl [(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,15,17-trimethyl-3,12-dioxo-13-oxa-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(18),6,8,10(21),16,19-hexaen-7-yl]phosphonate
-
-
diisopropylfluorophosphate
-
15 mM, 60 min, 50% inactivation
dimeric active site-inhibited blood clotting factor VIIa
-
dimeric fVIIai, 16000fold inhibitory effect
-
EEWEVLCWTWETCER
EEWEVLCWTWETCERGEG-(Z-domain of protein A)
-
IC50: 3.8 nM
-
EEWEVLCWTWETCERGEG-NH2
-
IC50: 1.5 nM
EEWEVLCWTWETCERGEGVEEELWEWR
-
maximal inhibition to 99%, IC50: 230 pM
EVLCWTWETCER-NH2
-
IC50: 470 nM
EWEVLCWTWETCERGE-(Z-domain of protein A)
-
IC50: 4.8 nM
-
FFR-FVIIa
-
derivate of FVIIa with a stably buried N-terminus representing the active conformation of FVIIa, IC50: 0.019 mM
-
hemextin A
-
0.05 mM, 70% inhibition
-
hemextin AB complex
-
IC50: 100 nM
-
MEEWEVLCWTWETCERGEGQ-(Z-domain of protein A)
-
IC50: 5.9 nM
-
methyl (2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,15,17-trimethyl-3,12-dioxo-13-oxa-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(18),6,8,10(21),16,19-hexaene-7-carboxylate
-
-
N-(3-[1-[(4-carbamimidoyl-benzylcarbamoyl)-methyl]-3-chloro-6-oxo-5-phenethylamino-1,6-dihydro-pyrazin-2-yl]-phenyl)-2,2,2-trifluoro-acetamide
-
pH 8.0, IC50: 450 nM
N-(4-(amino(imino)methyl)benzyl)-2-(2,6-difluoro-3-((2-phenylethyl)amino)phenyl)acetamide
-
IC50: 0.0164 mM
N-(4-(amino(imino)methyl)benzyl)-2-(3-fluoro-4-((2-phenylethyl)amino)-1,1'-biphenyl-2-yl)acetamide
-
IC50: 0.00398 mM
N-(4-(amino(imino)methyl)benzyl)-2-(3-hydroxy-4-((2-phenylethyl)amino)-1,1'-biphenyl-2-yl)acetamide
-
IC50: 0.0027 mM
N-(4-(amino(imino)methyl)benzyl)-2-(3-hydroxy-4-(isopropylamino)-1,1'-biphenyl-2-yl)acetamide
-
IC50: 0.0025 mM
N-(4-(amino(imino)methyl)benzyl)-2-(3-methoxy-4-((2-phenylethyl)amino)-1,1'-biphenyl-2-yl)acetamide
-
IC50: 0.025 mM
N-(4-(amino(imino)methyl)benzyl)-2-(4-(isopropylamino)-3-methoxy-1,1'-biphenyl-2-yl)acetamide
-
IC50: 0.0147 mM
N-(4-(amino(imino)methyl)benzyl)-2-(5-(isopropylamino)-3,6-dioxo-2-phenylcyclohexa-1,4-dien-1-yl)acetamide
-
IC50: 0.0028 mM
N-(4-(amino(imino)methyl)benzyl)-2-(6-(3,5-diaminophenyl)-3-(isopropylamino)-2-oxopyridin-1(2H)-yl)acetamide
-
IC50: 52 nM
N-(4-carbamimidoyl-benzyl)-2-(2-oxo-3-phenethylamino-6-phenyl-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 340 nM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-3-phenethylamino-6-m-tolyl-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 0.001 mM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-3-phenethylamino-6-o-tolyl-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 430 nM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-3-phenethylamino-6-p-tolyl-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 0.00414 mM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-3-phenethylamino-6-phenyl-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 630 nM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-6-phenyl-3-phenylamino-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 0.0112 mM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-6-phenyl-3-prop-2-ynylamino-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 720 nM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-6-phenyl-3-propylamino-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 400 nM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-6-phenyl-3-pyrrolidin-1-yl-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 0.0063 mM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-3-cyclobutylamino-2-oxo-6-phenyl-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 400 nM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-3-cyclohexylamino-2-oxo-6-phenyl-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 0.0014 mM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-3-ethylamino-2-oxo-6-phenyl-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 400 nM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-3-isopropylamino-2-oxo-6-phenyl-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 200 nM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-3-methylamino-2-oxo-6-phenyl-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 700 nM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-6-ethyl-2-oxo-3-phenethylamino-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 0.00345 mM
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-6-methyl-2-oxo-3-phenethylamino-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 0.00428 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-2-oxo-3-phenethylamino-6-(2-trifluoromethyl-phenyl)-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0027 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-2-oxo-3-phenethylamino-6-(3-trifluoromethyl-phenyl)-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0029 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-2-oxo-6-phenyl-3-(1-propyl-butylamino)-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0018 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-2-oxo-6-phenyl-3-(3-phenyl-propylamino)-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0126 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-2-oxo-6-phenyl-3-(3-trifluoromethyl-benzylamino)-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0063 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-2-oxo-6-phenyl-3-(4-phenyl-butylamino)-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0041 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(1,1-dioxo-tetrahydro-16-thiophen-3-ylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.001 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(1-ethyl-hexylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0098 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(1-ethyl-propylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 430 nM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(1-methyl-butylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 840 nM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(1-methyl-pentylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 900 nM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(2,5-difluoro-benzylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0038 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(2-dimethylamino-ethylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0209 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(2-hydroxy-ethylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 500 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(2-methoxy-ethylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 880 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(2-morpholin-4-yl-ethylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.008 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(3,5-difluoro-benzylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.006 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(3-dimethylamino-propylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0176 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(3-hydroxy-propylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 500 nM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(4-chloro-benzylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0043 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(4-hydroxy-butylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 600 nM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(6-hydroxy-hexylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 470 nM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(isopropyl-methyl-amino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0091 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-cyclobutylamino-6-(2-hydroxy-phenyl)-2-oxo-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 340 nM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-cyclobutylamino-6-(3-hydroxy-phenyl)-2-oxo-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 200 nM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(2-chloro-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.003 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(2-fluoro-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0018 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(2-methoxy-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0016 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(3-chloro-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.00198 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(3-dimethylamino-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0012 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(3-fluoro-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0023 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(3-methanesulfonylamino-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 600 nM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(3-methoxy-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0052 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(3-methylamino-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 600 nM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(3-nitro-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.00252 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(4-chloro-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.00888 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(4-fluoro-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.0081 mM
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(4-methoxy-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
-
pH 8.0, IC50: 0.02345 mM
N-(4-carbamimidoyl-benzyl)-2-{5-chloro-2-oxo-6-phenyl-3-[2-(3-trifluoromethyl-phenyl)-ethylamino]-2H-pyrazin-1-yl}-acetamide
-
pH 8.0, IC50: 0.03 mM
N-(4-carbamimidoyl-benzyl)-2-{5-chloro-3-[2-(3-chloro-phenyl)-ethylamino]-2-oxo-6-phenyl-2H-pyrazin-1-yl}-acetamide
-
pH 8.0, IC50: 180 nM
N-(4-carbamimidoyl-benzyl)-2-{5-chloro-3-[2-(4-chloro-phenyl)-ethylamino]-2-oxo-6-phenyl-2H-pyrazin-1-yl}-acetamide
-
pH 8.0, IC50: 600 nM
N-(5-carbamimidoyl-pyridin-2-ylmethyl)-2-(2-oxo-3-phenethylamino-6-phenyl-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 0.0167 mM
N-(6-carbamimidoyl-pyridin-3-ylmethyl)-2-(2-oxo-3-phenethylamino-6-phenyl-2H-pyrazin-1-yl)-acetamide
-
pH 8.0, IC50: 0.0014 mM
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-(3,4,5-trifluoro-phenyl)-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 200 nM, reversible, covalent
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-(3-trifluoromethyl-phenyl)-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 800 nM, reversible, covalent
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-(4-iodo-phenyl)-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 0.00156 mM, reversible, covalent
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-(4-nitro-phenyl)-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 0.00588 mM, reversible, covalent
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-hydroxy-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 110 nM, reversible, covalent
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-m-tolyl-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 170 nM, reversible, covalent
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-naphthalen-1-yl-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 0.0056 mM, reversible, covalent
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-naphthalen-2-yl-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 0.00195 mM, reversible, covalent
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-o-tolyl-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 240 nM, reversible, covalent
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-p-tolyl-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 0.00129 mM, reversible, covalent
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-phenyl-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 42 nM, reversible, covalent
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-pyridin-3-yl-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 200 nM, reversible, covalent
N-[2-(1-benzyl-1H-imidazol-4-yl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 0.00997 mM, reversible, covalent
N-[2-(2,6-dimethyl-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 700 nM, reversible, covalent
N-[2-(2-fluoro-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 90 nM, reversible, covalent
N-[2-(3,4-difluoro-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 160 nM, reversible, covalent
N-[2-(3,5-difluoro-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 190 nM, reversible, covalent
N-[2-(3-chloro-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 230 nM, reversible, covalent
N-[2-(3-fluoro-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 200 nM, reversible, covalent
N-[2-(4-acetylamino-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 570 nM, reversible, covalent
N-[2-(4-bromo-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 760 nM, reversible, covalent
N-[2-(4-chloro-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 680 mM, reversible, covalent
N-[2-(4-cyano-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 340 nM, reversible, covalent
N-[2-(4-fluoro-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 170 nM, reversible, covalent
N-[2-benzo[b]thiophen-3-yl-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 0.0005 mM, reversible, covalent
N-[2-benzyloxy-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 0.00153 mM, reversible, covalent
N-[2-biphenyl-3-yl-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 0.00183 mM, reversible, covalent
N-[2-biphenyl-4-yl-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 0.0178 mM, reversible, covalent
N-[2-cyclohexyl-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 0.0033 mM, reversible, covalent
N-[2-cyclopropyl-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
-
IC50: 820 nM, reversible, covalent
N-[3-[(2R)-1-[(2R)-2-[(1-aminoisoquinolin-6-yl)amino]-2-phenylacetyl]pyrrolidin-2-yl]-4-(propane-2-sulfonyl)phenyl]acetamide
-
-
N-[4-guanidino-1-(thiazole-2-carbonyl)-butyl]-3-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-succinamic acid cyclohexyl ester
-
IC50: 0.00318 mM, reversible, covalent
N-[4-guanidino-1-(thiazole-2-carbonyl)-butyl]-4-methanesulfonyl-2-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-butyramide
-
IC50: 0.0137 mM, reversible, covalent
N-[4-guanidino-1-(thiazole-2-carbonyl)-butyl]-4-phenyl-2-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-butyramide
-
IC50: 900 nM, reversible, covalent
N1-[4-guanidino-1-(thiazole-2-carbonyl)-butyl]-2-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-succinamide
-
IC50: 0.00103 mM, reversible, covalent
p-aminobenzamidine
-
-
SAEWEVLCWTWEGCGSVGL-(Z-domain of protein A)
-
IC50: 4400 nM
SEEWEVLCWTWEDCRLEGLE-(Z-domain of protein A)
-
IC50: 93 nM
-
tissue factor pathway inhibitor
-
Trp-Tyr-Thr-Arg-chloromethyl ketone
-
-
V154G-FVIIa
-
derivate of FVIIa with a fully exposed N-terminus representing the zymogen-like conformation of FVIIa, IC50: 0.014 mM
-
VLCWTWETCER-NH2
-
IC50: 0.022 nM
WEVLCWTWETC-NH2
-
IC50: 0.013 mM
WEVLCWTWETCE-NH2
-
IC50: 0.007 mM
WEVLCWTWETCER-NH2
-
IC50: 2.5 nM
Zn2+
-
two Zn2+ bind with high affinity to factor VIIa outside the N-terminal gamma-carboxyglutamic acid domain. Binding of Zn2+ is influenced by presence of Ca2+ and results in decreased amidolytic activity and slightly reduced affinity for tissue factor. After binding to tissue factor, factor VIIa is less susceptible to zinc inhibition
[(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,15,20-trimethyl-3,12-dioxo-13-oxa-4,11-diazatricyclo[14.2.2.16,10]henicosa-1-(18),6,8,10(21),16,19-hexaen-7-yl](ethoxy)phosphinic acid
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tissue factor
-
-
factor Xa
-
Herpes simplex virus 1 encoded glycoprotein C
-
gC, 1000fold activity-enhancing effect in the absence of tissue factor and in the presence of 5 mM Ca2+ and 0.1 mM synthetic small unilamellar vesicles composed of 75% phosphatidylcholine and 25% phosphatidylserine
-
Janus kinase 2
-
-
-
phospholipid vesicle
-
oleoyl-1,2-diacyl-sn-glycero-3-phosphocholine and dioleoyl-1,2-diacyl-sn-glycero-3-(phospho-L-serine)
-
protease-activated receptor-2
-
1.5fold activity enhancement
-
tissue factor
-
tissue factor TF
-
TF-induced allosteric activation of FVIIa, binding structure, overview
-
vitamin K
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2 - 14
D-Ile-Pro-Arg-4-nitroanilide
0.000012 - 0.0054
Factor X
-
0.85 - 10.4
D-Ile-Pro-Arg-p-nitroanilide
0.0000184 - 68
Factor X
-
1.5 - 9.8
H-D-isoleucyl-L-prolyl-arginine-p-nitroanilide
0.67
methanesulfonyl-D-cyclohexylalanyl-butyl-arginine p-nitroanilide
-
wild-type enzyme
0.8 - 50
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
11.8
S-2288
-
in 50 mM HEPES, pH 7.4, with 0.1 M NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, and 0.01% Tween 80, at 37°C
0.67
spectrozyme fVIIa
-
wild-type enzyme
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.7 - 34.6
D-Ile-Pro-Arg-4-nitroanilide
0.000007 - 0.004
Factor X
-
0.59 - 44.2
D-Ile-Pro-Arg-p-nitroanilide
0.00001 - 6800
Factor X
-
17
methanesulfonyl-D-cyclohexylalanyl-butyl-arginine p-nitroanilide
-
wild-type enzyme
8.4 - 396000
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
13
S-2288
-
in 50 mM HEPES, pH 7.4, with 0.1 M NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, and 0.01% Tween 80, at 37°C
16 - 17
spectrozyme fVIIa
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9 - 28
D-Ile-Pro-Arg-4-nitroanilide
0.0012 - 270
Factor X
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0493 - 1.485
4-aminobenzamidine
0.00000035
R-4-[2-(3-aminobenzenesulfonylamino)-1-(3,5-diethoxy-2-fluorophenyl)-2-oxoethylamino]-2-hydroxy-benzamidine
-
0.0004
(2R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(18),6(21),7,9,16,19-hexaene-3,12-dione
-
pH and temperature not specified in the publication
0.0000052 - 0.00003
(2R)-2-[(1-aminoisoquinolin-6-yl)amino]-7-(propane-2-sulfonyl)-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(18),6(21),7,9,16,19-hexaene-3,12-dione
0.00000043
(2R,15R)-2-[(1-amino-4-fluoroisoquinolin-6-yl)amino]-7-(cyclopropanesulfonyl)-4,15,17-trimethyl-13-oxa-4,11-diazatricyclo-[14.2.2.16,10]henicosa-1(18),6,8,10(21),16,19-hexaene-3,12-dione
-
at pH 7.4 and 37°C
0.00000023
(2R,15R)-2-[(1-amino-7-fluoroisoquinolin-6-yl)amino]-7-(cyclopropanesulfonyl)-4,15,17-trimethyl-13-oxa-4,11-diazatricyclo-[14.2.2.16,10]henicosa-1(18),6,8,10(21),16,19-hexaene-3,12-dione
-
at pH 7.4 and 37°C
0.000001
(2R,15R)-2-[(1-amino-8-fluoroisoquinolin-6-yl)amino]-7-(cyclopropanesulfonyl)-4,15,17- trimethyl-13-oxa-4,11-diazatricyclo-[14.2.2.16,10]henicosa-1(18),6,8,10(21),16,19-hexaene-3,12-dione
-
at pH 7.4 and 37°C
0.00002
(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,15,17-trimethyl-13-oxa-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(18),6,8,10-(21),16,19-hexaene-3,12-dione
-
at pH 7.4 and 37°C
0.000015
(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,15,17-trimethyl-3,12-dioxo-13-oxa-4,11- diazatricyclo[14.2.2.16,10]henicosa-1-(18),6,8,10(21),16,19-hexaene-7-carboxamide
-
at pH 7.4 and 37°C
0.0000055
(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,15,17-trimethyl-7-(trifluoromethoxy)-13-oxa-4,11-diazatricyclo[14.2.2.16,10]-henicosa-1(18),6,8,10(21),16,19-hexaene-3,12-dione
-
at pH 7.4 and 37°C
0.0000022
(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,15,20-trimethyl-7-(1-methyl-1H-pyrazol-5-yl)-13-oxa-4,11-diazatricyclo-[14.2.2.16,10]henicosa-1(18),6,8,10(21),16,19-hexaene-3,12-dione
-
at pH 7.4 and 37°C
0.00000016
(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-7-(cyclopropanesulfonyl)-4,15,20-trimethyl-13-oxa-4,11-diazatricyclo[14.2.2.16,10]-henicosa-1(18),6,8,10(21),16,19-hexaene-3,12-dione
-
at pH 7.4 and 37°C
0.0000025
(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-N,N,4,15,17-pentamethyl-3,12-dioxo-13-oxa-4,11-diazatricyclo[14.2.2.16,10]-henicosa-1(18),6,8,10(21),16,19-hexaene-7-carboxamide
-
at pH 7.4 and 37°C
0.00000057
(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-N,N-diethyl-4,15,17-trimethyl-3,12-dioxo-13-oxa-4,11-diazatricyclo[14.2.2.16,10]-henicosa-1(18),6,8,10(21),16,19-hexaene-7-carboxamide
-
at pH 7.4 and 37°C
0.018 - 0.054
(2S)-2-[(1-aminoisoquinolin-6-yl)amino]-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(18),6(21),7,9,16,19-hexaene-3,12-dione
0.0000016
(R)-2-(1-aminoisoquinolin-6-ylamino)-7-ethanesulfonyl-20-methyl-4,11-diaza-tricyclo[14.2.2.16,10]henicosa-1(19),6,8,10-(21),16(20),17-hexaene-3,12-dione
-
pH and temperature not specified in the publication
0.000008
(R)-2-(1-aminoisoquinolin-6-ylamino)-7-ethanesulfonyl-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(19),6,8,10(21),16-(20),17-hexaene-3,12-dione
-
pH and temperature not specified in the publication
0.0046
2-(1-aminoisoquinolin-6-ylamino)-16-oxa-4,11-diazatricyclo-[15.2.2.16,10]docosa-1(20),6,8,10(22),17(21),18-hexaene-3,12-dione trifluoroacetic acid
-
pH and temperature not specified in the publication
0.0046 - 0.01
2-[(1-aminoisoquinolin-6-yl)amino]-4,11-diazatricyclo[13.2.2.16,10]icosa-1(17),6(20),7,9,15,18-hexaene-3,12-dione
0.00092
2-[(1-aminoisoquinolin-6-yl)amino]-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(18),6(21),7,9,16,19-hexaene-3,12-dione
-
pH and temperature not specified in the publication
0.0061
2-[(1-aminoisoquinolin-6-yl)amino]-4,11-diazatricyclo[15.2.2.16,10]docosa-1(19),6(22),7,9,17,20-hexaene-3,12-dione
-
pH and temperature not specified in the publication
0.0000007
4-((R)-7-ethanesulfonyl-3,12-dioxo-4,11-diaza-tricyclo-[14.2.2.16,10]henicosa-1(19),6,8,10(21),16(20),17-hexaen-2-ylamino)benzamidine trifluoroacetic acid
-
pH and temperature not specified in the publication
3.2
4-aminobenzamidine
-
in 50 mM HEPES, pH 7.4, with 0.1 M NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, and 0.01% Tween 80, at 25°C
0.00000061
diethyl [(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,15,17-trimethyl-3,12-dioxo-13-oxa-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(18),6,8,10(21),16,19-hexaen-7-yl]phosphonate
-
at pH 7.4 and 37°C
0.0000002
EEWEVLCWTWETCER
-
inhibition of amidolytic activity
0.0000087
methyl (2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,15,17-trimethyl-3,12-dioxo-13-oxa-4,11-diazatricyclo[14.2.2.16,10]henicosa-1(18),6,8,10(21),16,19-hexaene-7-carboxylate
-
at pH 7.4 and 37°C
0.038 - 1.41
p-aminobenzamidine
0.00000028
[(2R,15R)-2-[(1-aminoisoquinolin-6-yl)amino]-4,15,20-trimethyl-3,12-dioxo-13-oxa-4,11-diazatricyclo[14.2.2.16,10]henicosa-1-(18),6,8,10(21),16,19-hexaen-7-yl](ethoxy)phosphinic acid
-
at pH 7.4 and 37°C
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000039
3-(3-[(R)-2-[(S)-1-(4-carbamimidoyl-benzylcarbamoyl)-3-carbamoylpropylcarbamoyl]-2-ethanesulfonylamino-ethyl]-1H-indol-5-yloxymethyl)-benzoic acid
Homo sapiens
in 500 mM Tris-HCl, pH 7.5, 1.5 M NaCl, 50 mM CaCl2, temperature not specified in the publication
0.000204
5-(4-carboxybutoxy)-N-(ethylsulfonyl)-D-tryptophyl-N1-(4-carbamimidoylbenzyl)-D-glutamamide
Homo sapiens
in 500 mM Tris-HCl, pH 7.5, 1.5 M NaCl, 50 mM CaCl2, temperature not specified in the publication
0.000056
5-[(3-carboxybenzyl)oxy]-N-(ethylsulfonyl)-D-tryptophyl-N1-(4-carbamimidoylbenzyl)-D-glutamamide
Homo sapiens
in 500 mM Tris-HCl, pH 7.5, 1.5 M NaCl, 50 mM CaCl2, temperature not specified in the publication
0.0024
D-prolyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
Homo sapiens
in 500 mM Tris-HCl, pH 7.5, 1.5 M NaCl, 50 mM CaCl2, temperature not specified in the publication
0.000069
N-(ethylsulfonyl)-1-methyl-D-tryptophyl-N1-(4-carbamimidoylbenzyl)-D-glutamamide
Homo sapiens
in 500 mM Tris-HCl, pH 7.5, 1.5 M NaCl, 50 mM CaCl2, temperature not specified in the publication
0.00014
N-(ethylsulfonyl)-5-hydroxy-D-tryptophyl-N1-(4-carbamimidoylbenzyl)-D-glutamamide
Homo sapiens
in 500 mM Tris-HCl, pH 7.5, 1.5 M NaCl, 50 mM CaCl2, temperature not specified in the publication
0.000065
N-(ethylsulfonyl)-5-methoxy-D-tryptophyl-N1-(4-carbamimidoylbenzyl)-D-glutamamide
Homo sapiens
in 500 mM Tris-HCl, pH 7.5, 1.5 M NaCl, 50 mM CaCl2, temperature not specified in the publication
0.000062
N-(ethylsulfonyl)-D-tryptophyl-N1-(4-carbamimidoylbenzyl)-L-glutamamide
Homo sapiens
in 500 mM Tris-HCl, pH 7.5, 1.5 M NaCl, 50 mM CaCl2, temperature not specified in the publication
0.00034
2-(3'-amino-3-fluoro-4-(isopropylamino)-1,1'-biphenyl-2-yl)-N-(4-(amino(imino)methyl)benzyl)acetamide
Homo sapiens
-
IC50: 340 nM
0.0005
2-(3'-amino-4-(benzylamino)-3-fluoro-1,1'-biphenyl-2-yl)-N-(4-(amino(imino)methyl)benzyl)acetamide
Homo sapiens
-
IC50: 500 nM
0.0007
2-(3-allylamino-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl)-N-(4-carbamimidoyl-benzyl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 700 nM
0.00077
2-(3-benzylamino-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl)-N-(4-carbamimidoyl-benzyl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 770 nM
0.0064
2-(3-benzylsulfanyl-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl)-N-(4-carbamimidoyl-benzyl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0064 mM
0.0032
2-(3-butylamino-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl)-N-(4-carbamimidoyl-benzyl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0032 mM
0.0021
2-[3-(2-amino-ethylamino)-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0021 mM
0.00089
2-[3-(3-amino-propylamino)-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 890 nM
0.00098
2-[3-(4-amino-butylamino)-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 980 nM
0.003
2-[3-(4-tert-butyl-cyclohexylamino)-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.003 mM
0.013
2-[3-(adamantan-1-ylamino)-5-chloro-2-oxo-6-phenyl-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.013 mM
0.00161
2-[6-(3-acetylamino-phenyl)-5-chloro-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.00161 mM
0.00007
2-[6-(3-amino-phenyl)-5-chloro-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 70 nM
0.00002
2-[6-(3-amino-phenyl)-5-chloro-3-cyclobutylamino-2-oxo-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 20 nM
0.00002
2-[6-(3-amino-phenyl)-5-chloro-3-isopropylamino-2-oxo-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 20 nM
0.0042
2-[6-(3-bromo-phenyl)-5-chloro-3-cyclobutylamino-2-oxo-2H-pyrazin-1-yl]-N-(4-carbamimidoyl-benzyl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0042 mM
0.000118
3-amino-5-(1-(1-((4-(amino(imino)methyl)benzyl)-amino)-2-oxoethyl)-5-(isopropylamino)-6-oxo-1,6-dihydropyridin-2-yl)benzoic acid
Homo sapiens
-
IC50: 118 nM
0.000016
3-amino-5-[1-[2-([4-[amino(imino)methyl]benzyl]amino)-2-oxoethyl]-3-chloro-5-(isopropylamino)-6-oxo-1,6-dihydropyrazin-2-yl]benzoic acid
Homo sapiens
-
pH 8.0, IC50: 16 nM, potent and highly selective inhibitor, selectivity versus factor Xa and thrombin
0.0003
3-methyl-2-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-pentanoic acid [4-guanidino-1-(thiazole-2-carbonyl)-butyl]-amide
Homo sapiens
-
IC50: 300 nM, reversible, covalent
0.00145
3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 0.00145 mM, reversible, covalent
0.00036
3-[1-[(4-carbamimidoyl-benzylcarbamoyl)-methyl]-3-chloro-5-isopropylamino-6-oxo-1,6-dihydro-pyrazin-2-yl]-benzoic acid
Homo sapiens
-
pH 8.0, IC50: 360 nM
0.00078
3-[1-[(4-carbamimidoyl-benzylcarbamoyl)-methyl]-3-chloro-5-isopropylamino-6-oxo-1,6-dihydro-pyrazin-2-yl]-benzoic acid methyl ester
Homo sapiens
-
pH 8.0, IC50: 780 nM
0.0007
4,4-dimethyl-2-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-pentanoic acid [4-guanidino-1-(thiazole-2-carbonyl)-butyl]-amide
Homo sapiens
-
IC50: 700 nM, reversible, covalent
0.00282
6-dimethylamino-2-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-hexanoic acid [4-guanidino-1-(thiazole-2-carbonyl)-butyl]-amide
Homo sapiens
-
IC50: 0.00282 mM, reversible, covalent
0.0000015 - 0.0000016
EEWEVLCWTWETCER
0.0000038
EEWEVLCWTWETCERGEG-(Z-domain of protein A)
Homo sapiens
-
IC50: 3.8 nM
-
0.0000015
EEWEVLCWTWETCERGEG-NH2
Homo sapiens
-
IC50: 1.5 nM
0.00000023
EEWEVLCWTWETCERGEGVEEELWEWR
Homo sapiens
-
maximal inhibition to 99%, IC50: 230 pM
0.00047
EVLCWTWETCER-NH2
Homo sapiens
-
IC50: 470 nM
0.0000048
EWEVLCWTWETCERGE-(Z-domain of protein A)
Homo sapiens
-
IC50: 4.8 nM
-
0.019
FFR-FVIIa
Homo sapiens
-
derivate of FVIIa with a stably buried N-terminus representing the active conformation of FVIIa, IC50: 0.019 mM
-
0.0001
hemextin AB complex
Homo sapiens
-
IC50: 100 nM
-
0.0000059
MEEWEVLCWTWETCERGEGQ-(Z-domain of protein A)
Homo sapiens
-
IC50: 5.9 nM
-
0.00045
N-(3-[1-[(4-carbamimidoyl-benzylcarbamoyl)-methyl]-3-chloro-6-oxo-5-phenethylamino-1,6-dihydro-pyrazin-2-yl]-phenyl)-2,2,2-trifluoro-acetamide
Homo sapiens
-
pH 8.0, IC50: 450 nM
0.0164
N-(4-(amino(imino)methyl)benzyl)-2-(2,6-difluoro-3-((2-phenylethyl)amino)phenyl)acetamide
Homo sapiens
-
IC50: 0.0164 mM
0.00398
N-(4-(amino(imino)methyl)benzyl)-2-(3-fluoro-4-((2-phenylethyl)amino)-1,1'-biphenyl-2-yl)acetamide
Homo sapiens
-
IC50: 0.00398 mM
0.0027
N-(4-(amino(imino)methyl)benzyl)-2-(3-hydroxy-4-((2-phenylethyl)amino)-1,1'-biphenyl-2-yl)acetamide
Homo sapiens
-
IC50: 0.0027 mM
0.0025
N-(4-(amino(imino)methyl)benzyl)-2-(3-hydroxy-4-(isopropylamino)-1,1'-biphenyl-2-yl)acetamide
Homo sapiens
-
IC50: 0.0025 mM
0.025
N-(4-(amino(imino)methyl)benzyl)-2-(3-methoxy-4-((2-phenylethyl)amino)-1,1'-biphenyl-2-yl)acetamide
Homo sapiens
-
IC50: 0.025 mM
0.0147
N-(4-(amino(imino)methyl)benzyl)-2-(4-(isopropylamino)-3-methoxy-1,1'-biphenyl-2-yl)acetamide
Homo sapiens
-
IC50: 0.0147 mM
0.0028
N-(4-(amino(imino)methyl)benzyl)-2-(5-(isopropylamino)-3,6-dioxo-2-phenylcyclohexa-1,4-dien-1-yl)acetamide
Homo sapiens
-
IC50: 0.0028 mM
0.000052
N-(4-(amino(imino)methyl)benzyl)-2-(6-(3,5-diaminophenyl)-3-(isopropylamino)-2-oxopyridin-1(2H)-yl)acetamide
Homo sapiens
-
IC50: 52 nM
0.00034
N-(4-carbamimidoyl-benzyl)-2-(2-oxo-3-phenethylamino-6-phenyl-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 340 nM
0.001
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-3-phenethylamino-6-m-tolyl-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.001 mM
0.00043
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-3-phenethylamino-6-o-tolyl-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 430 nM
0.00414
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-3-phenethylamino-6-p-tolyl-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.00414 mM
0.00063
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-3-phenethylamino-6-phenyl-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 630 nM
0.0112
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-6-phenyl-3-phenylamino-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0112 mM
0.00072
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-6-phenyl-3-prop-2-ynylamino-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 720 nM
0.0004
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-6-phenyl-3-propylamino-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 400 nM
0.0063
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-2-oxo-6-phenyl-3-pyrrolidin-1-yl-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0063 mM
0.0004
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-3-cyclobutylamino-2-oxo-6-phenyl-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 400 nM
0.0014
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-3-cyclohexylamino-2-oxo-6-phenyl-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0014 mM
0.0004
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-3-ethylamino-2-oxo-6-phenyl-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 400 nM
0.0002
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-3-isopropylamino-2-oxo-6-phenyl-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 200 nM
0.0007
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-3-methylamino-2-oxo-6-phenyl-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 700 nM
0.00345
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-6-ethyl-2-oxo-3-phenethylamino-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.00345 mM
0.00428
N-(4-carbamimidoyl-benzyl)-2-(5-chloro-6-methyl-2-oxo-3-phenethylamino-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.00428 mM
0.0027
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-2-oxo-3-phenethylamino-6-(2-trifluoromethyl-phenyl)-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0027 mM
0.0029
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-2-oxo-3-phenethylamino-6-(3-trifluoromethyl-phenyl)-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0029 mM
0.0018
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-2-oxo-6-phenyl-3-(1-propyl-butylamino)-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0018 mM
0.0126
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-2-oxo-6-phenyl-3-(3-phenyl-propylamino)-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0126 mM
0.0063
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-2-oxo-6-phenyl-3-(3-trifluoromethyl-benzylamino)-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0063 mM
0.0041
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-2-oxo-6-phenyl-3-(4-phenyl-butylamino)-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0041 mM
0.001
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(1,1-dioxo-tetrahydro-16-thiophen-3-ylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.001 mM
0.0098
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(1-ethyl-hexylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0098 mM
0.00043
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(1-ethyl-propylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 430 nM
0.00084
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(1-methyl-butylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 840 nM
0.0009
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(1-methyl-pentylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 900 nM
0.0038
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(2,5-difluoro-benzylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0038 mM
0.0209
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(2-dimethylamino-ethylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0209 mM
500
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(2-hydroxy-ethylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 500 mM
880
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(2-methoxy-ethylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 880 mM
0.008
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(2-morpholin-4-yl-ethylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.008 mM
0.006
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(3,5-difluoro-benzylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.006 mM
0.0176
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(3-dimethylamino-propylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0176 mM
0.0005
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(3-hydroxy-propylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 500 nM
0.0043
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(4-chloro-benzylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0043 mM
0.0006
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(4-hydroxy-butylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 600 nM
0.00047
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(6-hydroxy-hexylamino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 470 nM
0.0091
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-(isopropyl-methyl-amino)-2-oxo-6-phenyl-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0091 mM
0.00034
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-cyclobutylamino-6-(2-hydroxy-phenyl)-2-oxo-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 340 nM
0.0002
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-3-cyclobutylamino-6-(3-hydroxy-phenyl)-2-oxo-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 200 nM
0.003
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(2-chloro-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.003 mM
0.0018
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(2-fluoro-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0018 mM
0.0016
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(2-methoxy-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0016 mM
0.00198
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(3-chloro-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.00198 mM
0.0012
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(3-dimethylamino-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0012 mM
0.0023
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(3-fluoro-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0023 mM
0.0006
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(3-methanesulfonylamino-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 600 nM
0.0052
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(3-methoxy-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0052 mM
0.0006
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(3-methylamino-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 600 nM
0.00252
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(3-nitro-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.00252 mM
0.00888
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(4-chloro-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.00888 mM
0.0081
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(4-fluoro-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0081 mM
0.02345
N-(4-carbamimidoyl-benzyl)-2-[5-chloro-6-(4-methoxy-phenyl)-2-oxo-3-phenethylamino-2H-pyrazin-1-yl]-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.02345 mM
0.03
N-(4-carbamimidoyl-benzyl)-2-{5-chloro-2-oxo-6-phenyl-3-[2-(3-trifluoromethyl-phenyl)-ethylamino]-2H-pyrazin-1-yl}-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.03 mM
0.00018
N-(4-carbamimidoyl-benzyl)-2-{5-chloro-3-[2-(3-chloro-phenyl)-ethylamino]-2-oxo-6-phenyl-2H-pyrazin-1-yl}-acetamide
Homo sapiens
-
pH 8.0, IC50: 180 nM
0.0006
N-(4-carbamimidoyl-benzyl)-2-{5-chloro-3-[2-(4-chloro-phenyl)-ethylamino]-2-oxo-6-phenyl-2H-pyrazin-1-yl}-acetamide
Homo sapiens
-
pH 8.0, IC50: 600 nM
0.0167
N-(5-carbamimidoyl-pyridin-2-ylmethyl)-2-(2-oxo-3-phenethylamino-6-phenyl-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0167 mM
0.0014
N-(6-carbamimidoyl-pyridin-3-ylmethyl)-2-(2-oxo-3-phenethylamino-6-phenyl-2H-pyrazin-1-yl)-acetamide
Homo sapiens
-
pH 8.0, IC50: 0.0014 mM
0.0002
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-(3,4,5-trifluoro-phenyl)-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 200 nM, reversible, covalent
0.0008
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-(3-trifluoromethyl-phenyl)-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 800 nM, reversible, covalent
0.00156
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-(4-iodo-phenyl)-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 0.00156 mM, reversible, covalent
0.00588
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-(4-nitro-phenyl)-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 0.00588 mM, reversible, covalent
0.00011
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-hydroxy-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 110 nM, reversible, covalent
0.00017
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-m-tolyl-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 170 nM, reversible, covalent
0.0056
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-naphthalen-1-yl-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 0.0056 mM, reversible, covalent
0.00195
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-naphthalen-2-yl-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 0.00195 mM, reversible, covalent
0.00024
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-o-tolyl-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 240 nM, reversible, covalent
0.00129
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-p-tolyl-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 0.00129 mM, reversible, covalent
0.000042
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-phenyl-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 42 nM, reversible, covalent
0.0002
N-[1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-2-pyridin-3-yl-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 200 nM, reversible, covalent
0.00997
N-[2-(1-benzyl-1H-imidazol-4-yl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 0.00997 mM, reversible, covalent
0.0007
N-[2-(2,6-dimethyl-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 700 nM, reversible, covalent
0.00009
N-[2-(2-fluoro-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 90 nM, reversible, covalent
0.00016
N-[2-(3,4-difluoro-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 160 nM, reversible, covalent
0.00019
N-[2-(3,5-difluoro-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 190 nM, reversible, covalent
0.00023
N-[2-(3-chloro-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 230 nM, reversible, covalent
0.0002
N-[2-(3-fluoro-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 200 nM, reversible, covalent
0.00057
N-[2-(4-acetylamino-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 570 nM, reversible, covalent
0.00076
N-[2-(4-bromo-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 760 nM, reversible, covalent
680
N-[2-(4-chloro-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 680 mM, reversible, covalent
0.00034
N-[2-(4-cyano-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 340 nM, reversible, covalent
0.00017
N-[2-(4-fluoro-phenyl)-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 170 nM, reversible, covalent
0.0005
N-[2-benzo[b]thiophen-3-yl-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 0.0005 mM, reversible, covalent
0.00153
N-[2-benzyloxy-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 0.00153 mM, reversible, covalent
0.00183
N-[2-biphenyl-3-yl-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 0.00183 mM, reversible, covalent
0.0178
N-[2-biphenyl-4-yl-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 0.0178 mM, reversible, covalent
0.0033
N-[2-cyclohexyl-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 0.0033 mM, reversible, covalent
0.00082
N-[2-cyclopropyl-1-[4-guanidino-1-(thiazole-2-carbonyl)-butylcarbamoyl]-ethyl]-3-phenyl-2-phenylmethanesulfonylamino-propionamide
Homo sapiens
-
IC50: 820 nM, reversible, covalent
0.00318
N-[4-guanidino-1-(thiazole-2-carbonyl)-butyl]-3-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-succinamic acid cyclohexyl ester
Homo sapiens
-
IC50: 0.00318 mM, reversible, covalent
0.0137
N-[4-guanidino-1-(thiazole-2-carbonyl)-butyl]-4-methanesulfonyl-2-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-butyramide
Homo sapiens
-
IC50: 0.0137 mM, reversible, covalent
0.0009
N-[4-guanidino-1-(thiazole-2-carbonyl)-butyl]-4-phenyl-2-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-butyramide
Homo sapiens
-
IC50: 900 nM, reversible, covalent
0.00103
N1-[4-guanidino-1-(thiazole-2-carbonyl)-butyl]-2-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-succinamide
Homo sapiens
-
IC50: 0.00103 mM, reversible, covalent
0.0044
SAEWEVLCWTWEGCGSVGL-(Z-domain of protein A)
Homo sapiens
-
IC50: 4400 nM
0.000093
SEEWEVLCWTWEDCRLEGLE-(Z-domain of protein A)
Homo sapiens
-
IC50: 93 nM
-
0.014
V154G-FVIIa
Homo sapiens
-
derivate of FVIIa with a fully exposed N-terminus representing the zymogen-like conformation of FVIIa, IC50: 0.014 mM
-
0.000000022
VLCWTWETCER-NH2
Homo sapiens
-
IC50: 0.022 nM
0.013
WEVLCWTWETC-NH2
Homo sapiens
-
IC50: 0.013 mM
0.007
WEVLCWTWETCE-NH2
Homo sapiens
-
IC50: 0.007 mM
0.0000025
WEVLCWTWETCER-NH2
Homo sapiens
-
IC50: 2.5 nM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
7.4
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15
-
cleavage of Ile-Pro-Arg-p-nitroanilide
22
-
assay at room temperature
30
-
cleavage of Ile-Pro-Arg-p-nitroanilide, in presence of tissue factor
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 40
-
5°C: about 90% of maximal activity, 40°C: about 50% of maximal activity, cleavage of Ile-Pro-Arg-p-nitroanilide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FA7_HUMAN
466
0
51594
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
SDS-PAGE, recombinant fusion protein
45530
-
fully de-N-glycosylated protein, studied by MALDI-TOF mass spectrometry
46070
-
calculated from the amino acid sequence and considering 12 disulfide bridges
50000
50100
-
native FVIIa, studied by MALDI-TOF mass spectrometry
additional information
-
the zymogen, factor VII, is composed of a single polypeptide chain polypeptide of 48000 Da, with the NH2-terminal sequence Ala-Asn-Ala-Phe-Leu-(gamma-carboxyglutamic acid)-(gamma-carboxyglutamic acid)-Leu-Arg-Pro. It is converted to a two-chain form, factor VIIa, connected by disulfide bonds by the action of factor Xa, in the presence of phospholipids and calcium and by factor XIIa, without additional cofactors
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
FVII is secreted as a single-chain polypeptide and a peptide bond cleavage (after arginine 152) results in the enzymatically active form FVIIa. The two polypeptide chains are referred to as light (152 residues) and heavy (254 residues). The light chain contains an N-terminal gamma-carboxyglutamic acid (Gla) domain, in which all ten Glu residues are posttranslationally-carboxylated
glycoprotein
proteolytic modification
additional information
-
FVII undergoes many posttranslational modifications such as gamma-carboxylation, N- and O-glycosylation, beta-hydroxylation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with acetyl-ALCDDPRVDRWYCQFVEG-NH2, hanging-drop method
hanging drop vapor diffusion method, using 0.1 M sodium citrate buffer at pH 5.1, 16.6% PEG 3350, 12.5% (v/v) 1-propanol, or 0.1 M cacodylate buffer at pH 5.6, 12% (w/v) PEG 8000
hanging drop vapour diffusion method
in complex with tissue factor
N-terminally truncated factor VII, activated recombinant factor VII is crystallized in the presence of the reversible S1-site inhibitor benzamidine
structure of the gamma-carboxyglutamic acid-domainless human coagulation factor VIIa at a resolution of 2.8 A
2 A resolution crystal structure of a zymogen form of factor VII comprising the EGF2 and protease domains is revealed in a complex with the exosite binding inhibitory peptide A-183 and a vacant active site, hanging-drop method
-
crystal structure at 2.0 A resolution of active-site-inhibited factor VIIa complexed with the cleaved extracellular domain of tissue factor
-
crystal structure of factor FVIIa is inhibited at the active site with 1,5-dansyl-Glu-Gly-Arg-chloromethyl ketone and lacking the Gla domain
-
purified complex between Trp-Tyr-Thr-Arg-cmk-FVIIa and sTF1?209, hanging drop vapour diffusion method, 10 mg/ml protein in 10 mM Tris-HCl, pH 7.5, 100 mM NaCl and 2 mM CaCl2, with 0.1 M sodium citrate, 16.5–15.5% w/v PEG 4000 and 12% v/v propan-1-ol, pH 5.6, as the precipitating agent, X-ray diffraction structure determination and analysis, modeling
-
sitting-drop vapour-diffusion method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
306X
mutation studies show that the interaction between protein cofactor tissue factor and methionine-306 in the serine protease domain of FVIIa triggers the activation process and suggested some ensuing steps on the pathway to the active conformation
G372A
mutant G372A, both in the free and tissue factor-bound form, exhibit reduced cleavage of factor X and of D-Ile-Pro-Arg-4-nitroanilide (kcat increased compared to wild-type), and have increased Km values compared with wild-type FVIIa. Inhibition of mutant G372A +soluble tissue factor by 4-aminobenzamidine is characterized by a seven-fold higher Ki than obtained with wild-type. Crystallographic and modelling data suggest that the most active conformation of FVIIa depends on the backbone hydrogen bond between Gly372 and Arg315 in the 170 loop. Native and active site-inhibited mutant G372A binds soluble tissue factor with the same affinity as the corresponding forms of FVIIa
R353Q
in an observational study of 93 Japanese women 10 SNPs in relation to thrombosis or atherosclerosis are studied. Factor VII Arg353Gln and higher HDL-cholesterol (HDL-C) are linked to Arg/Arg carriers at higher levels
A294V
-
mutant enzyme shows delayed activation by activated factor X as well as reduced activity towards peptidyl and macromolecular substrates without impairing the catalytic efficiency of the triad
C164V/V299C-FVIIa
-
introduction of a new disulfide bridge between Cys-159 and an introduced Cys at position 299
D102Q
-
inactive mutant enzyme
D186A
-
turnover-number for activation of factor X is 5.5fold lower than that of the wild-type factor VII, Km-value for activation of factor X is 1.2fold lower than that of the wild-type factor VII
D343H
-
mutant enzyme shows no activity with methanesulfonyl-D-cyclohexylalanyl-butyl-arginine p-nitroanilide, factor X and factor IX
D72N
-
the mutant shows 13% of wild type FVIIa signaling activity towards protease-activated receptor 2
DELTA360-329
-
lower affinity for soluble tissue factor as compared to wild-type factor VIIa, 7fold smaller tissue factor-mediated acceleration of amidolytic activity compared to wild type factor VIIa
E154A
-
slightly increased Km-value and decreased turnover number compared to the wild-type enzyme
E154R
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
E296R
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
F256A
-
turnover-number and Km-value for activation of factor X are nearly identical to that of the wild-type factor VII
F374P
-
the specific clotting activity in presence of tissue factor is 50% of that of the wild-type factor VIIa
H101A
-
turnover-number for activation of factor X is 1.12fold lower than that of the wild-type factor VII, Km-value for activation of factor X is 1.23fold lower than that of the wild-type factor VII. Activation by factor Xa is significantly more slowly than that of wild-type enzyme. Tissue factor affinity and small substrate activity is similar to wild-type enzyme
H216A
-
mutant enzyme with decreased sensitivity to Zn2+ inhibition
H257A
-
mutant enzyme with decreased sensitivity to Zn2+ inhibition
K192E
-
completely ineffective mutant enzyme
K192Q
K305V
-
the ratio of turnover number to Km-value is 5.3fold higher than that of the wild-type enzyme with factor X as substrate, increased inhibition rate compared to wild-type enzyme with antithrobin in presence of heparin
K337A
K341Q
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
L144A
L144A/R147A/D186A
-
turnover-number for activation of factor X is 239fold lower than that of the wild-type factor VII, Km-value for activation of factor X is 1.2fold higher than that of the wild-type factor VII
L280I/V299M-FVIIa
-
without description
L305V
-
mutant enzyme exhibits an increased rate of inhibition as compared with wild-type enzyme, both by D-Phe-Phe-Arg-chloromethyl ketone and antithombin III in presence of heparin. In complex with tissue factor both the amydolytic activity and the proteolytic activity are similar to that of the wild-type activity.The specific clotting activity in presence of tissue factor is 93% of that of the wild-type factor VIIa
L305V/K337A
-
the ratio of turnover number to Km-value is 6.3fold higher than that of the wild-type enzyme with factor X as substrate, increased inhibition rate compared to wild-type enzyme with antithrobin in presence of heparin
L305V/M306D/D309S
-
amidylatic and proteolytic activity are virtually unaffected by the presence of tissue factor, 1.1fold increase. The specific clotting activity in presence of tissue factor is about 1% of that of the wild-type factor VIIa
M156K
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
M156Q
M298K
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
M298Q
M306D
M306N
-
amidolytic activity of the mutant enzyme is stimulated 7fold
M306N/N309S
-
amidolytic activity of the mutant enzyme is stimulated 1.5fold
M306S
-
amidolytic activity of the mutant enzyme is stimulated 9fold
M306T
-
amidolytic activity of the mutant enzyme is stimulated 12fold
N100A
-
turnover-number for activation of factor X is 3fold lower than that of the wild-type factor VII, Km-value for activation of factor X is 1.4fold lower than that of the wild-type factor VII
N100A/H101A/Y179A/F256A
-
turnover-number for activation of factor X is 3fold lower than that of the wild-type factor VII, Km-value for activation of factor X is nearly identical to that of the wild-type factor VII. Activation by factor Xa is significantly more slowly than that of wild-type enzyme
P10Q
-
site-directed mutagenesis, the mutant shows 2fold enhancement in membrane binding affinity over wild-type FVIIa
P10Q/K32E
-
site-directed mutagenesis, the mutant shows 27fold enhancement in membrane binding affinity over wild-type FVIIa, the double mutant displays a significantly improved procoagulant effect in haemophilic blood
P10Q/K32E/D33F/A34E
-
site-directed mutagenesis, the mutant shows 150-300fold enhancement in membrane binding affinity over wild-type FVIIa
P10Q/Q32E
-
mutant enzyme with elevated affinity for membrane. Phospholipid and cell-based assays show that mutant enzyme has an up to 40fold higher function then wild-type enzyme in both tissue-factor dependent reaction and in tissue factor independent reaction
Q143N
-
the mutant reduces interleukin-8 expression to background levels but maintains essentially normal pro-coagulant activity
Q143R
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
Q176G
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
Q217E
-
the mutant shows enhanced protease-activated receptor 2 activation
Q286R
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
Q40A
-
the mutant reduces interleukin-8 expression to background levels but maintains essentially normal pro-coagulant activity
Q40G
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
R147A
-
turnover-number for activation of factor X is 3.7fold lower than that of the wild-type factor VII, Km-value for activation of factor X is 1.2fold lower than that of the wild-type factor VII
R152Q
-
mutant enzyme shows no activity with methanesulfonyl-D-cyclohexylalanyl-butyl-arginine p-nitroanilide, factor X and factor IX
S344A
-
mutant enzyme shows no activity with methanesulfonyl-D-cyclohexylalanyl-butyl-arginine p-nitroanilide, factor X and factor IX
T151A
-
the mutant shows 13% of wild type FVIIa signaling activity towards protease-activated receptor 2
T151Q
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
T151S
-
the variant activates macromolecular coagulation substrates and supports signaling of the ternary tissue factor-FVIIa-Xa complex normally but is severely impaired in binary tissue factor-FVIIa-protease-activated receptor 2 signaling
T239A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T239G
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T239I
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T239Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T293Q
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
T99A
-
the mutant shows 17% of wild type FVIIa signaling activity towards protease-activated receptor 2
T99Y
-
the mutation leads to enhanced protease-activated receptor 2 activation (2-3fold above the wild type FVIIa activity)
V154A
-
mutant enzyme shows reduced proteolytic activity towards factor X and undetectable activity towards factor IX
V154G
-
naturally occuring mutation, mutant enzyme with a zymogen-like form, markedly reduced activity towards peptidyl substrate and undetectable activity towards macromolecular substrates
V158D/D296V/M298Q
-
the ratio of turnover number to Km-value is 37.5fold higher than that of the wild-type enzyme with factor X as substrate, increased inhibition rate compared to wild-type enzyme with antithrobin in presence of heparin
V158D/D296V/M298Q/K337A
-
the ratio of turnover number to Km-value is 56.3fold higher than that of the wild-type enzyme with factor X as substrate, increased inhibition rate compared to wild-type enzyme with antithrobin in presence of heparin
V158D/D296V/M298Q/L305V
-
the ratio of turnover number to Km-value is 50fold higher than that of the wild-type enzyme with factor X as substrate, increased inhibition rate compared to wild-type enzyme with antithrobin in presence of heparin
V158D/D296V/M298Q/L305V/L337
-
the ratio of turnover number to Km-value is 100fold higher than that of the wild-type enzyme with factor X as substrate, increased inhibition rate compared to wild-type enzyme with antithrobin in presence of heparin
V158D/E296V/M298Q
-
site-directed mutagenesis, FVIIa analogues with a stabilized activation domain and N-terminal insertion, the mutant shows increased activity compared to the wild-type enzyme
V158E
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
V21E
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
V21N/E154I/M156Q
-
mutant enzyme with stabilized amino-terminal Ile16-Asp194 salt bridge and enhanced catalytic function
V299M-FVIIa
-
modification of the first Leu-X-Val motif by the introduction of Met in the third position
Y179A
-
turnover-number for activation of factor X is nearly identical to that of the wild-type factor VII, Km-value for activation of factor X is 1.6fold lower than that of the wild-type factor VII. Activation by factor Xa is significantly more slowly than that of wild-type enzyme. Tissue factor affinity and small substrate activity is similar to wild-type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58
-
heat inactivation is fully reversible up to 15 min
60
-
the melting temperature of the recombinant enzyme is at about 60°C. GlycoPEGylation delays the thermally induced aggregation, and slightly increases the unfolding temperature of the protein from 57.7°C to 59°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification process starts with pH adjustment of the clarified medium, which is loaded onto an anion-exchange column. Detergent is added to the eluate in order to inactivate enveloped viruses. Subsequently, FVII and FVIIa are affinity purified on a column with a monoclonal antibody recognizing the FVII Gla domain in its functional conformation. Only FVII/FVIIa without propetide and with a functional and sufficiently gamma-carboxylated Gla domain is captured and purified. The eluate from the affinity column is subjected to two anion-exchange chromatography steps
recombinant factor VII
ResourceQ column chromatography
using Ni-NTA chromatography
anion exchange chromatography
-
dialysis
-
factor VII
-
method not mentioned
-
recombinant FVII zymogen from BHK cell medium
-
wild-type and mutant enzymes expressed in CHO-K1 cells
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Spodoptera frugiperda Sf9 cell line using the baculovirus expression system. Recombinant human FVII (rhFVII) produced in this study carries a 6x-His tag at the C-terminal
expression of an N-terminally truncated factor VII in Escherichia coli
for expression as a recombinant protein in baby hamster kidney cells cDNA comprising the entire FVII open reading frame encoding signal peptide, propeptide and the mature FVII protein is inserted into an expression plasmid containing the elements required to direct transcription of the FVII cDNA in mammalian cells. The endogenous signal peptide and propeptide of FVII are necessary for intracellular transport and processing of FVII in the producer cells but are both removed prior to secretion
expressed as a recombinant protein
-
expressed in baby hamster kidney cells
-
expressed in CHO-K1 cells
-
expressed in human 293 cells
-
expression of wild-type and mutant enzymes in BHK cells
-
expression of wild-type and mutant enzymes in CHO-K1 cells
-
genetic localization at 13q34, cloning from a liver gene library, expression in BHK cells with secretion to the medium
-
recombinant wild-type and mutant factor VII is expressed in Chinese hamster ovary cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
raised FVIIc activity levels in coronary heart disease are significantly positively correlated with insulin resistance
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
to overcome the defect for high-level expression of the functional recombinant coagulation FVII in Sf9 cell this method involves simultaneous expression of both human c-carboxylase and human FVII genes in the host leading to a high-level expression of functional recombinant factor VII
medicine
the therapeutic efficacy and safety of recombinant factor VIIa in haemophilia patients with inhibitors is established in a number of clinical trials which also forms the basis for regulatory approval
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Broze, G.J.; Majerus, P.W.
Purification and properties of human coagulation factor VII
J. Biol. Chem.
255
1242-1247
1990
Homo sapiens
Manually annotated by BRENDA team
Kemball-Cook, G.; Johnson, D.J.D.; Tuddenham, E.G.D.; Harlos, K.
Crystal structure of active site-directed human coagulation factor VIIa (des-Gla)
J. Struct. Biol.
127
213-223
1999
Homo sapiens
Manually annotated by BRENDA team
Thiruvikraman, S.V.; Roboz, J.; Wang, T.; Ma, L.; Seaman, G.; Guha, A.
Characterization of digoxigenin derivatives of human coagulation factors VIIa and X by electrospray mass spectrometry
Rapid Commun. Mass Spectrom.
10
1367-1370
1996
Homo sapiens
Manually annotated by BRENDA team
Petersen, L.C.; Persson, E.; Fresgard, P.O.
Thermal effects on an enzymatically latent conformation of coagulation factor VIIa
Eur. J. Biochem.
261
124-129
1999
Homo sapiens
Manually annotated by BRENDA team
Banner, D.W.; D'Arcy, A.; Chene, C.; Winkler, F.K.; Guha, A.; Konigsberg, W.H.; Nemerson, Y.; Kirchhofer, D.
The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
Nature
380
41-46
1996
Homo sapiens
Manually annotated by BRENDA team
Shobe, J.; Dickinson, C.D.; Ruf, W.
Regulation of the catalytic function of coagulation factor VIIa by a conformational linkage of surface residue Glu 154 to the active site
Biochemistry
38
2745-2751
1999
Homo sapiens
Manually annotated by BRENDA team
Pike, A.C.W.; Brzozowski, A.M.; Roberts, S.M.; Olsen, O.H.; Persson, E.
Structure of human factor VIIa and its implications for the triggering of blood coagulation
Proc. Natl. Acad. Sci. USA
96
8925-8930
1999
Homo sapiens (P08709), Homo sapiens
Manually annotated by BRENDA team
Neuenschwander, P.F.; Morrissey, J.H.
Alteration of the substrate and inhibitor specificities of blood coagulation factor VIIa: importance of amino acid residue K
Biochemistry
34
8701-8707
1995
Homo sapiens
Manually annotated by BRENDA team
Toso, R.; Pinotti, M.; High, K.A.; Pollak, E.S.; Bernardi, F.
A frequent human coagulation Factor VII mutation (A294V, c152) in loop 140s affects the interaction with activators, tissue factor and substrates
Biochem. J.
363
411-416
2002
Homo sapiens
Manually annotated by BRENDA team
Toso, R.; Bernardi, F.; Tidd, T.; Pinotti, M.; Camire, R.M.; Marchetti, G.; High, K.A.; Pollak, E.S.
Factor VII mutant V154G models a zymogen-like form of factor VIIa
Biochem. J.
369
563-571
2003
Homo sapiens
Manually annotated by BRENDA team
Jin, J.; Chang, J.; Stafford, D.W.; Straight, D.L.
Residues Y179 and H101 of a hydrophobic patch of factor VII are involved in activation by factor Xa
Biochemistry
40
11405-11410
2001
Homo sapiens
Manually annotated by BRENDA team
Persson, E.; Nielsen, L.S.; Olsen, O.H.
Substitution of aspartic acid for methionine-306 in factor VIIa abolishes the allosteric linkage between the active site and the binding interface with tissue factor
Biochemistry
40
3251-3256
2001
Homo sapiens
Manually annotated by BRENDA team
Dennis, M.S.; Roberge, M.; Quan, C.; Lazarus, R.A.
Selection and characterization of a new class of peptide exosite inhibitors of coagulation factor VIIa
Biochemistry
40
9513-9521
2001
Homo sapiens
Manually annotated by BRENDA team
Neuenschwander, P.F.; Vernon, J.T.; Morrissey, J.H.
Tissue factor alters the pKa values of catalytically important factor VIIa residues
Biochemistry
41
3364-3371
2002
Homo sapiens
Manually annotated by BRENDA team
Petrovan, R.J.; Ruf, W.
Role of zymogenicity-determining residues of coagulation factor VII/VIIa in cofactor interaction and macromolecular substrate recognition
Biochemistry
41
9302-9309
2002
Homo sapiens
Manually annotated by BRENDA team
Soejima, K.; Mizuguchi, J.; Yuguchi, M.; Nakagaki, T.; Higashi, S.; Iwanaga, S.
Factor VIIa modified in the 170 loop shows enhanced catalytic activity but does not change the zymogen-like property
J. Biol. Chem.
276
17229-17235
2001
Homo sapiens
Manually annotated by BRENDA team
Persson, E.; Bak, H.; Olsen, O.H.
Substitution of valine for leucine 305 in factor VIIa increases the intrinsic enzymatic activity
J. Biol. Chem.
276
29195-29199
2001
Homo sapiens
Manually annotated by BRENDA team
Nelsestuen, G.L.; Stone, M.; Martinez, M.B.; Harvey, S.B.; Foster, D.; Kisiel, W.
Elevated function of blood clotting factor VIIa mutants that have enhanced affinity for membranes: behavior in a diffusion-limited reaction
J. Biol. Chem.
276
39825-39831
2001
Homo sapiens
Manually annotated by BRENDA team
Petrovan, R.J.; Ruf, W.
Residue Met(156) contributes to the labile enzyme conformation of coagulation factor VIIa
J. Biol. Chem.
276
6616-6620
2001
Homo sapiens
Manually annotated by BRENDA team
Maun, H.R.; Eigenbrot, C.; Lazarus, R.A.
Engineering exosite peptides for complete inhibition of factor VIIa using a protease switch with substrate phage
J. Biol. Chem.
278
21823-21830
2003
Homo sapiens
Manually annotated by BRENDA team
Parlow, J.J.; Dice, T.A.; Lachance, R.M.; Girard, T.J.; Stevens, A.M.; Stegeman, R.A.; Stallings, W.C.; Kurumbail, R.G.; South, M.S.
Polymer-assisted solution-phase library synthesis and crystal structure of alpha-ketothiazoles as tissue factor VIIa inhibitors
J. Med. Chem.
46
4043-4049
2003
Homo sapiens
Manually annotated by BRENDA team
Parlow, J.J.; Case, B.L.; Dice, T.A.; Fenton, R.L.; Hayes, M.J.; Jones, D.E.; Neumann, W.L.; Wood, R.S.; Lachance, R.M.; Girard, T.J.; Nicholson, N.S.; Clare, M.; Stegeman, R.A.; Stevens, A.M.; Stallings, W.C.; Kurumbail, R.G.; South, M.S.
Design, parallel synthesis, and crystal structures of pyrazinone antithrombotics as selective inhibitors of the tissue factor VIIa complex
J. Med. Chem.
46
4050-4062
2003
Homo sapiens
Manually annotated by BRENDA team
Parlow, J.J.; Stevens, A.M.; Stegeman, R.A.; Stallings, W.C.; Kurumbail, R.G.; South, M.S.
Synthesis and crystal structures of substituted benzenes and benzoquinones as tissue factor VIIa inhibitors
J. Med. Chem.
46
4297-4312
2003
Homo sapiens
Manually annotated by BRENDA team
Parlow, J.J.; Kurumbail, R.G.; Stegeman, R.A.; Stevens, A.M.; Stallings, W.C.; South, M.S.
Design, Synthesis, and crystal structure of selective 2-pyridone tissue factor VIIa inhibitors
J. Med. Chem.
46
4696-4701
2003
Homo sapiens
Manually annotated by BRENDA team
Sichler, K.; Banner, D.W.; D'Arcy, A.; Hopfner, K.P.; Huber, R.; Bode, W.; Kresse, G.B.; Kopetzki, E.; Brandstetter, H.
Crystal structures of uninhibited factor VIIa link its cofactor and substrate-assisted activation to specific interactions
J. Mol. Biol.
322
591-603
2002
Homo sapiens (P08709)
Manually annotated by BRENDA team
Dennis, M.S.; Eigenbrot, C.; Skelton, N.J.; Ultsch, M.H.; Santell, L.; Dwyer, M.A.; O'Connell, M.P.; Lazarus, R.A.
Peptide exosite inhibitors of factor VIIa as anticoagulants
Nature
404
465-470
2000
Homo sapiens (P08709)
Manually annotated by BRENDA team
Persson, E.; Kjalke, M.; Olsen, O.H.
Rational design of coagulation factor VIIa variants with substantially increased intrinsic activity
Proc. Natl. Acad. Sci. USA
98
13583-13588
2001
Homo sapiens
Manually annotated by BRENDA team
Petersen, L.C.; Olsen, O.H.; Nielsen, L.S.; Freskgard, P.O.; Persson, E.
Binding of Zn2+ to a Ca2+ loop allosterically attenuates the activity of factor VIIa and reduces its affinity for tissue factor
Protein Sci.
9
859-866
2000
Homo sapiens
Manually annotated by BRENDA team
Eigenbrot, C.; Kirchhofer, D.; Dennis, M.S.; Santell, L.; Lazarus, R.A.; Stamos, J.; Ultsch, M.H.
The factor VII zymogen structure reveals reregistration of beta strands during activation
Structure
9
627-636
2001
Homo sapiens
Manually annotated by BRENDA team
Carr, M.E., Jr.; Martin, E.J.; Kuhn, J.G.; Seremetis, S.V.
Effects of recombinant factor VIIa on platelet function and clot structure in blood with deficient prothrombin conversion
Thromb. Haemost.
89
803-811
2003
Homo sapiens
Manually annotated by BRENDA team
Persson, E.
Macromolecular substrate affinity for free factor VIIa is independent of a buried protease domain N-terminus
Biochem. Biophys. Res. Commun.
341
28-32
2006
Homo sapiens
Manually annotated by BRENDA team
Persson, E.; Bak, H.; Ostergaard, A.; Olsen, O.H.
Augmented intrinsic activity of Factor VIIa by replacement of residues 305, 314, 337 and 374: evidence of two unique mutational mechanisms of activity enhancement
Biochem. J.
379
497-503
2004
Homo sapiens
Manually annotated by BRENDA team
Kelley, R.F.; Yang, J.; Eigenbrot, C.; Moran, P.; Peek, M.; Lipari, M.T.; Kirchhofer, D.
Similar molecular interactions of factor VII and factor VIIa with the tissue factor region that allosterically regulates enzyme activity
Biochemistry
43
1223-1229
2004
Homo sapiens
Manually annotated by BRENDA team
Olsen, O.H.; Nielsen, P.F.; Persson, E.
Prevention of beta strand movement into a zymogen-like position does not confer higher activity to coagulation factor VIIa
Biochemistry
43
14096-14103
2004
Homo sapiens
Manually annotated by BRENDA team
Stone, M.D.; Harvey, S.B.; Martinez, M.B.; Bach, R.R.; Nelsestuen, G.L.
Large enhancement of functional activity of active site-inhibited factor VIIa due to protein dimerization: insights into mechanism of assembly/disassembly from tissue factor
Biochemistry
44
6321-6330
2005
Homo sapiens
Manually annotated by BRENDA team
Hathcock, J.J.; Rusinova, E.; Gentry, R.D.; Andree, H.; Nemerson, Y.
Phospholipid regulates the activation of factor X by tissue factor/factor VIIa (TF/VIIa) via substrate and product interactions
Biochemistry
44
8187-8197
2005
Homo sapiens
Manually annotated by BRENDA team
Morris, D.R.; Ding, Y.; Ricks, T.K.; Gullapalli, A.; Wolfe, B.L.; Trejo, J.
Protease-activated receptor-2 is essential for factor VIIa and Xa-induced signaling, migration, and invasion of breast cancer cells
Cancer Res.
66
307-314
2006
Homo sapiens
Manually annotated by BRENDA team
Versteeg, H.H.; Spek, C.A.; Slofstra, S.H.; Diks, S.H.; Richel, D.J.; Peppelenbosch, M.P.
FVIIa:TF induces cell survival via G12/G13-dependent Jak/STAT activation and BclXL production
Circ. Res.
94
1032-1040
2004
Homo sapiens
Manually annotated by BRENDA team
Sethi, A.S.; Lees, D.M.; Douthwaite, J.A.; Corder, R.
Factor VIIa stimulates endothelin-1 synthesis in TNF-primed endothelial cells by activation of protease-activated receptor 2
Clin. Sci.
108
255-263
2005
Homo sapiens
Manually annotated by BRENDA team
Banerjee, Y.; Mizuguchi, J.; Iwanaga, S.; Kini, R.M.
Hemextin AB complex, a unique anticoagulant protein complex from Hemachatus haemachatus (African Ringhals cobra) venom that inhibits clot initiation and factor VIIa activity
J. Biol. Chem.
280
42601-42611
2005
Homo sapiens
Manually annotated by BRENDA team
Olivero, A.G.; Eigenbrot, C.; Goldsmith, R.; Robarge, K.; Artis, D.R.; Flygare, J.; Rawson, T.; Sutherlin, D.P.; Kadkhodayan, S.; Beresini, M.; Elliott, L.O.; DeGuzman, G.G.; Banner, D.W.; Ultsch, M.; Marzec, U.; Hanson, S.R.; Refino, C.; Bunting, S.; Kirchhofer, D.
A selective, slow binding inhibitor of factor VIIa binds to a nonstandard active site conformation and attenuates thrombus formation in vivo
J. Biol. Chem.
280
9160-9169
2005
Homo sapiens (P08709)
Manually annotated by BRENDA team
Rand, K.D.; Jorgensen, T.J.; Olsen, O.H.; Persson, E.; Jensen, O.N.; Stennicke, H.R.; Andersen, M.D.
The allosteric activation of coagulation factor VIIa visualized by hydrogen exchange
J. Biol. Chem.
281
23018-23024
2006
Homo sapiens
Manually annotated by BRENDA team
Gosalia, D.N.; Salisbury, C.M.; Ellman, J.A.; Diamond, S.L.
High throughput substrate specificity profiling of serine and cysteine proteases using solution-phase fluorogenic peptide microarrays
Mol. Cell. Proteomics
4
626-636
2005
Homo sapiens
Manually annotated by BRENDA team
Sutherland, M.R.; Friedman, H.M.; Pryzdial, E.L.
Herpes simplex virus type 1-encoded glycoprotein C enhances coagulation factor VIIa activity on the virus
Thromb. Haemost.
92
947-955
2004
Homo sapiens
Manually annotated by BRENDA team
Larsen, K.S.; stergaard, H.; Bjelke, J.R.; Olsen, O.H.; Rasmussen, H.B.; Christensen, L.; Kragelund, B.B.; Stennicke, H.R.
Engineering the substrate and inhibitor specificities of human coagulation factor VIIa
Biochem. J.
405
429-438
2007
Homo sapiens
Manually annotated by BRENDA team
Franchini, M.; Manzato, F.; Salvagno, G.L.; Lippi, G.
Potential role of recombinant activated factor VII for the treatment of severe bleeding associated with disseminated intravascular coagulation: a systematic review
Blood Coagul. Fibrinolysis
18
589-593
2007
Homo sapiens
Manually annotated by BRENDA team
Taketomi, T.; Szlam, F.; Bader, S.O.; Sheppard, C.A.; Levy, J.H.; Tanaka, K.A.
Effects of recombinant activated factor VII on thrombin-mediated feedback activation of coagulation
Blood Coagul. Fibrinolysis
19
135-141
2008
Homo sapiens
Manually annotated by BRENDA team
Olsen, O.H.; Persson, E.
Cofactor-induced and mutational activity enhancement of coagulation factor VIIa
Cell. Mol. Life Sci.
65
953-963
2008
Homo sapiens
Manually annotated by BRENDA team
Bjelke, J.R.; Persson, E.; Rasmussen, H.B.; Kragelund, B.B.; Olsen, O.H.
A loop of coagulation factor VIIa influencing macromolecular substrate specificity
FEBS Lett.
581
71-76
2007
Homo sapiens
Manually annotated by BRENDA team
Bosinski, T.J.; El Solh, A.A.
Recombinant factor VIIa, its clinical properties, and the tissue factor pathway of coagulation
Mini Rev. Med. Chem.
6
1111-1117
2006
Homo sapiens
Manually annotated by BRENDA team
Ahamed, J.; Versteeg, H.H.; Kerver, M.; Chen, V.M.; Mueller, B.M.; Hogg, P.J.; Ruf, W.
Disulfide isomerization switches tissue factor from coagulation to cell signaling
Proc. Natl. Acad. Sci. USA
103
13932-13937
2006
Homo sapiens
Manually annotated by BRENDA team
Olsen, O.H.; Rand, K.D.; stergaard, H.; Persson, E.
A combined structural dynamics approach identifies a putative switch in factor VIIa employed by tissue factor to initiate blood coagulation
Protein Sci.
16
671-682
2007
Homo sapiens
Manually annotated by BRENDA team
Ohkubo, Y.Z.; Tajkhorshid, E.
Distinct structural and adhesive roles of Ca2+ in membrane binding of blood coagulation factors
Structure
16
72-81
2008
Homo sapiens
Manually annotated by BRENDA team
Karatela, R.A.; Sainani, G.S.
Interrelationship between coagulation factor VII and obesity in diabetes mellitus (type 2)
Diabetes Res. Clin. Pract.
84
e41-e44
2009
Homo sapiens
Manually annotated by BRENDA team
Fenaille, F.; Groseil, C.; Ramon, C.; Riande, S.; Siret, L.; Chtourou, S.; Bihoreau, N.
Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII
Glycoconj. J.
25
827-842
2008
Homo sapiens
Manually annotated by BRENDA team
Bolt, G.; Kristensen, C.; Steenstrup, T.D.
More than one intracellular processing bottleneck delays the secretion of coagulation factor VII
Thromb. Haemost.
100
204-210
2008
Homo sapiens
Manually annotated by BRENDA team
Shinagawa, K.; Ploplis, V.A.; Castellino, F.J.
A severe deficiency of coagulation factor VIIa results in attenuation of the asthmatic response in mice
Am. J. Physiol. Lung Cell Mol. Physiol.
296
L763-L770
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Athanasiadis, G.; Esteban, E.; Gaya-Vidal, M.; Dugoujon, J.M.; Moschonas, N.; Chaabani, H.; Bissar-Tadmouri, N.; Harich, N.; Stoneking, M.; Moral, P.
Different evolutionary histories of the coagulation factor VII gene in human populations?
Ann. Hum. Genet.
74
34-45
2010
Homo sapiens
Manually annotated by BRENDA team
Masroori, N.; Halabian, R.; Mohammadipour, M.; Roushandeh, A.M.; Rouhbakhsh, M.; Najafabadi, A.J.; Fathabad, M.E.; Salimi, M.; Shokrgozar, M.A.; Roudkenar, M.H.
High-level expression of functional recombinant human coagulation factor VII in insect cells
Biotechnol. Lett.
32
803-809
2010
Homo sapiens (P08709), Homo sapiens
Manually annotated by BRENDA team
Woodruff, S.I.; Dougherty, A.L.; Dye, J.L.; Mohrle, C.R.; Galarneau, M.R.
Use of recombinant factor VIIA for control of combat-related haemorrhage
Emerg. Med. J.
27
121-124
2010
Homo sapiens
Manually annotated by BRENDA team
Persson, E.; Olsen, O.H.
Activation loop 3 and the 170 loop interact in the active conformation of coagulation factor VIIa
FEBS J.
276
3099-3109
2009
Homo sapiens (P08709)
Manually annotated by BRENDA team
Mei, H.; Hu, Y.; Wang, H.; Shi, W.; Deng, J.; Guo, T.
Binding of EGF1 domain peptide in coagulation factor VII with tissue factor and its implications for the triggering of coagulation
J. Huazhong Univ. Sci. Technol. Med. Sci.
30
42-47
2010
Homo sapiens
Manually annotated by BRENDA team
Beier, U.H.; Schmidt, M.L.; Hast, H.; Kecskes, S.; Valentino, L.A.
Control of disseminated intravascular coagulation in Klippel-Trenaunay-Weber syndrome using enoxaparin and recombinant activated factor VIIa: a case report
J. Med. Case Rep.
4
92
2010
Homo sapiens
Manually annotated by BRENDA team
Funami, J.; Hayashi, T.; Nomura, H.; Ding, Q.F.; Ishitsuka-Watanabe, A.; Matsui-Hirai, H.; Ina, K.; Zhang, J.; Yu, Z.Y.; Iguchi, A.
Clinical factors such as B-type natriuretic peptide link to factor VII, endothelial NO synthase and estrogen receptor alpha polymorphism in elderly women
Life Sci.
85
316-321
2009
Homo sapiens (P08709), Homo sapiens
Manually annotated by BRENDA team
Persson, E.; Bolt, G.; Steenstrup, T.D.; Ezban, M.
Recombinant coagulation factor VIIa--from molecular to clinical aspects of a versatile haemostatic agent
Thromb. Res.
125
483-489
2010
Homo sapiens (P08709)
Manually annotated by BRENDA team
Karatela, R.; Sainani, G.
Interrelationships of factor VII activity and plasma leptin with insulin resistance in coronary heart disease
Atherosclerosis
209
235-240
2010
Homo sapiens
Manually annotated by BRENDA team
Balandina, A.N.; Shibeko, A.M.; Kireev, D.A.; Novikova, A.A.; Shmirev, I.I.; Panteleev, M.A.; Ataullakhanov, F.I.
Positive feedback loops for factor V and factor VII activation supply sensitivity to local surface tissue factor density during blood coagulation
Biophys. J.
101
1816-1824
2011
Homo sapiens
Manually annotated by BRENDA team
Chuansumrit, A.; Teeraratkul, S.; Wanichkul, S.; Treepongkaruna, S.; Sirachainan, N.; Pakakasama, S.; Nuntnarumit, P.; Hongeng, S.; Hongeng, S.
Recombinant-activated factor VII for control and prevention of hemorrhage in nonhemophilic pediatric patients
Blood Coagul. Fibrinolysis
21
354-362
2010
Homo sapiens
Manually annotated by BRENDA team
Shiraishi, T.; Kadono, S.; Haramura, M.; Kodama, H.; Ono, Y.; Iikura, H.; Esaki, T.; Koga, T.; Hattori, K.; Watanabe, Y.; Sakamoto, A.; Yoshihashi, K.; Kitazawa, T.; Esaki, K.; Ohta, M.; Sato, H.; Kozono, T.
Design and synthesis of peptidomimetic factor VIIa inhibitors
Chem. Pharm. Bull.
58
38-44
2010
Homo sapiens (P08709)
Manually annotated by BRENDA team
Plesner, B.; Westh, P.; Nielsen, A.D.
Biophysical characterisation of GlycoPEGylated recombinant human factor VIIa
Int. J. Pharm.
406
62-68
2011
Homo sapiens
Manually annotated by BRENDA team
Larsen, K.S.; Ostergaard, H.; Olsen, O.H.; Bjelke, J.R.; Ruf, W.; Petersen, L.C.
Engineering of substrate selectivity for tissue factor-factor VIIa complex signaling through protease-activated receptor 2
J. Biol. Chem.
285
19959-19966
2010
Homo sapiens
Manually annotated by BRENDA team
Soeda, T.; Nogami, K.; Matsumoto, T.; Ogiwara, K.; Shima, M.
Mechanisms of factor VIIa-catalyzed activation of factor VIII
J. Thromb. Haemost.
8
2494-2503
2010
Homo sapiens
Manually annotated by BRENDA team
Hoffman, M.; Volovyk, Z.; Persson, E.; Gabriel, D.A.; Ezban, M.; Monroe, D.M.
Platelet binding and activity of a factor VIIa variant with enhanced tissue factor independent activity
J. Thromb. Haemost.
9
759-766
2011
Homo sapiens
Manually annotated by BRENDA team
Zhou, H.; Shi, W.; Zhou, B.; Guo, D.; Wang, T.
Tissue factor-factor VIIa regulates interleukin-8, tissue factor and caspase-7 expression in SW620 cells through protease-activated receptor-2 activation
Mol. Med. Rep.
3
269-274
2011
Homo sapiens
Manually annotated by BRENDA team
Seested, T.; Nielsen, H.; Christensen, E.; Appa, R.
Cellular and intracellular distribution of recombinant activated factor VII in the rat liver
Thromb. Haemost.
103
860-862
2010
Homo sapiens
Manually annotated by BRENDA team
Persson, E.; Olsen, O.
Current status on tissue factor activation of factor VIIa
Thromb. Res.
125
S11-S12
2010
Homo sapiens
Manually annotated by BRENDA team
Seested, T.; Appa, R.S.; Christensen, E.I.; Ioannou, Y.A.; Krogh, T.N.; Karpf, D.M.; Nielsen, H.M.
In vivo clearance and metabolism of recombinant activated factor VII (rFVIIa) and its complexes with plasma protease inhibitors in the liver
Thromb. Res.
127
356-362
2011
Homo sapiens
Manually annotated by BRENDA team
Maroney, S.A.; Ellery, P.E.; Wood, J.P.; Ferrel, J.P.; Bonesho, C.E.; Mast, A.E.
Caveolae optimize tissue factor-Factor VIIa inhibitory activity of cell-surface-associated tissue factor pathway inhibitor
Biochem. J.
443
259-266
2012
Homo sapiens
Manually annotated by BRENDA team
Andersen, L.M.; Andreasen, P.A.; Svendsen, I.; Keemink, J.; ?stergaard, H.; Persson, E.
Antibody-induced enhancement of factor VIIa activity through distinct allosteric pathways
J. Biol. Chem.
287
8994-9001
2012
Homo sapiens
Manually annotated by BRENDA team
Eriksson, O.; Ramstroem, M.; Hoernaeus, K.; Bergquist, J.; Mokhtari, D.; Siegbahn, A.
The Eph tyrosine kinase receptors EphB2 and EphA2 are novel proteolytic substrates of tissue factor/coagulation factor VIIa
J. Biol. Chem.
289
32379-32391
2014
Homo sapiens
Manually annotated by BRENDA team
Vadivel, K.; Agah, S.; Messer, A.S.; Cascio, D.; Bajaj, M.S.; Krishnaswamy, S.; Esmon, C.T.; Padmanabhan, K.; Bajaj, S.P.
Structural and functional studies of gamma-carboxyglutamic acid domains of factor VIIa and activated protein C: role of magnesium at physiological calcium
J. Mol. Biol.
425
1961-1981
2013
Homo sapiens (P08709)
Manually annotated by BRENDA team
Vatsyayan, R.; Kothari, H.; Mackman, N.; Pendurthi, U.R.; Rao, L.V.
Inactivation of factor VIIa by antithrombin in vitro, ex vivo and in vivo: role of tissue factor and endothelial cell protein C receptor
PLoS ONE
9
e103505
2014
Homo sapiens
Manually annotated by BRENDA team
Aberg, M.; Eriksson, O.; Mokhtari, D.; Siegbahn, A.
Tissue factor/factor VIIa induces cell survival and gene transcription by transactivation of the insulin-like growth factor 1 receptor
Thromb. Haemost.
111
748-760
2014
Homo sapiens
Manually annotated by BRENDA team
Sheffield, W.P.; Bhakta, V.
The M358R variant of alpha1-proteinase inhibitor inhibits coagulation factor VIIa
Biochem. Biophys. Res. Commun.
470
710-713
2016
Homo sapiens
Manually annotated by BRENDA team
Gajsiewicz, J.M.; Nuzzio, K.M.; Rienstra, C.M.; Morrissey, J.H.
Tissue factor residues that modulate magnesium-dependent rate enhancements of the tissue factor/factor VIIa complex
Biochemistry
54
4665-4671
2015
Homo sapiens
Manually annotated by BRENDA team
Sorensen, A.B.; Madsen, J.J.; Frimurer, T.M.; Overgaard, M.T.; Gandhi, P.S.; Persson, E.; Olsen, O.H.
Allostery in coagulation factor VIIa revealed by ensemble refinement of crystallographic structures
Biophys. J.
116
1823-1835
2019
Homo sapiens (P08709)
Manually annotated by BRENDA team
Eriksson, O.; Thulin, A.; Asplund, A.; Hegde, G.; Navani, S.; Siegbahn, A.
Cross-talk between the tissue factor/coagulation factor VIIa complex and the tyrosine kinase receptor EphA2 in cancer
BMC Cancer
16
341
2016
Homo sapiens
Manually annotated by BRENDA team
Sorensen, A.B.; Madsen, J.J.; Svensson, L.A.; Pedersen, A.A.; Ostergaard, H.; Overgaard, M.T.; Olsen, O.H.; Gandhi, P.S.
Molecular basis of enhanced activity in factor VIIa-trypsin variants conveys insights into tissue factor-mediated allosteric regulation of factor VIIa activity
J. Biol. Chem.
291
4671-4683
2016
Homo sapiens (P08709)
Manually annotated by BRENDA team
Prasad, R.; Sen, P.
Structural modulation of factor VIIa by full-length tissue factor (TF1-263) implication of novel interactions between EGF2 domain and TF
J. Biomol. Struct. Dyn.
36
621-633
2018
Homo sapiens (P08709)
Manually annotated by BRENDA team
Priestley, E.S.; Cheney, D.L.; DeLucca, I.; Wei, A.; Luettgen, J.M.; Rendina, A.R.; Wong, P.C.; Wexler, R.R.
Structure-based design of macrocyclic coagulation factor VIIa inhibitors
J. Med. Chem.
58
6225-6236
2015
Homo sapiens
Manually annotated by BRENDA team
Zhang, X.; Glunz, P.W.; Johnson, J.A.; Jiang, W.; Jacutin-Porte, S.; Ladziata, V.; Zou, Y.; Phillips, M.S.; Wurtz, N.R.; Parkhurst, B.; Rendina, A.R.; Harper, T.M.; Cheney, D.L.; Luettgen, J.M.; Wong, P.C.; Seiffert, D.; Wexler, R.R.; Priestley, E.S.
Discovery of a highly potent, selective, and orally bioavailable macrocyclic inhibitor of blood coagulation factor VIIa-tissue factor complex
J. Med. Chem.
59
7125-7137
2016
Homo sapiens
Manually annotated by BRENDA team
Rothmeier, A.S.; Versteeg, H.H.; Ruf, W.
Factor VIIa-induced interaction with integrin controls the release of tissue factor on extracellular vesicles from endothelial cells
J. Thromb. Haemost.
17
627-634
2019
Homo sapiens
Manually annotated by BRENDA team
Prasad, R.; Sen, P.
Molecular determinants involved in differential behaviour between soluble tissue factor and full-length tissue factor towards factor VIIa
Phys. Chem. Chem. Phys.
19
22230-22242
2017
Homo sapiens
Manually annotated by BRENDA team
Gajsiewicz, J.M.; Morrissey, J.H.
Structure-function relationship of the interaction between tissue factor and factor VIIa
Semin. Thromb. Hemost.
41
682-690
2015
Homo sapiens
Manually annotated by BRENDA team
D'Alessandro, E.; Posma, J.J.N.; Spronk, H.M.H.; Ten Cate, H.
Tissue factor ( Factor VIIa) in the heart and vasculature More than an envelope
Thromb. Res.
168
130-137
2018
Homo sapiens
Manually annotated by BRENDA team