Any feedback?
Information on EC 3.4.21.21 - coagulation factor VIIa
for references in articles please use BRENDA:EC3.4.21.21Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.21.21 coagulation factor VIIaSpecify your search results
Word Map
- 3.4.21.21
- bleeding
- fibrinogen
- platelet
- viii
-
hemostatic
- hemorrhage
- thrombosis
-
anticoagulant
- thromboplastin
- plasminogen
- haemophilia
- antithrombin
- coagulopathy
- coronary
-
transfusion
- willebrand
-
thromboembolic
- trauma
- fibrin
-
fibrinolysis
-
haemostasis
-
d-dimers
-
antithrombotic
- warfarin
-
hypercoagulable
-
intravascular
- pai-1
-
off-label
-
perioperative
- hematoma
-
k-dependent
-
amidolytic
-
thrombogenic
-
antifibrinolytic
-
tranexamic
-
prothrombotic
-
thrombin-antithrombin
-
plasma-derived
- drug development
- prothrombinase
- epistaxis
- fondaparinux
- desmopressin
-
cryoprecipitate
-
thromboelastometry
- dabigatran
- biotechnology
-
gamma-carboxyglutamic
- menorrhagia
- apixaban
-
thromboelastography
-
bethesda
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
factor vii, rfviia, fvii, fviia, factor viia, activated factor vii, recombinant factor viia, coagulation factor vii, fviic, novoseven, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
activated blood coagulation factor VII
-
-
-
-
activated factor VII
blood-coagulation factor VII, activated
-
-
-
-
blood-coagulation factor VIIa
-
-
-
-
coagulation factor VII
Eptacog alfa
-
-
-
-
Factor VII
factor VIIa
FVII
FVIIa
Serum prothrombin conversion accelerator
-
-
-
-
tissue factor/factor VIIa
additional information
-
the enzyme is a member of the trypsin family of serine proteases
factor VIIa
-
-
FVIIa
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Selective cleavage of Arg-/-Ile bond in factor X to form factor Xa
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
Phosphorylation
-
phosphorylation of signal transducers and activators of transcription
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
65312-43-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzoyl-Ile-Glu-gamma-methoxyglutamyl-Gly-Arg-p-nitroanilide + H2O
benzoyl-Ile-Glu-gamma-methoxyglutamyl-Gly-Arg + p-nitroaniline
-
i.e. S2222, 2% of the activity with N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide, plasma-derived wild-type enzyme
-
-
?
benzyloxycarbonyl-Arg-p-nitrobenzyl ester + H2O
benzyloxycarbonyl-Arg + 4-nitrophenyl
-
-
-
-
?
benzyloxycarbonyl-D-Arg-Gly-Arg + H2O
?
-
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
?
-
chromogenic S-2765
-
-
?
benzyloxycarbonyl-D-arginyl-D-glycyl-D-arginine-p-nitroanilide + H2O
p-nitroaniline + benzyloxycarbonyl-D-arginyl-D-glycyl-D-arginine
-
-
-
-
?
benzyloxycarbonyl-D-arginyl-glycyl-arginine-p-nitroanilide + H2O
benzyloxycarbonyl-D-arginyl-glycyl-arginine + p-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-D-arginyl-glycyl-L-arginyl-p-nitroanilide + H2O
benzyloxycarbonyl-D-arginyl-glycyl-L-arginine + p-nitroaniline
-
-
-
-
?
Chromozym tissue plasminogen activator + H2O
?
-
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
-
-
-
-
?
D-isoleucyl-L-prolyl-L-arginine-p-nitroanilide + H2O
D-isoleucyl-L-prolyl-L-arginine + p-nitroaniline
-
-
-
-
?
D-phenylalanyl-L-pipecolyl-L-arginine-p-nitroanilide + H2O
D-phenylalanyl-L-pipecolyl-L-arginine + p-nitroaniline
-
-
-
-
?
D-Pro-Phe-Arg-p-nitroanilide + H2O
D-Pro-Phe-Arg + p-nitroaniline
-
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
?
-
cleavage site at the Arg159-His160 bond
-
-
?
Eph tyrosine kinase receptor EphB2 + H2O
?
-
cleavage site at the Arg159-His160 bond
-
-
?
factor VIII + H2O
factor VIIIa + ?
-
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
-
-
?
H-D-isoleucyl-L-prolyl-arginine-p-nitroanilide + H2O
H-D-isoleucyl-L-prolyl-arginine + p-nitroaniline
-
i.e. S-2288
-
-
?
methanesulfonyl-D-cyclohexylalanyl-butyl-arginine p-nitroanilide + H2O
methanesulfonyl-D-cyclohexylalanyl-butyl-arginine + p-nitroaniline
-
-
-
-
?
N-acetyl-Ala-P3-P2-Lys-7-amido-4-carbamoylmethylcoumarin + H2O
?
-
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
-
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-4-nitroanilide + H2O
N-methylsulfonyl-D-Phe-Gly-Arg + 4-nitroaniline
-
-
-
?
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide + H2O
N-methylsulfonyl-D-Phe-Gly-Arg + p-nitroaniline
N-methylsulfonyl-D-phenyl-D-glycyl-D-arginyl-4-nitroanilide + H2O
N-methylsulfonyl-D-phenyl-D-glycyl-D-arginine + 4-nitroaniline
-
-
-
?
pyroglutamyl-Gly-Arg-p-nitroanilide + H2O
pyroglutamyl-Gly-Arg + p-nitroaniline
-
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
-
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
-
i.e. S2366, 38% of the activity with N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide, plasma-derived wild-type enzyme
-
-
?
signal transducer and activator of transcription 5 + ?
activated signal transducer and activator of transcription 5 + ?
-
STAT5
-
-
?
Z-D-arginyl-glycyl-arginine-p-nitroanilide + H2O
Z-D-arginyl-glycyl-arginine + p-nitroaniline
-
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
chromogenic substrate S-2288
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
S-2288
-
-
?
D-Ile-Pro-Arg-p-nitroanilide + H2O
D-Ile-Pro-Arg + p-nitroaniline
-
i.e. S2288
-
-
?
D-Ile-Pro-Arg-p-nitroanilide + H2O
D-Ile-Pro-Arg + p-nitroaniline
-
i.e. S2288, 68% of the activity with N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide, plasma-derived wild-type enzyme
-
-
?
D-Phe-pipecolyl-Arg-p-nitroanilide + H2O
D-Phe-pipecolyl-Arg + p-nitroaniline
-
-
-
-
?
D-Phe-pipecolyl-Arg-p-nitroanilide + H2O
D-Phe-pipecolyl-Arg + p-nitroaniline
-
i.e. S2238, 34% of the activity with N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide, plasma-derived wild-type enzyme
-
-
?
factor X + H2O
activated factor X + ?
-
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
-
-
-
-
?
Factor X + H2O
Factor Xa + ?
-
-
683347, 683477, 683855, 717385, 731271, 732085, 752660, 752758, 753091, 754519, 755008, 755547, 755589
-
-
?
Factor X + H2O
Factor Xa + ?
-
the enzyme is involved in the coagulation cascade, pathways, overview
-
-
?
Factor X + H2O
Factor Xa + ?
-
FX cleavage site Asn-Leu-Thr-Ar-/-Ile-Val-Gly-Gly
-
-
?
Factor X + H2O
Factor Xa + ?
-
macromolecular substrate interactions at exosites, sites within the FVIIa-TF complex distant from the active site of FVIIa, determine affinity and specificity in the productive recognition of FX
-
-
?
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide + H2O
N-methylsulfonyl-D-Phe-Gly-Arg + p-nitroaniline
-
-
-
-
?
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide + H2O
N-methylsulfonyl-D-Phe-Gly-Arg + p-nitroaniline
-
i.e. chromozym t-PA
-
-
?
protease-activated receptor 2 + H2O
?
-
protease-activated receptor 2 is cleaved by FVIIa in the binary tissue factor-FVIIa complex
-
-
?
thrombinogen + H2O
thrombin + ?
-
antifibrinolytic effect of the enzyme in relation to the activity of thrombin, regulation, overview
-
-
?
additional information
?
-
-
factor VIIa initiates the coagulation pathway upon complex formation with its cellular receptor and cofactor tissue factor
-
-
?
additional information
?
-
-
blood coagulation is initiated when tissue factor binds to coagulation factor VII to give an enzymatically active complex which then activates factors IX and X, leading to thrombin generation and clot formation
-
-
?
additional information
?
-
the enzyme plays a key role in the blood coagulation cascade
-
-
?
additional information
?
-
-
the enzyme plays a key role in the blood coagulation cascade
-
-
?
additional information
?
-
-
cell-surface tissue factor TF binds the serine protease factor VIIa to activate coagulation or, alternatively, to trigger signaling through the G protein-coupled, protease-activated receptor 2 relevant to inflammation and angiogenesis, TF-VIIa-mediated coagulation and cell signaling involve distinct cellular pools of TF, regulation, overview
-
-
?
additional information
?
-
-
membrane binding constitutes a key process in enzymatic activation of various blood coagulation factors
-
-
?
additional information
?
-
-
a loop of factor VIIa influences the macromolecular substrate specificity, overview
-
-
?
additional information
?
-
-
structure-function relationship, the enzyme forms a complex with the cell surface receptor tissue factor TF required for attaining its catalytically competent conformation, Asp338 is a catalytically important residue
-
-
?
additional information
?
-
-
substrate and cleavage site specificity with 7-amino-4-carbamoylmethylcoumarin-linked tetrapeptides, specificity profiling of the recombinant enzyme, overview
-
-
?
additional information
?
-
complex formation with the essential protein cofactor tissue factor
-
-
?
additional information
?
-
-
enzyme blood coagulation activity is regulated in the circadian clock machinery, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Eph tyrosine kinase receptor EphA2 + H2O
?
-
cleavage site at the Arg159-His160 bond
-
-
?
Eph tyrosine kinase receptor EphB2 + H2O
?
-
cleavage site at the Arg159-His160 bond
-
-
?
factor VIII + H2O
factor VIIIa + ?
-
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 + ?
-
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 + ?
-
-
-
-
?
Factor X + H2O
Factor Xa + ?
-
the enzyme is involved in the coagulation cascade, pathways, overview
-
-
?
protease-activated receptor 2 + H2O
?
-
protease-activated receptor 2 is cleaved by FVIIa in the binary tissue factor-FVIIa complex
-
-
?
thrombinogen + H2O
thrombin + ?
-
antifibrinolytic effect of the enzyme in relation to the activity of thrombin, regulation, overview
-
-
?
additional information
?
-
-
factor VIIa initiates the coagulation pathway upon complex formation with its cellular receptor and cofactor tissue factor
-
-
?
additional information
?
-
-
blood coagulation is initiated when tissue factor binds to coagulation factor VII to give an enzymatically active complex which then activates factors IX and X, leading to thrombin generation and clot formation
-
-
?
additional information
?
-
the enzyme plays a key role in the blood coagulation cascade
-
-
?
additional information
?
-
-
the enzyme plays a key role in the blood coagulation cascade
-
-
?
additional information
?
-
-
cell-surface tissue factor TF binds the serine protease factor VIIa to activate coagulation or, alternatively, to trigger signaling through the G protein-coupled, protease-activated receptor 2 relevant to inflammation and angiogenesis, TF-VIIa-mediated coagulation and cell signaling involve distinct cellular pools of TF, regulation, overview
-
-
?
additional information
?
-
-
membrane binding constitutes a key process in enzymatic activation of various blood coagulation factors
-
-
?
additional information
?
-
complex formation with the essential protein cofactor tissue factor
-
-
?
additional information
?
-
-
enzyme blood coagulation activity is regulated in the circadian clock machinery, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
complex formation with the essential protein cofactor tissue factor
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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
Ca2+
bound to the backbone-carbonyl groups of Asp72 and Glu75, and to the side-chain carboxylate groups of Glu70 and Glu80
Ca2+
-
dependent on, eight Ca2+ are bound via the Gla domain and involved in enzyme binding to the membrane with different tasks, structure and coordination, mechanism of Ca2+-mediated binding, overview
Ca2+
-
one FVIIa molecule binds 8 Ca2+ in the epidermal growth factor-like and the gamma-carboxyglutamic acid-rich domains
Ca2+
Ca2+ ions constitute an important cofactor for FVIIa and bind to a total of nine sites, seven in the N-terminal gamma-carboxyglutamic acid (Gla) domain and one each in the first EGF-like and protease domains
Ca2+
-
the enzyme binds the phospholipid membrane in a Ca2+-dependent manner. Ca2+ ions are required for assembly and function of the tissue factor-enzyme complex
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
-
-
([5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]methyl)propanedioic acid
-
-
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-([5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-5'-fluoro-2',6-dihydroxybiphenyl-3-yl]methyl)butanedioic acid
-
-
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-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-5'-fluoro-2',6-dihydroxybiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]butanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]pentanedioic acid
-
-
2-[5-(5-carbamimidoyl-1H-indol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]butanedioic acid
-
-
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-(3-[(R)-2-[(S)-1-(4-carbamimidoyl-benzylcarbamoyl)-3-carbamoylpropylcarbamoyl]-2-ethanesulfonylamino-ethyl]-1H-indol-5-yloxymethyl)-benzoic acid
-
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
3-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]pentanedioic acid
-
-
3-[5-(5-carbamimidoyl-1H-indol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]pentanedioic acid
-
-
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-[5-(4-fluorophenyl)-2-[4-(methylsulfonyl)phenyl]-1H-imidazol-4-yl]pyridine
-
-
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
-
6-dimethylamino-2-(3-phenyl-2-phenylmethanesulfonylamino-propionylamino)-hexanoic acid [4-guanidino-1-(thiazole-2-carbonyl)-butyl]-amide
-
IC50: 0.00282 mM, reversible, covalent
Bovine pancreatic trypsin inhibitor
-
mutant enzyme K192E is poorly inhibited, mutant enzyme K192Q is inhibited more than the wild-type enzyme
-
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
-
-
dimeric active site-inhibited blood clotting factor VIIa
-
dimeric fVIIai, 16000fold inhibitory effect
-
FFR-FVIIa
-
derivate of FVIIa with a stably buried N-terminus representing the active conformation of FVIIa, IC50: 0.019 mM
-
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-(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
-
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
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
V154G-FVIIa
-
derivate of FVIIa with a fully exposed N-terminus representing the zymogen-like conformation of FVIIa, IC50: 0.014 mM
-
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
-
-
[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-5'-fluoro-2',6-dihydroxybiphenyl-3-yl]acetic acid
-
-
[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]acetic acid
-
-
[5-(5-carbamimidoyl-1H-indol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]acetic acid
-
-
antithrombin
-
in presence of heparin, 20% loss of activity of wild-type enzyme after 15 min, 59% loss of activity of the K337A mutant enzyme after 15 min, 77% loss of activity of the L305V/K337A mutant enzyme after 15 min, 78% loss of activity of the V158D/D296V/M298Q mutant enzyme after 15 min, 87% loss of activity of the V158D/D296V/M298Q/K337A mutant enzyme after 15 min, 91% loss of activity of the V158D/D296V/M298Q/L305V/K337A mutant enzyme after 15 min, 53% loss of activity of the M298Q mutant enzyme after 15 min
-
antithrombin
-
0.1 mg/ml in the presence of 1 unit/ml heparin, less than 10% residual activity after 15min incubation with enzyme FVIIa-sTF
-
antithrombin
-
can inhibit factor VIIa effectively only when it is bound to tissue factor
-
EEWEVLCWTWETCER
-
IC50: 1.6 nM, partial hyperbolic mixed-type inhibitor of factor X activation, partial competitive inhibitor of amidolytic activity. Inhibits activation of factor X and factor IX and amidolytic activity of Chromozym t-PA with IC50 values of 1.6 nM, 3.5 nM and 8.5 nM
tissue factor pathway inhibitor
-
no inhibition of the mutant enzymes K192E and K192Q
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
phospholipid vesicle
-
oleoyl-1,2-diacyl-sn-glycero-3-phosphocholine and dioleoyl-1,2-diacyl-sn-glycero-3-(phospho-L-serine)
-
tissue factor TF
-
TF-induced allosteric activation of FVIIa, binding structure, overview
-
tissue factor
-
factor VIIa remains in a zymogen-like state following proteolytic activation and depends on interactions with the cofactor tissue factor for function. Val21, Glu154 and Met156 cooperate to stabilize the conformation of the enzyme and to enhance the affinity for tissue factor
-
tissue factor
-
the enzyme initiates blood clotting after interacting with its cofactor tissue factor. Soluble tissue factor concentrations of 5.0 nM and 22.4 nM for the activated wild-type factor VII and for the mutant form A294V of the activated wild-type factor yield an activity of 50% towards spectrozyme fVIIa
-
tissue factor
-
tissue factor binding to factor VIIa allosterically augments the enzymatic activity of factor VIIa towards macromolecular substrates and small peptidyl substrates. Tissue factor binding to factor VIIa alters the chemical environment of the active site of factor VIIa by protecting Ile153 from deprotonation in the free enzyme while deprotecting the catalytic triad as a whole when in the Michaelis complex
-
tissue factor
-
cell-surface tissue factor TF binds the serine protease factor VIIa to activate coagulation or, alternatively, to trigger signaling through the G protein-coupled, protease-activated receptor 2 relevant to inflammation and angiogenesis, extracellular Cys186-Cys209 disulfide bond of TF is critical for coagulation, overview, mutant TF C209A with an unpaired Cys186 retains TF-VIIa signaling activity, and it has reduced affinity for VIIa, regulation, overview
-
tissue factor
-
required to attain full catalytic competency and to initiate blood coagulation, mechanism of TF allosterical activation of FVIIa, structural dynamics approach that combines molecular dynamics simulations and hydrogen/deuterium exchange mass spectrometry on free and TF-bound FVIIa, TF structures involved are activation loop 3 residues 365-374/216-225 of the so-called activation domain and the 170-loop residues 313-322/170A-175, overview
-
tissue factor
-
formation of a complex between factor VIIa and tissue factor is necessary to enhance the procoagulant activity of factor VIIa, not only by providing membrane localization, substrate exosites and positioning the active site at an appropriate distance above the surface but also by allosteric enhancement of the enzymatic activity, and this event signals initiation of blood coagulation
-
tissue factor
-
in the absence of its cofactor tissue factor, coagulation factor VIIa predominantly exists in a zymogen-like, catalytically incompetent state
-
tissue factor
-
binding of tissue factor with factor FVIIa only partially enhances the enzyme's proteolytic activity. Soluble tissue factor has a lower binding capacity with the enzyme compared to membrane bound full-length tissue factor
-
tissue factor
-
tissue factor allosterically activates factor VIIa by several mechanisms such as active site positioning, spatial stabilization, and direct interactions with the substrate
-
additional information
-
enzyme activation involves residue 343, mechanisms, overview
-
additional information
-
the relative catalytic efficiency is increased 170 and 150fold in the presence of saturating amounts of monoclonal antibodies F36 and F37, respectively
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.67
methanesulfonyl-D-cyclohexylalanyl-butyl-arginine p-nitroanilide
-
wild-type enzyme
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
1.2
D-Ile-Pro-Arg-4-nitroanilide
wild type enzyme, in the presence of soluble tissue factor (1-219), at pH 7.4 and 25°C
1.8
D-Ile-Pro-Arg-4-nitroanilide
wild-type FVIIa + soluble tissue factor for induced allosteric activation of factor VIIa
7.1
D-Ile-Pro-Arg-4-nitroanilide
mutant G372A + soluble tissue factor for induced allosteric activation of factor VIIa, pH 7.4
8.9
D-Ile-Pro-Arg-4-nitroanilide
wild type enzyme, in the absence of soluble tissue factor (1-219), at pH 7.4 and 25°C
1.25
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, plasma derived wild-type enzyme, activated by tissue factor
1.43
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, activated wild-type enzyme, activated by tissue factor
1.53
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, mutant enzyme DELTA360-329, without tissue factor
1.73
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, mutant enzyme which has all of the residues of the loop formed by a disulfide bond between Cys310 and Cys329 replaced with those of trypsin, activated by tissue factor
2.22
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, activated wild-type enzyme, without tissue factor
2.82
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, plasma derived wild-type enzyme, without tissue factor
2.98
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, mutant enzyme DELTA360-329, activated by tissue factor
3.06
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, mutant enzyme which has all of the residues of the loop formed by a disulfide bond between Cys310 and Cys329 replaced with those of trypsin, without tissue factor
0.000012
Factor X
mutant G372A + lipidated tissue factor for induced allosteric activation of factor VIIa, pH 7.4
-
0.000015
Factor X
wild-type FVIIa + lipidated tissue factor for induced allosteric activation of factor VIIa, pH 7.4
-
0.000043
Factor X
-
mutant enzyme L144A, tissue factor/phosphatidylcholine-phosphatidylserine vesicles
-
0.000051
Factor X
-
mutant enzyme L192A, tissue factor/phosphatidylcholine-phosphatidylserine vesicles
-
0.000059
Factor X
-
mutant enzyme E154A, tissue factor/phosphatidylcholine-phosphatidylserine vesicles
-
0.000069
Factor X
-
wild-type enzyme VIIa, tissue factor/phosphatidylcholine-phosphatidylserine vesicles
-
0.0019
Factor X
wild-type FVIIa + soluble tissue factor for induced allosteric activation of factor VIIa, pH 7.4
-
0.0032
Factor X
mutant G372A + soluble tissue factor for induced allosteric activation of factor VIIa, pH 7.4
-
0.0054
Factor X
-
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
-
0.0124
Factor X
-
wild-type enzyme VIIa, tissue factor/phosphatidylcholine vesicles
-
0.0153
Factor X
-
mutant enzyme K192A, tissue factor/phosphatidylcholine vesicles
-
0.0207
Factor X
-
mutant enzyme L144A, tissue factor/phosphatidylcholine vesicles
-
1.5
H-D-isoleucyl-L-prolyl-arginine-p-nitroanilide
-
wild type enzyme, in the presence of tissue factor, pH 7.4
2
H-D-isoleucyl-L-prolyl-arginine-p-nitroanilide
-
mutant enzyme L280I/V299M-FVIIa, in the presence of tissue factor, pH 7.4
2.2
H-D-isoleucyl-L-prolyl-arginine-p-nitroanilide
-
mutant enzyme C164V/V299C FVIIa, in the presence of tissue factor, pH 7.4
2.3
H-D-isoleucyl-L-prolyl-arginine-p-nitroanilide
-
mutant enzyme V299M-FVIIa, in the presence of tissue factor, pH 7.4
6.6
H-D-isoleucyl-L-prolyl-arginine-p-nitroanilide
-
mutant enzyme L280I/V299M-FVIIa, pH 7.4
9.2
H-D-isoleucyl-L-prolyl-arginine-p-nitroanilide
-
mutant enzyme C164V/V299C, pH 7.4
9.8
H-D-isoleucyl-L-prolyl-arginine-p-nitroanilide
-
mutant enzyme V299M-FVIIa, pH 7.4
0.8
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, wild-type enzyme, with addition of tissue factor
0.9
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, mutant enzyme V21N/E154I/M156Q, with addition of tissue factor
1.1
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, 37°C, wild-type enzyme, addition of tissue factor
1.2
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, 37°C, mutant enzyme M156Q, addition of tissue factor
2.2
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 6.5, MTE buffer, without tissue factor
2.3
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 6.5, MES buffer, without tissue factor
3.1
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, mutant enzyme V21N/E154I/M156Q, without tissue factor
5.3
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, 37°C, mutant enzyme M156Q
5.5
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, wild-type enzyme, without tissue factor
6.3
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 7.5, Tris buffer, without tissue factor
6.4
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 9.5, BTP buffer, without tissue factor
6.8
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 9.5, ethanolamine buffer, without tissue factor
8
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 7.5, HEPES buffer, without tissue factor
10
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 7.5, MTE buffer, without tissue factor
13
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 9.5, MTE buffer, without tissue factor
50
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 9.5, veronal buffer, without tissue factor
additional information
additional information
-
the KM-value for spectrozyme fVIIa for the mutant enzyme A294V is above 2.5 mM
-
additional information
additional information
-
the ratio of turnover number to KM-value for the substrate methanesulfonyl-D-cyclohexylalanyl-butyl-arginine p-nitroanilide is 25000 for wild-type enzyme, 500 for mutant enzyme V154G and 2500 for mutant enzyme V154A
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes with different substrates, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17
methanesulfonyl-D-cyclohexylalanyl-butyl-arginine p-nitroanilide
-
wild-type enzyme
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
7.7
D-Ile-Pro-Arg-4-nitroanilide
wild type enzyme, in the absence of soluble tissue factor (1-219), at pH 7.4 and 25°C
34.6
D-Ile-Pro-Arg-4-nitroanilide
wild type enzyme, in the presence of soluble tissue factor (1-219), at pH 7.4 and 25°C
0.59
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, mutant enzyme DELTA360-329, without tissue factor
1.95
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, activated wild-type enzyme, without tissue factor
3.29
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, plasma derived wild-type enzyme, without tissue factor
7.81
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, mutant enzyme DELTA360-329, activated by tissue factor
18.53
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, mutant enzyme which has all of the residues of the loop formed by a disulfide bond between Cys310 and Cys329 replaced with those of trypsin, without tissue factor
20.98
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, mutant enzyme which has all of the residues of the loop formed by a disulfide bond between Cys310 and Cys329 replaced with those of trypsin, activated by tissue factor
37.08
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, activated wild-type enzyme, activated by tissue factor
44.2
D-Ile-Pro-Arg-p-nitroanilide
-
pH 8.0, 30°C, plasma derived wild-type enzyme, activated by tissue factor
0.00001
Factor X
-
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
-
0.00062
Factor X
mutant G372A + soluble tissue factor for induced allosteric activation of factor VIIa, pH 7.4
-
0.0021
Factor X
mutant G372A + lipidated tissue factor for induced allosteric activation of factor VIIa, pH 7.4
-
0.0027
Factor X
wild-type FVIIa + soluble tissue factor for induced allosteric activation of factor VIIa, pH 7.4
-
0.004
Factor X
wild-type FVIIa + lipidated tissue factor for induced allosteric activation of factor VIIa, pH 7.4
-
0.05
Factor X
-
mutant enzyme L144A, tissue factor/phosphatidylcholine vesicles
-
0.15
Factor X
-
mutant enzyme L192A or E154A, tissue factor/phosphatidylcholine vesicles
-
0.15
Factor X
-
mutant enzyme L144A, tissue factor/phosphatidylcholine-phosphatidylserine vesicles
-
0.8
Factor X
-
mutant enzyme K192A, tissue factor/phosphatidylcholine-phosphatidylserine vesicles
-
1.25
Factor X
-
mutant enzyme E154A, tissue factor/phosphatidylcholine-phosphatidylserine vesicles
-
1.55
Factor X
-
wild-type enzyme VIIa, tissue factor/phosphatidylcholine vesicles
-
7.4
Factor X
-
wild-type enzyme VIIa, tissue factor/phosphatidylcholine-phosphatidylserine vesicles
-
8.4
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, wild-type enzyme, without tissue factor
12.1
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, 37°C, wild-type enzyme
24.6
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, 37°C, mutant enzyme M156Q
32.2
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, mutant enzyme V21N/E154I/M156Q, without tissue factor
37.2
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, wild-type enzyme, with addition of tissue factor
47
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, mutant enzyme V21N/E154I/M156Q, with addition of tissue factor
49.1
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, 37°C, wild-type enzyme, addition of tissue factor
49.8
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, 37°C, mutant enzyme M156Q, addition of tissue factor
1500
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 6.5, MTE buffer, without tissue factor
1560
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 6.5, MES buffer, without tissue factor
5940
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 9.5, BTP buffer, without tissue factor
7200
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 9.5, ethanolamine buffer, without tissue factor
9600
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 9.5, MTE buffer, without tissue factor
31800
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 7.5, Tris buffer, without tissue factor
33600
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 7.5, HEPES buffer, without tissue factor
38400
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 7.5, MTE buffer, without tissue factor
84000
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 9.5, veronal buffer, without tissue factor
96000
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 6.5, MES buffer, in presence of tissue factor
96000
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 6.5, MTE buffer, in presence of tissue factor
198000
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 7.5, HEPES buffer, in presence of tissue factor
216000
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 7.5, MTE buffer, in presence of tissue factor
246000
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 7.5, Tris buffer, in presence of tissue factor
324000
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 9.5, veronal buffer, in presence of tissue factor
360000
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 9.5, MTE buffer, in presence of tissue factor
366000
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 9.5, BTP buffer, in presence of tissue factor
396000
N-methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 9.5, ethanolamine buffer, in presence of tissue factor
additional information
additional information
-
turnover-number of wild-type and mutant enzymes
-
additional information
additional information
-
the ratio of turnover number to KM-value for the substrate methanesulfonyl-D-cyclohexylalanyl-butyl-arginine p-nitroanilide is 25000 for wild-type enzyme, 500 for mutant enzyme V154G and 2500 for mutant enzyme V154A
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.9
D-Ile-Pro-Arg-4-nitroanilide
wild type enzyme, in the absence of soluble tissue factor (1-219), at pH 7.4 and 25°C
28
D-Ile-Pro-Arg-4-nitroanilide
wild type enzyme, in the presence of soluble tissue factor (1-219), at pH 7.4 and 25°C
0.19
Factor X
mutant G372A + soluble tissue factor for induced allosteric activation of factor VIIa, pH 7.4
-
1.4
Factor X
wild-type FVIIa + soluble tissue factor for induced allosteric activation of factor VIIa, pH 7.4
-
180
Factor X
mutant G372A + lipidated tissue factor for induced allosteric activation of factor VIIa, pH 7.4
-
270
Factor X
wild-type FVIIa + lipidated tissue factor for induced allosteric activation of factor VIIa
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.000021
([5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]methyl)propanedioic acid
-
-
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
0.000004
2-([5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-5'-fluoro-2',6-dihydroxybiphenyl-3-yl]methyl)butanedioic acid
-
-
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
0.000004
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-5'-fluoro-2',6-dihydroxybiphenyl-3-yl]butanedioic acid
-
-
0.000022
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]butanedioic acid
-
-
0.000017
2-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]pentanedioic acid
-
-
0.000001
2-[5-(5-carbamimidoyl-1H-indol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]butanedioic acid
-
-
0.000036
3-[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]pentanedioic acid
-
-
0.000013
3-[5-(5-carbamimidoyl-1H-indol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]pentanedioic acid
-
-
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
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
0.0000087
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
0.00000035
R-4-[2-(3-aminobenzenesulfonylamino)-1-(3,5-diethoxy-2-fluorophenyl)-2-oxoethylamino]-2-hydroxy-benzamidine
-
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
0.000002
[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-5'-fluoro-2',6-dihydroxybiphenyl-3-yl]acetic acid
-
-
0.000015
[5-(5-carbamimidoyl-1H-benzimidazol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]acetic acid
-
-
0.000003
[5-(5-carbamimidoyl-1H-indol-2-yl)-6-hydroxy-3'-nitrobiphenyl-3-yl]acetic acid
-
-
0.0000052
(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
-
pH and temperature not specified in the publication
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
-
pH and temperature not specified in the publication
0.018
(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
-
Ki above 0.018 mM, pH and temperature not specified in the publication
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
-
pH and temperature not specified in the publication
0.0046
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
-
pH and temperature not specified in the publication
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
-
pH and temperature not specified in the publication
0.0493
4-aminobenzamidine
wild type enzyme, in the presence of soluble tissue factor (1-219), at pH 7.4 and 25°C
0.1
4-aminobenzamidine
wild-type + soluble tissue factor for induced allosteric activation of factor VIIa
0.7
4-aminobenzamidine
mutant G372 + soluble tissue factor for induced allosteric activation of factor VIIa
1.485
4-aminobenzamidine
wild type enzyme, in the absence of soluble tissue factor (1-219), at pH 7.4 and 25°C
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
0.116
p-aminobenzamidine
-
pH 8.0, wild-type enzyme, chromozym tPA as substrate with addition of tissue factor
0.124
p-aminobenzamidine
-
pH 8.0, mutant enzyme V21N/E154I/M156Q, chromozym tPA as substrate with addition of tissue factor
0.317
p-aminobenzamidine
-
pH 8.0, mutant enzyme V21N/E154I/M156Q, chromozym tPA as substrate without addition of tissue factor
additional information
additional information
-
because of competitive binding of p-aminobenzamidine and D-Ile-Pro-Arg-p-nitroanilide, the apparent Ki values were calculated from the p-aminobenzamidine IC50, taking into account the concentration of D-Ile-Pro-Arg-p-nitroanilide ([S]) and the Km for this substrate using Ki =IC50/(1 + [S]/Km)
-
additional information
additional information
-
inhibition kinetics of wild-type and mutant enzymes, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.000039
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
0.000118
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
0.000204
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
0.00282
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
0.0024
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
0.00000023
EEWEVLCWTWETCERGEGVEEELWEWR
Homo sapiens
-
maximal inhibition to 99%, IC50: 230 pM
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
-
0.00045
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
0.000069
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
0.0002
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
0.014
V154G-FVIIa
Homo sapiens
-
derivate of FVIIa with a fully exposed N-terminus representing the zymogen-like conformation of FVIIa, IC50: 0.014 mM
-
0.0000016
EEWEVLCWTWETCER
Homo sapiens
-
IC50: 1.6 nM, partial hyperbolic mixed-type inhibitor of factor X activation, partial competitive inhibitor of amidolytic activity. Inhibits activation of factor X and factor IX and amidolytic activity of Chromozym t-PA with IC50 values of 1.6 nM, 3.5 nM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
catalytic efficiencies of wild-type and mutant enzymes with different substrates, overview
additional information
-
enzyme activity in the circadian clock machinery, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 40
-
5°C: about 90% of maximal activity, 40°C: about 50% of maximal activity, cleavage of Ile-Pro-Arg-p-nitroanilide
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
95336, 654496, 654508, 654583, 654595, 654613, 654639, 654663, 656000, 656015, 656025, 656033, 656136, 656462, 656463, 656464, 656465
-
-
brenda
-
657181, 657312, 657378, 657386, 667430, 667474, 667584, 667588, 667668, 667680, 668158, 668259, 668304, 669415
-
-
brenda
-
669484, 670270, 670935, 683139, 683297, 683298, 683347, 683477, 683855, 683996, 684040, 684070, 692003, 692535, 695182, 707073, 707149
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
Ca2+ and the Gla domain are required for membrane binding by the enzyme, mechanism of Ca2+-mediated binding, molecular dynamics simulation of complex formation, overview
brenda
-
the major function of the enzyme's Gla domain is to attach FVIIa to membranes, i.e. to add binding energy to the interaction with membrane-associated tissue factor
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
eosinophil counts in the bronchoalveolar lavage fluid of wild-type mice increases after ovalbumin challenge, a response that is diminished in comparably challenged low-expressing coagulation factor VII (FVIItTA/tTA) mice. Levels of T helper type 2 cytokines, IL-4, IL-5, and IL-13, and eosinophil-attracting chemokines, eotaxin and RANTES, are also lower in the ovalbumin-challenged low expression factor VIIa mice. Eosinophils purified from low-FVII mice undergo apoptosis at a faster rate compared with wild-type eosinophils, and eosinophil migration in response to eotaxin is reduced in eosinophils obtained from low expressing factor VIIa mice. Airway hyperresponsiveness and mucous layer thickness are reduced in ovalbumin-treated low expressing factor VIIa mice
malfunction
-
the small nuclear RNA-U1 (U1+ 5a) mediated rescue of FVII mRNA processing impaired by the 9726 + 5G to A mutation results in an appreciable secretion of functional FVII
physiological function
-
chronic sleep deprivation in a mouse model reduces, in a reversible manner, the FVII expression levels and activity level, thus influencing the TF/FVIIa activation pathway efficiency
physiological function
-
surface plasmon resonance results show that recombinant factor VII can depress the integration of EGFP-EGF1 (fusion protein epidermal growth factor 1-enhanced green fluorescent protein) with recombinant tissue factor
physiological function
-
this study investigates the evolutionary history of F7 variation in human populations from the broader Mediterranean region and other parts of the world. Different evolutionary histories in the F7 promoter region between Mediterraneans and Amerindians are indicated
physiological function
-
following injection in mice, both hepatocytes and Kupffer cells appear to be involved in the hepatic clearance and metabolism of both full-length recombinant factor VIIa and recombinant factor VIIa in complex with at least two plasma protease inhibitors
physiological function
FVIIa in complex with tissue factor initiates the extrinsic coagulation pathway
physiological function
-
hepatocytes and Kupffer cells and possibly sinusoidal endothelial cells of the rat liver are shown to be physiologically relevant for the clearance of pharmacological doses of recombinant factor FVIIa in rats
physiological function
-
tissue factor-factor VIIa increases interleukin-8 release, decreases caspase-7 expression, enhances tissue factor expression, and suppresses the phosphorylation of p38MAPK in SW-620 cells through protease-activated receptor-2 activation thereby promoting colon cancer cell proliferation and migration
physiological function
-
factor VIIa induces cell survival and gene transcription by transactivation of the insulin-like growth factor 1 receptor. Binding of coagulation factor VIIa to ist receptor tissue factor protects cancer cells from TNF-related apoptosis inducing ligand-induced apoptosis
physiological function
-
FVIIa causes potentiation of cell repulsion by the Eph tyrosine kinase receptor EphB2 ligand ephrin-B1, demonstrating a proteolytical event to control Eph-mediated cell segregation
physiological function
-
factor VIIa-induced interaction with integrin controls the release of tissue factor on extracellular vesicles from endothelial cells. Intracellular trafficking controlled by factor FVIIa forcing interaction with integrin beta1 regulates tissue factor availability for release on procoagulant extracellular vesicles
physiological function
the complex of coagulation factor VIIa and membrane-bound tissue factor initiates blood coagulation upon vascular injury
physiological function
-
tissue factor facilitates the activation of the enzyme thereby initiating the extrinsic coagulation pathway followed by the activation of factor X and thrombin formation. The enzyme functions in blood coagulation and maintenance of the hemostatic balance in the vasculature. The tissue factor:factor VIIa complex is one of the triggers of PAR-2 activation. The tissue factor:factorVIIa pathway is also implicated in the onset of cardiac fibrosis
physiological function
-
tissue factor/coagulation factor VIIa-EphA2 cross-talk potentiates ligand-dependent EphA2 signaling in human cancers. Tissue factor and EphA2 co-localize constitutively in MDA-MB-231 cells, and addition of enzyme results in cleavage of EphA2 by a protease activated receptor 2-independent mechanism
Show AA Sequence and Transmembrane Helices (639 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46070
-
calculated from the amino acid sequence and considering 12 disulfide bridges
50000
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
Ca2+ and the Gla domain are required for membrane binding by the enzyme involving residues R9, R15, K18, R28, K32, R36, and K38, molecular dynamics simulation of complex formation, structure, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
additional information
-
FVII undergoes many posttranslational modifications such as gamma-carboxylation, N- and O-glycosylation, beta-hydroxylation
glycoprotein
-
modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans
proteolytic modification
-
the zymogen, factor VII, is composed of a single polypeptide chain possessing an amino-terminal sequence of Ala-Asn-Gly-Phe-Leu-, the zymogen contains 13% carbohydrate
proteolytic modification
-
the activated two-chain enzyme factor VIIa is formed from the single chain zymogen factor VII
proteolytic modification
-
the single chain zymogen, factor VII, is hydrolyzed by factor Xa in the presence of calcium ions and phospholipids, and by thrombin, to the two-chain form factor VIIa
proteolytic modification
-
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
proteolytic modification
-
proteolytic cleavage of the peptide bond between Arg152 and Ile153 converts the procoagulant protein factor VII to an activated two-chain form. The formation of a salt bridge between Ile153 and Asp343 drives the conversion to the active form
proteolytic modification
-
the product of the reaction with factor X, the activated factor X is also the most efficient activator of zymogen factor VII
proteolytic modification
-
zymogen FVII is converted to the activated form by proteolytic cleavage of the Arg152{15}-Ile153{16} peptide bond, zymogen factor VII is activated by thrombin
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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
N-terminally truncated factor VII, activated recombinant factor VII is crystallized in the presence of the reversible S1-site inhibitor benzamidine
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, 16.515.5% 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
-
structure of the gamma-carboxyglutamic acid-domainless human coagulation factor VIIa at a resolution of 2.8 A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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
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
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
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
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
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
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
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
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
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
K192Q
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
K337A
-
the ratio of turnover number to Km-value is 4.4fold 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
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
L144A
-
slightly increased Km-value and decreased turnover number compared to the wild-type enzyme
L144A
-
turnover-number for activation of factor X is 40fold lower than 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
M156Q
-
mutation has no influence on the amidolytic and proteolytic activity of tissue factor bound enzyme, increased affinity for tissue factor
M156Q
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
M298Q
-
the ratio of turnover number to Km-value is 6.9fold 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
M298Q
-
site-directed mutagenesis, activity and active site structure in comparison to the wild-type
M306D
-
mutation abolishes the allosteric linkage between the active site and the binding interface with tissue factor. 2fold increase in amidolytic activity. In sharp contrast to the wild-type enzyme its binding kinetic to soluble tissue factor are unaltered after inactivation with D-Phe-Phe-Arg chloromethyl ketone
M306D
-
the mutant displays barely any tissue factor-induced enhancement in amidolytic activity or active site inhibitor affinity, no increased burial of the protease domain N-terminus and only partial protection of Asn-322 from deglycosylation
additional information
-
mutant enzyme which has all of the residues of the loop formed by a disulfide bond between Cys310 and Cys329 replaced with those of trypsin has lower affinity for soluble tissue factor as compared to wild-type enzyme, 2fold smaller tissue factor-mediated acceleration of amidolytic activity compared to wild type enzyme, the catalytic efficiencies of the mutant towards various chromogenic substrates are 2-18fold greater than those of the wild-type factor VIIa. As well as the wild-type enzyme the mutant exists predominantly in the zymogen-like state
additional information
-
construction of FVIIa analogues with a stabilized activation domain and N-terminal insertion
additional information
-
beside wild-type FVII, FVII-N145/322Q without N-glycosylation sites or FVII-S52/60A without O-glycosylation sites
additional information
-
changes in the protease domain in an analog of FVIIa with increased tissue factor-independent activity, NN1731, enhances platelet binding as well as proteolytic activity (50times)
additional information
-
deficiency of coagulation Factor VII results in spontaneous cardiac fibrosis in mice, resulting in diastolic and systolic cardiac dysfunction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
factor VII
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
raised FVIIc activity levels in coronary heart disease are significantly positively correlated with insulin resistance
-
seven days of a partial sleep deprivation in a mouse model reduces significantly factor VII mRNA expression
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
drug development
medicine
medicine
-
digoxigenin ester derivatives of factor VIIa facilitate staining studies to localize tissue factor activity in human atherosclerotic plaques. The product of factor VIIa obtained at 50fold digoxigenin excess is the best choice for pathologic staining because it retains full enzyme activity together with a large number of incorporated digoxigenin units
medicine
-
the recombinant activated factor VII corrects the deficient thrombin generation seen in factor VII and factor IX deficiency, and in blood containing factor VIII inhibitors. As s consequence, platelet function is improved and clot structure is enhanced
medicine
-
recombinant FVIIa constitutes an efficient substitution therapy for treatment of patients with haemophilia A and haemophilia B which lack or have dysfunctional FVIII and FIX, respectively, pharmacological mechanism of action of FVIIa, overview
medicine
-
the enzyme is clinically used to treat hemophilia, clinical trials, overview
medicine
-
the recombinant enzyme is useful as hemostatic agent in the treatment of hemorrhage in hemophiliacs with inhibitors, and in use as hemostatic agent in severe bleeding unresponsive to standard treatment, associated with disseminated intravascular coagulation, clinical trials, mode of action, overview
medicine
-
recombinant coagulation factor VIIa is administered to control acute bleeding in a patient with Klippel-Trenaunay-Weber syndrome
medicine
-
the efficacy of recombinant factor VIIa for the reversal of anticoagulation in patients with warfarin-associated intracranial hemorrhage is described in several case reports, case series, and retrospective cohort studies. Its use may be considered for as a viable alternative treatment to standard treatment with fresh-frozen plasma. Patients should be screened for increased risk of thrombosis before administration of the drug
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
-
to assess effects of rFVIIa on survival outcomes, rFVIIa cases are matched to controls on injury severity and age. 22 battle-injured patients from the Combat Trauma Registry received rFVIIa. Over two-thirds (68%) of the rFVIIa patients survived, an identical outcome seen for a matched control group of 22 patients
medicine
-
gene-based FVIIa variants show improved hemostatic efficacy for the treatment of hemophilia. Factor VIIa variants VEAY7 and DVQ30 exhibit increased tissue factor-independent coagulant activity relative to the wild type
medicine
-
recombinant factor-activated VII has safety and potential benefit for control and prevention of hemorrhage in pediatric patients without congenital hemophilia
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.4.21.21)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
