Any feedback?
Information on EC 3.4.21.22 - coagulation factor IXa
for references in articles please use BRENDA:EC3.4.21.22Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.21.22 coagulation factor IXaSpecify your search results
Word Map
- 3.4.21.22
- hemophilia
- bleeding
- clot
- prothrombin
- thrombin
- thromboplastin
-
anticoagulant
- platelet
- thrombosis
- antithrombin
- viiia
-
x-linked
- heparin
-
adeno-associated
- fibrinogen
-
plasma-derived
- willebrand
-
prophylaxis
-
k-dependent
-
infusions
-
prophylactic
-
hemostatic
- zymogen
-
procoagulant
-
haemostasis
- fixa
-
thrombogenicity
-
gamma-carboxyglutamic
-
one-stage
- coagulopathy
-
thromboembolic
-
anti-factor
-
amidolytic
-
on-demand
-
high-purity
-
fibrinopeptide
-
d-dimer
-
thrombin-antithrombin
-
exosite
- arthropathy
- prekallikrein
-
cryoprecipitate
- medicine
-
gamma-carboxylation
- rfviia
-
bethesda
-
alloantibodies
- prothrombinase
-
thrombin-activated
- diathesis
- novoseven
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
factor ix, factor ixa, coagulation factor ix, activated factor ix, intrinsic xase, activated fix, coagulation factor ixa, factor ixabeta, activated coagulation factor ix, factor ixan, 
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 Christmas factor
-
-
-
-
activated factor IX
blood coagulation factor IXa
Christmas factor
-
-
-
-
coagulation factor IX
factor IXa
factor IXabeta
factor IXabeta'
-
converted from factor IXAalpha by alpha-chymotrypsin in the presence of Ca2+
FIXa
additional information
the enzyme is a member of the serine protease family and shares a high degree of homology with trypsin
factor IXa
-
-
-
-
factor IXa
-
-
FIXa
-
-
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
free of thrombin activity
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37316-87-3
-
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
(methylsulfonyl)-D-cyclohexylalanine-Gly-Arg-7-amido-4-methylcoumarin + H2O
(methylsulfonyl)-D-cyclohexylalanine-Gly-Arg + 7-amino-4-methylcoumarin
Pefa10
-
-
?
(methylsulfonyl)-D-cyclohexylglycine-Gly-Arg-7-amido-4-methylcoumarin + H2O
(methylsulfonyl)-D-cyclohexylglycine-Gly-Arg + 7-amino-4-methylcoumarin
Pefa9
-
-
?
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide + H2O
4-methylsulfonyl-D-Leu-Gly-Arg + p-nitroaniline
-
-
-
?
D-cyclohexylglycyl-Gly-Arg-7-amido-4-methylcoumarin + H2O
D-cyclohexylglycyl-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
D-cyclohexylglycyl-Gly-Arg-p-nitroanilide + H2O
D-cyclohexylglycyl-Gly-Arg + p-nitroaniline
-
-
-
?
D-Leu-Phe-Gly-Arg-4-nitroanilide + H2O
D-Leu-Phe-Gly-Arg + 4-nitroaniline
-
-
-
-
?
methoxycarbonyl-D-cyclohexylglycyl-glycyl-L-arginyl-p-nitroanilide + H2O
methoxycarbonyl-D-cyclohexylglycyl-glycyl-L-arginine + p-nitroaniline
-
-
-
-
?
methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide + H2O
?
-
rFIXa, ethanol, 25% v/v enhances the activity 6fold, methanol 4fold, ethylene glycol, 25-40% v/v enhances the activity up to 20fold, glycerol, 50% v/v enhances the activity 6fold
-
-
?
methylsulfonyl-D-cyclohexylglycyl-Arg-7-amido-4-methylcoumarin + H2O
methylsulfonyl-D-cyclohexylglycyl-Arg + 7-amino-4-methylcoumarin
-
assay at 37°C
-
-
?
methylsulfonyl-D-cyclohexylglycyl-Gly-Arg-p-nitroanilide + H2O
methylsulfonyl-D-cyclohexylglycyl-Gly-Arg + 4-nitroaniline
-
-
-
-
?
N-alpha-benzyloxycarbonyl-D-arginylglycyl-L-arginine-para-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-D-arginylglycyl-L-arginine + para-nitroaniline
-
-
-
?
Nalpha-benzyloxycarbonyl-D-Arg-Gly-Arg-4-nitroanilide + H2O
Nalpha-benzyloxycarbonyl-D-Arg-Gly-Arg + 4-nitroaniline
-
S-2765
-
-
?
Spectrofluor FIXa + H2O
(methylsulfonyl)-D-cyclohexylglycine-Gly-Arg + 7-amino-4-methylcoumarin
i.e. (methylsulfonyl)-D-cyclohexylglycine-Gly-Arg-7-amido-4-methylcoumarin
-
-
?
Spectrozyme t-PA + H2O
?
-
i.e. CH3SO2-D-cyclohexyl-Thr-Gly-L-Arg-4-nitroanilide
-
-
?
tert-butoxycarbonyl-Ile-Glu-Gly-Arg-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-Ile-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide + H2O
?
commercial chromogenic substrate CBS 31.39
-
-
?
CH3SO2-D-Leu-Gly-L-Arg-p-nitroanilide + H2O
CH3SO2-D-Leu-Gly-L-Arg + p-nitroaniline
-
-
-
?
CH3SO2-D-Leu-Gly-L-Arg-p-nitroanilide + H2O
CH3SO2-D-Leu-Gly-L-Arg + p-nitroaniline
-
-
-
-
?
CH3SO2-D-Leu-Gly-L-Arg-p-nitroanilide + H2O
CH3SO2-D-Leu-Gly-L-Arg + p-nitroaniline
-
-
?
factor X + H2O
?
-
gamma-carboxyglutamic acid, Gla-domains of vitamin K-dependent coagulation factors are essential for binding of phospholipid and for the activation raections such as factor X, the interaction of the Gla-domain with metal ions like Ca2+ is essential for its function
-
-
?
factor X + H2O
?
-
a chymotrypsin homologue, and one of the gamma-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor IX is activated by factor XIa
-
-
?
factor X + H2O
?
-
a chymotrypsin homologue, and one of the gamma-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor IX is activated by factor XIa
-
-
?
factor X + H2O
activated factor X + ?
factor IXa is a vitamin K-dependent blood coagulation factor that is essential for the amplification or consolidation phase of blood coagulation
-
-
?
factor X + H2O
activated factor X + ?
-
proteolytic activity, factor IXa acts as part of phosphocholine/phosphoserine vesicles interacting with factor VIIIa in the complex in a sodium-dependent manner, overview
-
-
?
factor X + H2O
activated factor X + ?
-
the enzyme acts in complex with factor VIIIa, FVIIIa deficiency causes the bleeding disorder hemaphilia A
-
-
?
factor X + H2O
activated factor X + ?
-
the enzyme is part of the coagulation cascade, factor X activation by the intrinsic tenase complex, factor IXa-factor VIIIa, is the rate-limiting step for thrombin generation
-
-
?
factor X + H2O
activated factor X + ?
factor IXa acts as part of phosphocholine/phosphoserine vesicles interacting with factor VIIIa in the intrinsic tenase complex
-
-
?
factor X + H2O
activated factor X + ?
-
factor IXa acts as part of phosphocholine/phosphoserine vesicles interacting with factor VIIIa in the intrinsic tenase complex, the factor IXa heparin-binding exosite participates in both cofactor binding and protease activation, and cofactor affinity is linked to active site conformation and factor X interaction during enzyme assembly, overview
-
-
?
factor X + H2O
activated factor X + ?
oligosaccharide binding at loop 99 can allosterically modulate the fIXa active site region
-
-
?
factor X + H2O
activated factor X + ?
-
proteolytic activity, factor IXa acts as part of the FXase complex with factor VIIIa on the surface of phospholipid vesicles, overview
-
-
?
factor X + H2O
activated factor X + ?
-
the reaction is performed by the intrinsic FX-activating complex consisting of FIXa and FVIIIa on a negatively charged phospholipid surface in presence of Ca2+
-
-
?
factor X + H2O
factor Xa
-
-
-
-
?
factor X + H2O
factor Xa
in the presence of FVIIIa (5 units/ml) at 37 °C
-
-
?
factor X + H2O
factor Xa
-
in the presence of cofactor fVIIIa and Ca2+ on the surface of platelets or endothelial cells via the intrinsic pathway
-
-
?
Factor X + H2O
Factor Xa + ?
-
-
-
-
?
Factor X + H2O
Factor Xa + ?
-
the activation of factor X by factor IXa-factor VIIIa complex, known as the intrinsic tenase complex, results in the loss of a 55-residue activation peptide and subsequent formation of activated factor X
-
-
?
L-Leu-Gly-L-Arg-4-nitroanilide + H2O
L-Leu-Gly-L-Arg + 4-nitroaniline
-
FIXa-specific chromogenic substrate CBS 31.39
-
-
?
L-Leu-Gly-L-Arg-4-nitroanilide + H2O
L-Leu-Gly-L-Arg + 4-nitroaniline
-
CBS 31.39
-
-
?
L-Leu-Gly-L-Arg-4-nitroanilide + H2O
L-Leu-Gly-L-Arg + 4-nitroaniline
-
FIXa-specific chromogenic substrate CBS 31.39
-
-
?
additional information
?
-
-
fIXa among the S1 family of serine proteinases is uniquely inefficient against synthetic peptide substrates
-
-
?
additional information
?
-
the enzyme is a trypsin-like serine protease in plasma that binds to its cofactor factor VIIIa on negatively charged membrane surfaces in the presence of Ca2+, i.e. intrinsic Xase, to activate factor X to factor Xa in the clotting cascade, factor IXa plays an essential role in hemostasis and its deficiency is associated with the life threatening disease, hemophilia B
-
-
?
additional information
?
-
the loop harboring the S1 specficity site contains the residues His185, Glu186, and Arg188, which, incontrast to other coagulation factor proteases, e.g. unlike thrombin and factor Xa, do not play a functional role in modulating the catalytic function of fIXa in the intrinsic Xase complex, overview
-
-
?
additional information
?
-
human recombinant factor IX has blood clotting activity
-
-
?
additional information
?
-
-
human recombinant factor IX has blood clotting activity
-
-
?
additional information
?
-
-
factor IX-binding protein binds factor IXa with high binding-affinity in a Mg2+-dependent manner
-
-
?
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
methylsulfonyl-D-cyclohexylglycyl-Arg-7-amido-4-methylcoumarin + H2O
methylsulfonyl-D-cyclohexylglycyl-Arg + 7-amino-4-methylcoumarin
-
assay at 37°C
-
-
?
factor X + H2O
?
-
gamma-carboxyglutamic acid, Gla-domains of vitamin K-dependent coagulation factors are essential for binding of phospholipid and for the activation raections such as factor X, the interaction of the Gla-domain with metal ions like Ca2+ is essential for its function
-
-
?
factor X + H2O
?
-
a chymotrypsin homologue, and one of the gamma-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor IX is activated by factor XIa
-
-
?
factor X + H2O
?
-
a chymotrypsin homologue, and one of the gamma-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor IX is activated by factor XIa
-
-
?
factor X + H2O
activated factor X + ?
factor IXa is a vitamin K-dependent blood coagulation factor that is essential for the amplification or consolidation phase of blood coagulation
-
-
?
factor X + H2O
activated factor X + ?
-
proteolytic activity, factor IXa acts as part of phosphocholine/phosphoserine vesicles interacting with factor VIIIa in the complex in a sodium-dependent manner, overview
-
-
?
factor X + H2O
activated factor X + ?
-
the enzyme acts in complex with factor VIIIa, FVIIIa deficiency causes the bleeding disorder hemaphilia A
-
-
?
factor X + H2O
activated factor X + ?
-
the enzyme is part of the coagulation cascade, factor X activation by the intrinsic tenase complex, factor IXa-factor VIIIa, is the rate-limiting step for thrombin generation
-
-
?
factor X + H2O
factor Xa
in the presence of FVIIIa (5 units/ml) at 37 °C
-
-
?
Factor X + H2O
Factor Xa + ?
-
-
-
-
?
Factor X + H2O
Factor Xa + ?
-
the activation of factor X by factor IXa-factor VIIIa complex, known as the intrinsic tenase complex, results in the loss of a 55-residue activation peptide and subsequent formation of activated factor X
-
-
?
additional information
?
-
the enzyme is a trypsin-like serine protease in plasma that binds to its cofactor factor VIIIa on negatively charged membrane surfaces in the presence of Ca2+, i.e. intrinsic Xase, to activate factor X to factor Xa in the clotting cascade, factor IXa plays an essential role in hemostasis and its deficiency is associated with the life threatening disease, hemophilia B
-
-
?
additional information
?
-
human recombinant factor IX has blood clotting activity
-
-
?
additional information
?
-
-
human recombinant factor IX has blood clotting activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Factor VIIIa
-
factor IXa binds to factor VIIIa on phospholipid membranes to form an enzymatic complex, the tenase complex
-
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+
Na+
Ca2+
-
factor IX activation is the first calcium-dependent reaction in intrinsic system clotting
Ca2+
-
5 mM, optimal concentration for cleavage of factor X by factor IXa on phospholipid membranes
Ca2+
for proper binding of factor IXa to phospholipid and factor VIIIa, all of the Ca2+-sites in factor IXa must be filled
Ca2+
-
binding of a subpopulation of platelets to the enzyme is activated by the protease-activated receptor-1, PAR-1, requirring both release of calcium from internal stores and influx of extracellular calcium, overview
Ca2+
-
the reaction is performed by the intrinsic FX-activating complex consisting of FIXa and FVIIIa on a negatively charged phospholipid surface in presence of Ca2+
Ca2+
-
inhibition of activation of aFIX to FIXa when lowering concentration from 1.0 to 0.5 mM
Mg2+
-
1.0 mM, highest aFIX concentration of 1.36 IU/ml in combination with 1.0 mM Ca2+
Mg2+
-
factor IX-binding protein binds factor IXa with high binding-affinity in a Mg2+-dependent manner
Na+
-
activates the amidolytic activity of the enzyme, but does only marginally influence the proteolytic activity of factor IXa in the prothrombinase complex, not required for activation of factor X
Na+
no requirement for Na+ in presence of Ca2+, can partially substite for Ca2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2-carbamimidoylbenzo[b]thiophen-6-yloxy)thiophen-2-ylacetic acid ethyl ester
-
-
(2E)-3-[(7S)-7-[2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-10-yl]prop-2-enoic acid
-
-
(2R)-N-1,3-benzothiazol-5-yl-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
(2R)-N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
(2S)-N-1,3-benzothiazol-5-yl-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
(2S)-N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
(7S)-2-methyl-7-phenyl-7-[4-(4H-1,2,4-triazol-4-yl)benzamido]-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
-
(7S)-2-methyl-7-phenyl-7-[[5-(4H-1,2,4-triazol-4-yl)pyridine-2-carbonyl]amino]-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
-
(7S)-7-[2-chloro-4-(1H-tetrazol-1-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
-
(7S)-7-[2-chloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
-
(7S)-7-[2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxamide
-
-
1-(3-chloro-4-[[(2R)-2,8-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]carbamoyl]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
2,6-dichloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)-N-[(2R)-8-methyl-2-[3-(trifluoromethyl)phenyl]-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]benzamide
-
-
2,6-dichloro-N-((R)-2-((S)-1-hydroxyethyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl)-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(2R)-10-hydroxy-2,7-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(2R)-2,8-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(2R)-2-(3,4-difluorophenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(2R)-2-(3-fluorophenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(2R)-2-(4-fluorophenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(2R)-8-methyl-2-(3-methylphenyl)-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(2R)-8-methyl-2-[1-(propan-2-yl)-1H-1,2,3-triazol-4-yl]-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2,6-dichloro-N-[(3R)-3,7-dimethyl-2,3,4,9-tetrahydro-1H-carbazol-3-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenyl-N-(4-[3-(trifluoromethyl)-1H-pyrazol-1-yl]phenyl)propanamide
-
-
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenyl-N-[4-(4-phenyl-1H-imidazol-1-yl)phenyl]propanamide
-
-
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-cyanophenyl)-3-phenylpropanamide
-
-
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-methylphenyl)-3-phenylpropanamide
-
-
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-phenoxyphenyl)-3-phenylpropanamide
-
-
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-[(6-chloropyridazin-3-yl)sulfamoyl]phenyl)-3-phenylpropanamide
-
-
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(5-fluoro-2-methylphenyl)-3-phenylpropanamide
-
-
2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenyl-N-(2'-sulfamoylbiphenyl-4-yl)propanamide
-
-
2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenyl-N-[4-(5-phenyl-1H-imidazol-4-yl)phenyl]propanamide
-
-
2-(5-carbamimidoyl-1H-indol-3-yl)-N-(4-ethylphenyl)-3-phenylpropanamide - 1H-benzimidazole
-
(1:1)
2-(7-carbamimidoylnaphthalen-1-yl)-N-[2-(1-ethoxyethenyl)cyclohexyl]-3-phenylpropanamide
-
-
2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)-N-ethylcyclohexanecarboxamide
-
-
2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylic acid
-
-
2-chloro-N-[(2R)-2-(3-methoxyphenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2-chloro-N-[(2R)-8-methyl-2-phenyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
-
2-chloro-N-[(7S)-10-cyclopropyl-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
-
2-chloro-N-[(7S)-10-[(E)-(hydroxyimino)methyl]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
-
2-chloro-N-[(7S)-2-methyl-7-phenyl-10-(2,2,2-trifluoro-1-hydroxyethyl)-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
-
2-chloro-N-[(7S)-2-methyl-7-phenyl-10-(2H-tetrazol-5-yl)-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
-
2-chloro-N-[3-methyl-1-(4-methyl-2-nitrophenyl)pyrrolidin-3-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenyl-N-[4-(pyrrolidin-1-ylcarbonyl)phenyl]acetamide
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (1,3-dimethyl-1H-pyrazol-5-yl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2,4-difluorophenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2,6-difluorophenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2-fluorophenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2-methylphenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2-[[(2-methylpropyl)amino]methyl]phenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (3,5-dimethyl-1,2-oxazol-4-yl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (3,5-dimethyl-1H-pyrazol-4-yl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (3-fluorophenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (4-fluorophenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (4-methoxyphenyl)carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [1,3-dimethyl-5-[(propan-2-ylamino)methyl]-1H-pyrazol-4-yl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [1-methyl-3-[(methylamino)methyl]-1H-pyrazol-5-yl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-(aminomethyl)phenyl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-(piperazin-1-ylmethyl)phenyl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-[(dimethylamino)methyl]phenyl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-[(methylamino)methyl]phenyl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [3-(methoxymethyl)-1-methyl-1H-pyrazol-5-yl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [4-[(4-methylpiperazin-1-yl)methyl]phenyl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [4-[2-(dimethylamino)ethoxy]phenyl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [5-[(ethylamino)methyl]-1,3-dimethyl-1H-pyrazol-4-yl]carbamate
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-(2-methoxyphenyl)-2-phenylacetamide
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-(3-methoxyphenyl)-2-phenylacetamide
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-(4-methoxyphenyl)-2-phenylacetamide
-
-
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-[2-(dimethylamino)ethyl]-2-phenylacetamide
-
-
2-[(2-carbamimidoyl-6-fluoro-1-benzothiophen-4-yl)oxy]-2-phenylethyl phenylcarbamate
-
-
2-[(2-carbamimidoyl-6-fluoro-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-(aminomethyl)phenyl]carbamate
-
-
2-[(2-carbamimidoyl-6-fluoro-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-[(dimethylamino)methyl]phenyl]carbamate
-
-
3-(1-[4-(1H-benzimidazol-1-yl)phenyl]-2-oxopyrrolidin-3-yl)-1-benzothiophene-5-carboximidamide
-
-
3-(2-carbamimidoylbenzo[b]thiophen-6-yloxy)-3-(4-chlorophenyl)propionic acid methyl ester
-
-
3-(2-[4-(1H-benzimidazol-1-yl)phenyl]-1-benzyl-2-oxoethyl)-1-benzothiophene-5-carboximidamide
-
-
3-(4-aminophenyl)-N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)propanamide
-
-
3-(4-aminophenyl)-N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)propanamide
-
-
3-[(7R)-7-[2-chloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamido]-2-methyl-7-phenyl-4a,6,7,8,9,10a-hexahydropyrido[1,2-a]indol-10-yl]propanoic acid
-
-
3-[3-([4-(1H-benzimidazol-1-yl)phenyl]amino)-2-(5-carbamimidoyl-1H-indol-3-yl)-3-oxopropyl]benzoic acid
-
-
4-(([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)methyl)-N-[5-(methylsulfonyl)-1H-benzimidazol-2-yl]benzamide
-
-
4-(2-carbamimidoylbenzo[b]thiophen-6-yloxy)-4-(4-chlorophenyl) butyric acid methyl ester
-
-
4-([[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy](phenyl)acetyl]amino)-N,N-dimethylbenzamide
-
-
4-cyano-2-fluoro-N-(10-hydroxy-2,7-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl)benzamide
-
-
4-[phenyl(3-phenyl[1,2,4]oxadiazol-5-yl)methoxy]benzo[b]thiophene-2-carboxamidine
-
-
aptamer
-
RNA aptamers isolated by iterative in vitro selection technique, complete inhibition at 0.00004 mM, inhibition is reversed by specific antidotes, i.e. oligonucleotides, complementary to the aptamers
-
BPTI
Kunitz-type inhibitor, competitive, reversible inhibition, low molecular weight heparin binding to fIXa enhances reactivity of fIXa with the Kunitz-type inhibitor BPTI
-
ethyl 1-[4-([[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy](phenyl)acetyl]amino)phenyl]-1H-imidazole-2-carboxylate
-
-
ethyl 2-([2-(5-carbamimidoyl-1,1-dioxido-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
ethyl 2-([2-(5-carbamimidoyl-1-benzofuran-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
ethyl 2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
ethyl [4-[([2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethoxy]carbonyl)amino]-3,5-dimethyl-1H-pyrazol-1-yl]acetate
-
-
FIX1-47 peptide
-
benzoylphenylalanine containing peptide, 0.038 mM, 50% inhibition
-
methyl (1R)-2-(2-[2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
methyl (1S,2R)-2-(2-[(2R)-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
methyl (1S,2R)-2-(2-[(2S)-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
methyl (1S,2R)-2-(2-[2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
methyl 2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
methyl 2-([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
methyl 3-([[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy](phenyl)acetyl]amino)propanoate
-
-
N-(2-amino-2-oxoethyl)-2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxamide
-
-
N-(4-[3-([4-(1H-benzimidazol-1-yl)phenyl]amino)-2-(5-carbamimidoyl-1H-indol-3-yl)-3-oxopropyl]phenyl)benzamide
-
-
N-1,3-benzothiazol-5-yl-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
N-1H-benzimidazol-2-yl-3-([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)benzamide
-
-
N-1H-benzimidazol-2-yl-4-([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)benzamide
-
-
N-benzyl-2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxamide
-
-
N-[(3R)-1-(3-amino-4,5-dichloro-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1-methyl-2-oxo-1,2-dihydropyrimidin-5-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1-methyl-5-oxo-1,5-dihydro-4H-1,2,4-triazol-4-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1-methyl-6-oxo-1,6-dihydropyridin-3-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1H-imidazo[4,5-b]pyridin-1-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(pyrimidin-2-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(pyrimidin-5-yl)benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-[3-(difluoromethyl)-4H-1,2,4-triazol-4-yl]benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-[4-(2-hydroxyethyl)-1H-imidazol-1-yl]benzamide
-
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-4-(1H-benzimidazol-1-yl)-2-chlorobenzamide
-
N-[(3R)-1-(3-amino-4-fluoro-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[(3R)-1-(3-amino-5-methyl[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[(7S)-10-(5-aminopyridin-3-yl)-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
-
N-[1-(3-amino-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[1-(3-amino-5-methyl-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[1-(3-amino[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
N-[2-(5,6-dimethyl-1H-benzimidazol-2-yl)ethyl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
-
N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1-methyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(6-carbamimidoyl-1H-indol-1-yl)-3-phenylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-naphthalen-1-ylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)butanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-2-methylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-(4-[(phenylsulfonyl)amino]phenyl)propanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-cyclohexylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-naphthalen-2-ylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-pyridin-3-ylpropanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-4-phenylbutanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)butanamide
-
-
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)propanamide
-
-
N-[4-(1H-benzimidazol-2-yl)phenyl]-2-benzyl-3-(5-carbamimidoyl-1H-indol-3-yl)propanamide
-
-
N-[4-(1H-benzimidazol-2-yl)phenyl]-3-(5-carbamimidoyl-1H-indol-3-yl)-4-phenylbutanamide
-
-
supersulfated low molecular weight heparin
-
inhibits the intrinsic tenase (factor IXa-factor VIIIa) complex in an antithrombin-independent manner by 90% when using factor X as substrate. Supersulfated low molecular weight heparin is 32fold more potent than unmodified low molecular weight heparin in the inhibition of factor X activation by the intrinsic tenase complex
-
antithrombin
-
almost no inhibition in the absence of heparin, strong acceleration of the inhibition rate in the presence of heparin and physiologic levels of Ca2+
-
antithrombin
-
more than 1200fold increase in inhibition in the presence of heparin, 11fold increase in inhibition in the presence of fondaparinux, 7fold increase in inhibition in the presence of 2 mM CaCl2
-
antithrombin
in vivo and in vitro inhibition, the interaction is improved by heparin binding via the formation of bridged complexes where heparin acts as a template
-
antithrombin
-
inactivation, second-order-association rate constants in absence or presence of H5, a pentasaccharide fragment derived from heparin, in a Ca2+-dependent manner, but independent of Na+, overview
-
antithrombin III
-
a nonspecific protein inhibitor, in presence of heparin, this forms a stable or covalent-like intermediate with the factor IXa
-
additional information
-
factor IXa is resistant to inhibition by the plasma inhibitors protein Z-dependent protease inhibitor and tissue factor pathway inhibitor
-
additional information
-
protamine sulfate is able to reverse the heparin effect of the enhanced inhibition with bovine pancreatic trypsin inhibitor
-
additional information
oligosaccharide binding at loop 99 can allosterically modulate the fIXa active site region, overview
-
additional information
-
allosteric activation of antithrombin inhibits factor IXa
-
additional information
-
aptamer 9.3t blocks the activity of factor IXa-factor VIIIa complex
-
additional information
-
factor IXa is resistant to inhibition by the plasma inhibitors protein Z-dependent protease inhibitor and tissue factor pathway inhibitor
-
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
1,2-dicaproyl-sn-glycero-3-phospho-L-serine
-
up-regulates the catalytic activity of the enzyme
1,2-propanediol
-
25-40% v/v, up to 20fold increase of the activity, methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide as substrate, rFIXa
emicizumab
-
factorIXa/factorX bispecific antibody. Emicizumab functions as a cofactor to promote the factor IXa-catalyzed factor X activation
-
ethanol
-
25% v/v, 6fold increase of the activity, methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide as substrate, rFIXa, alcohols modify the conformation of FIXa rendering the active-site cleft more easily accessible to tripeptide substrates with a hydrophobic residue in the P3-position
factor IX
-
concentrations of approximately 100 nM, physiological levels in plasma, increases the activation of factor X catalyzed by factor IXa by increasing the affinity of the factor X for the intrinsic factor X activation complex
-
factor IX-specific antibodies
-
antibosies specific for human factor I, e.g. 198A1, 198B3, and 224F3, enhance the factor IXa activity mimicking the stimulatory effect of FVIIIa, and thus can replace FVIIIa as cofactor in the FX activation reaction, overview
-
Factor XIa
-
factor XIa proteolytically activates factor IX by an exosite- and Ca2+-mediated release-rebind mechanism. XIa cleaves IX after Arg145, forming IXalpha, and then after Arg180, forming IXabeta
-
glycerol
-
50% v/v, 6fold increase of the activity, methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide as substrate, rFIXa
i-erythritol
-
50% v/v, 1.5fold increase of the activity, methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide as substrate, rFIXa
low molecular weight heparin
-
enhances the activity of factor IXa (0.01 mM used in assay conditions)
-
methanol
-
25% v/v, 4fold increase of the activity, methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide as substrate, rFIXa, alcohols modify the conformation of FIXa rendering the active-site cleft more easily accessible to tripeptide substrates with a hydrophobic residue in the P3-position
tert-butanol
-
up to 10% v/v, increase of the activity, higher concentrations lead to a drastic activity decrease, methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide as substrate, rFIXa, alcohols modify the conformation of FIXa rendering the active-site cleft more easily accessible to tripeptide substrates with a hydrophobic residue in the P3-position
TRYLRIHPQSWVHQIALRMEV
-
approx. 600fold lower km, slight increase in kcat, optimal activation in the presence of 0.5-1 mM Ca2+
ethylene glycol
-
25-40% v/v, up to 20fold increase of the activity, methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide as substrate, rFIXa
ethylene glycol
-
enhances the activity of factor IXa (30% (v/v) used in assay conditions)
Factor VIIIa
-
protein cofactor, consists of A1, A2, and A3-C1-C2 subunits, A2 enhances the turnover number 100fold, the A1 subunit increases the A2-dependent stimulation by 10fold
-
Factor VIIIa
-
200000fold activation in the presence of phospholipid membrane through a combinantion of a decrease in Km and an increase in kcat
-
Factor VIIIa
-
a ternary complex of factor IXa, factor VIIIa and factor X is assembled on the activated platelet surface
-
Factor VIIIa
stoichoimetric complex with factor IXa, helix 330 of factor IXa interacts with the 558-565 region of factor VIII A2 subunit
-
Factor VIIIa
-
the tenase complex, consisting of factor IXa and factor VIIIa assembled on a phospholipid-containing membrane, is the kinetically significant activator of factor X
-
Factor VIIIa
-
binding curves of FIXa and FVIIIa, binding of factor VIIIa with engineered disulfide bond resulting in a more stable FVIIIa: C662C1828 FVIIIa binds with similar affinity to that of wild-type FVIIIa, while C664-C1826 FVIIIa binds to FIXa with a significantly lower affinity, binding structures, overview
-
Factor VIIIa
-
binds to the activated factor IX and enhances the activation of factor X by several orders of magnitude
-
Factor VIIIa
-
factor IXa acts as part of phosphocholine/phosphoserine vesicles interacting with factor VIIIa in the intrinsic tenase complex
-
Factor VIIIa
-
factor VIIIa functions as a cofactor for factor IXa in the conversion of zymogen factor X to factor Xa. Factor IXa binding affinity for factor VIIIa is significantly reduced in the presence of GMA8011 (about 10fold)
-
Factor VIIIa
-
factor VIIIa may directly modulate the active catalytic site of factor IXa to increase kcat of the factor IXa-catalyzed factor X activation
-
heparin
-
activates by mediating cofactor binding, heparin binds to an exosite on the factor IXa protease domain, the factor IXa heparin-binding exosite participates in both cofactor binding and protease activation, and cofactor affinity is linked to active site conformation and factor X interaction during enzyme assembly, overview
Phospholipid
-
the reaction is performed by the intrinsic FX-activating complex consisting of FIXa and FVIIIa on a negatively charged phospholipid surface in presence of Ca2+
phospholipid membrane
-
200000fold activation in the presence of factor VIIIa through a combinantion of a decrease in Km and an increase in kcat
-
phospholipid membrane
-
phospholipid vesicles composed of 1-palmityl-2-oleoyl-sn-glycero-3-phosphoethanolamine, phosphatidylserine and phosphatidylcholine support factor Xa generation
-
Phospholipids
-
factor IXa acts as part of phosphocholine/phosphoserine vesicles interacting with factor VIIIa in the intrinsic tenase complex
Phospholipids
-
the vesicles binding the enzyme consist of 40% phosphatidylcholine, 20% phosphatidylserine, and 40% phosphatidylethanolamine
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
3.62
methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide
-
rFIXa, at pH 7.4, in the presence of 33% v/v ethylene glycol
1.43
methylsulfonyl-D-cyclohexylglycyl-Gly-Arg-p-nitroanilide
-
rFIXa, at pH 7.4, in the presence of 33% v/v ethylene glycol
5.99
methylsulfonyl-D-hexahydrotyrosyl-Gly-Arg-p-nitroanilide
-
rFIXa, at pH 7.4, in the presence of 33% v/v ethylene glycol
0.5
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
wild type enzyme FIXa, in presence of 200 mM Na+
2.1
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
mutant enzyme FIXagamma225P
3.1
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
mutant enzyme FIXagamma225P, in presence of 200 mM Na+
4.5
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
wild type enzyme FIXa, in presence of 5 mM Ca2+ and 185 mM Na+
7.3
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
mutant enzyme FIXagamma225P, in presence of 5 mM Ca2+ and 185 mM Na+
7.9
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
mutant enzyme FIXagamma225P, in presence of 200 mM Ca2+
8.7
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
wild type enzyme FIXa, in presence of 200 mM Ca2+
1.7
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
-
pH 7.5, 22°C, in presence of 5 mM Ca2+ and 0.2 M ChCl
2.2
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
-
pH 7.5, 22°C, in presence of 5 mM Ca2+ with or without presence of 0.2 M LiCl
2.2
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
pH 7.5, 37°C, recombinant wild-type enzyme, in absence of NaCl
2.2
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
pH 7.5, 37°C, recombinant wild-type enzyme, in presence of 0.2 M NaCl
2.3
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
-
pH 7.5, 22°C, in presence of 5 mM Ca2+ and 0.2 M NaCl
3.2
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
-
pH 7.5, 22°C, in presence of 5 mM Ca2+ and 0.2 M RbCl
0.000001
Factor X
-
pH 7.4, 22°C, recombinant mutant N178A the intrinsic tenase complex, in absence of ethylene glycol
-
0.00000311
Factor X
-
chimera enzyme FIXa7omegaloop7EGF2, in the presence of phospholipid vesicles
-
0.0000052
Factor X
-
pH 7.4, 22°C, recombinant mutant R165A the intrinsic tenase complex, in absence of ethylene glycol
-
0.0000068
Factor X
mutant enzyme rFIXa90A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.0000073
Factor X
-
pH 7.4, 22°C, recombinant mutant K126A the intrinsic tenase complex, in absence of ethylene glycol
-
0.0000085
Factor X
-
pH 7.4, 22°C, recombinant mutants N129A and K132A, each in the intrinsic tenase complex, in absence of ethylene glycol
-
0.00000864
Factor X
-
chimera enzyme FIX7EGF2, in the presence of phospholipid vesicles
-
0.0000089
Factor X
mutant enzyme rFIXa107A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.0000096
Factor X
-
pH 7.4, 22°C, recombinant wild-type enzyme the intrinsic tenase complex, in absence of ethylene glycol
-
0.000013
Factor X
-
mutant Y94F/A95aK/K98T/Y177F/I213V/E219G, FX activation in presence of FVIIIa
-
0.000014
Factor X
-
mutant Y94F/K98T/Y177F, FX activation in presence of FVIIIa
-
0.000017
Factor X
-
mutant Y94F/K98T/Y177F/I213V/E219, FX activation in presence of FVIIIa
-
0.0000181
Factor X
mutant enzyme rFIXa90A, 5 units/ml FVIIIa and extruded phosphatidylcholine-phosphatidylserine phospholipid vesicles supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.00002
Factor X
mutant enzyme rFIXa104A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.0000216
Factor X
-
chimera enzyme FIX7EGF2, in the presence of SFLLRN-activated platelets
-
0.0000224
Factor X
mutant enzyme rFIXa94A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.0000251
Factor X
mutant enzyme rFIXa105A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.0000259
Factor X
-
chimera enzyme FIX7omegaloop, in the presence of SFLLRN-activated platelets
-
0.0000286
Factor X
-
chimera enzyme FIX7omegaloop, in the presence of phospholipid vesicles
-
0.00002877
Factor X
-
wild type enzyme, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
0.0000295
Factor X
mutant enzyme rFIXa91A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.000034
Factor X
mutant enzyme rFIXa107A, 5 units/ml FVIIIa and extruded phosphatidylcholine-phosphatidylserine phospholipid vesicles supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.000037
Factor X
-
25°C, pH 7.4, in the presence of phospholipid vesicle containing 79% phosphatidylcholine, 1% phosphatidylserine and 20% phosphatidylethanolamine
-
0.000038
Factor X
-
FIXa/FXa chimera in which the 39-loop of the protease is replaced with the corresponding loop of FXa, in TBS containing 0.1 mg/ml bovine serum albumin, 0.1% polyethylene glycol (PEG) 8000, and 5 mM Ca2+, at 22°C, pH not specified in the publication
-
0.0000396
Factor X
plasma-derived FIXa, 5 units/ml FVIIIa and extruded phosphatidylcholine-phosphatidylserine phospholipid vesicles supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.00004
Factor X
-
mutant Y94F/K98T/Y177F/I213V/E219, FX activation in absence of FVIIIa
-
0.0000405
Factor X
-
chimera enzyme FIXaN, in the presence of SFLLRN-activated platelets
-
0.0000428
Factor X
plasma-derived FIXa, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.000048
Factor X
-
pH 7.4, 22°C, recombinant mutant K132A the intrinsic tenase complex, in presence of 30% ethylene glycol
-
0.0000502
Factor X
-
chimera enzyme FIXaN, in the presence of phospholipid vesicles
-
0.0000508
Factor X
-
chimera enzyme FIXa7omegaloop7EGF2, in the presence of SFLLRN-activated platelets
-
0.000055
Factor X
-
pH 7.4, 22°C, recombinant wild-type enzyme the intrinsic tenase complex, in presence of 30% ethylene glycol
-
0.000055
Factor X
-
mutant Y94F/A95aK/K98T/Y177F/I213V/E219G, FX activation in absence of FVIIIa
-
0.00005793
Factor X
-
mutant enzyme E410N, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
0.000061
Factor X
-
pH 7.4, 22°C, recombinant mutant N129A the intrinsic tenase complex, in presence of 30% ethylene glycol
-
0.0000629
Factor X
mutant enzyme rFIXa91A, 5 units/ml FVIIIa and extruded phosphatidylcholine-phosphatidylserine phospholipid vesicles supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.000064
Factor X
mutant enzyme rFIXa94A, 5 units/ml FVIIIa and extruded phosphatidylcholine-phosphatidylserine phospholipid vesicles supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.000067
Factor X
-
pH 7.4, 22°C, recombinant mutant R165A the intrinsic tenase complex, in presence of 30% ethylene glycol
-
0.000068
Factor X
-
mutant Y94F/K98T/Y177F, FX activation in absence of FVIIIa
-
0.00006988
Factor X
-
mutant enzyme E410L, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
0.000071
Factor X
-
wild type enzyme, in TBS containing 0.1 mg/ml bovine serum albumin, 0.1% polyethylene glycol (PEG) 8000, and 5 mM Ca2+, at 22°C, pH not specified in the publication
-
0.0000751
Factor X
-
mutant enzyme E410H, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
0.0000787
Factor X
mutant enzyme rFIXa104A, 5 units/ml FVIIIa and extruded phosphatidylcholine-phosphatidylserine phospholipid vesicles supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.00008
Factor X
-
factor IXabeta', 0.1 mg/ml phospholipids, factor VIIIa in activating mixture
-
0.00008
Factor X
-
pH 7.4, 22°C, recombinant mutant N178A the intrinsic tenase complex, in presence of 30% ethylene glycol
-
0.00008004
Factor X
-
mutant enzyme E410A, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
0.0000869
Factor X
mutant enzyme rFIXa105A, 5 units/ml FVIIIa and extruded phosphatidylcholine-phosphatidylserine phospholipid vesicles supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.000089
Factor X
-
pH 7.4, 22°C, recombinant mutant K126A the intrinsic tenase complex, in presence of 30% ethylene glycol
-
0.00013
Factor X
-
25°C, pH 7.4, in the presence of GIGAVLKVLTTGLPALISSWIKRKRQQ
-
0.0001542
Factor X
mutant enzyme rFIXa89A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
0.00017
Factor X
-
factor IXabeta', 0.1 mg/ml phospholipids in activating mixture
-
0.0002227
Factor X
-
mutant enzyme E410N, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
0.0002241
Factor X
-
mutant enzyme E410A, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
0.000231
Factor X
-
mutant enzyme E410H, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
0.0002328
Factor X
-
mutant enzyme E410L, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
0.0004478
Factor X
-
wild type enzyme, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
0.0006
Factor X
-
Gla-domainless factor IXabeta', 0.1 mg/ml phospholipids, factor VIIIa in activating mixture
-
0.0008
Factor X
-
Gla-domainless factor IXabeta', 0.1 mg/ml phospholipids in activating mixture
-
0.0045
Factor X
-
in the presence of recombinant tissue factor protein and vesicles composed of 75% (w/w) L-alpha-phosphatidylcholine and 25% (w/w) L-alpha-phosphatidylserine
-
0.38
Factor X
-
25°C, pH 7.4, in the presence of phospholipid vesicle containing 79% phosphatidylcholine, 1% phosphatidylserine and 20% phosphatidylethanolamine
-
1.2
L-Leu-Gly-L-Arg-4-nitroanilide
-
FIXa/FXa chimera in which the 39-loop of the protease is replaced with the corresponding loop of FXa, in 0.02 M Tris-HCl (pH 7.5) buffer containing 0.1 M NaCl, 0.1 mg/ml bovine serum albumin, 33% ethylene glycol, and 5 mM Ca2+, at 22°C
2.3
L-Leu-Gly-L-Arg-4-nitroanilide
-
wild type enzyme, in 0.02 M Tris-HCl (pH 7.5) buffer containing 0.1 M NaCl, 0.1 mg/ml bovine serum albumin, 33% ethylene glycol, and 5 mM Ca2+, at 22°C
additional information
additional information
-
kinetic determination of the affinity for factor IXa-factor VIIIa complex formation, effect of ethylene glycol at 30% on reaction kinetics, overview
-
additional information
additional information
steady-state kinetics of wild-type and mutant enzymes n presence or absence of NaCl
-
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
2.01
methoxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide
-
rFIXa, at pH 7.4, in the presence of 33% v/v ethylene glycol
5.67
methylsulfonyl-D-cyclohexylglycyl-Gly-Arg-p-nitroanilide
-
rFIXa, at pH 7.4, in the presence of 33% v/v ethylene glycol
6.11
methylsulfonyl-D-hexahydrotyrosyl-Gly-Arg-p-nitroanilide
-
rFIXa, at pH 7.4, in the presence of 33% v/v ethylene glycol
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
0.005
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
mutant enzyme FIXagamma225P
0.058
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
mutant enzyme FIXagamma225P, in presence of 200 mM Na+
0.63
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
wild type enzyme FIXa, in presence of 200 mM Na+
0.78
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
mutant enzyme FIXagamma225P, in presence of Ca2+ and 185 mM Na+
0.89
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
mutant enzyme FIXagamma225P, in presence of 200 mM Ca2+
3.15
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
wild type enzyme FIXa, in presence of 200 mM Ca2+
3.38
4-methylsulfonyl-D-Leu-Gly-Arg-p-nitroanilide
wild type enzyme FIXa, in presence of Ca2+ and 185 mM Na+
18.5
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
-
pH 7.5, 22°C, in presence of 5 mM Ca2+
18.5
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
pH 7.5, 37°C, recombinant wild-type enzyme, in absence of NaCl
19
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
-
pH 7.5, 22°C, in presence of 5 mM Ca2+ and 0.2 M LiCl
20.2
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
-
pH 7.5, 22°C, in presence of 5 mM Ca2+ and 0.2 M NaCl
20.2
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
pH 7.5, 37°C, recombinant wild-type enzyme, in presence of 0.2 M NaCl
21.3
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
-
pH 7.5, 22°C, in presence of 5 mM Ca2+ and 0.2 M ChCl
21.9
CH3SO2-D-Leu-Gly-Arg-4-nitroanilide
-
pH 7.5, 22°C, in presence of 5 mM Ca2+ and 0.2 M RbCl
0.00011
Factor X
-
mutant Y94F/K98T/Y177F, FX activation in presence of FVIIIa
-
0.0002
Factor X
-
mutant Y94F/A95aK/K98T/Y177F/I213V/E219G, FX activation in presence of FVIIIa
-
0.00023
Factor X
-
25°C, pH 7.4, in the presence of GIGAVLKVLTTGLPALISSWIKRKRQQ
-
0.00088
Factor X
-
mutant Y94F/K98T/Y177F/I213V/E219, FX activation in presence of FVIIIa
-
0.00096
Factor X
-
mutant enzyme E410H, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
0.00096
Factor X
-
mutant enzyme E410N, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
0.001
Factor X
-
mutant Y94F/A95aK/K98T/Y177F/I213V/E219G, FX activation in absence of FVIIIa
-
0.00105
Factor X
-
mutant enzyme E410A, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
0.0012
Factor X
-
mutant enzyme E410L, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
0.00127
Factor X
-
wild type enzyme, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
0.00157
Factor X
-
wild type enzyme, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
0.0022
Factor X
-
mutant Y94F/K98T/Y177F/I213V/E219, FX activation in absence of FVIIIa
-
0.00248
Factor X
-
mutant enzyme E410N, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
0.00361
Factor X
-
mutant enzyme E410L, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
0.00397
Factor X
-
mutant enzyme E410H, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
0.00399
Factor X
-
mutant enzyme E410A, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
0.048
Factor X
-
in the presence of emicizumab, pH and temperature not specified in the publication
-
0.38
Factor X
-
25°C, pH 7.4, in the presence of phospholipid vesicle containing 79% phosphatidylcholine, 1% phosphatidylserine and 20% phosphatidylethanolamine
-
1
Factor X
-
FIXa/FXa chimera in which the 39-loop of the protease is replaced with the corresponding loop of FXa, in TBS containing 0.1 mg/ml bovine serum albumin, 0.1% polyethylene glycol (PEG) 8000, and 5 mM Ca2+, at 22°C, pH not specified in the publication
-
1.9
Factor X
-
pH 7.4, 22°C, recombinant mutant R165A the intrinsic tenase complex, in absence of ethylene glycol
-
2.1
Factor X
-
in the presence of factor VIIIa, pH and temperature not specified in the publication
-
2.9
Factor X
mutant enzyme rFIXa104A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
2.9
Factor X
mutant enzyme rFIXa94A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
3.2
Factor X
-
chimera enzyme FIXaN, in the presence of SFLLRN-activated platelets
-
3.3
Factor X
-
chimera enzyme FIX7EGF2, in the presence of SFLLRN-activated platelets
-
3.3
Factor X
mutant enzyme rFIXa107A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
3.4
Factor X
plasma-derived FIXa, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
3.5
Factor X
-
wild type enzyme, in TBS containing 0.1 mg/ml bovine serum albumin, 0.1% polyethylene glycol (PEG) 8000, and 5 mM Ca2+, at 22°C, pH not specified in the publication
-
3.8
Factor X
-
chimera enzyme FIX7omegaloop, in the presence of SFLLRN-activated platelets
-
3.8
Factor X
mutant enzyme rFIXa105A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
4.1
Factor X
mutant enzyme rFIXa90A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
5.08
Factor X
-
pH 7.4, 22°C, recombinant mutant N178A the intrinsic tenase complex, in absence of ethylene glycol
-
5.2
Factor X
mutant enzyme rFIXa91A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
5.2
Factor X
-
pH 7.4, 22°C, recombinant mutant K126A the intrinsic tenase complex, in absence of ethylene glycol
-
5.47
Factor X
-
pH 7.4, 22°C, recombinant mutant K132A the intrinsic tenase complex, in absence of ethylene glycol
-
5.51
Factor X
-
pH 7.4, 22°C, recombinant wild-type enzyme the intrinsic tenase complex, in absence of ethylene glycol
-
5.6
Factor X
-
pH 7.4, 22°C, recombinant mutant N129A the intrinsic tenase complex, in absence of ethylene glycol
-
16.6
Factor X
mutant enzyme rFIXa89A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C
-
600
Factor X
-
pH 7.4, 22°C, recombinant mutant N178A the intrinsic tenase complex, in presence of 30% ethylene glycol
-
1000
Factor X
-
pH 7.4, 22°C, recombinant mutant R165A the intrinsic tenase complex, in presence of 30% ethylene glycol
-
1340
Factor X
-
pH 7.4, 22°C, recombinant wild-type enzyme and mutant N129A, each in the intrinsic tenase complex, in presence of 30% ethylene glycol
-
1780
Factor X
-
pH 7.4, 22°C, recombinant mutant K132A the intrinsic tenase complex, in presence of 30% ethylene glycol
-
1999
Factor X
-
pH 7.4, 22°C, recombinant mutant K126A the intrinsic tenase complex, in presence of 30% ethylene glycol
-
17.5
L-Leu-Gly-L-Arg-4-nitroanilide
-
FIXa/FXa chimera in which the 39-loop of the protease is replaced with the corresponding loop of FXa, in 0.02 M Tris-HCl (pH 7.5) buffer containing 0.1 M NaCl, 0.1 mg/ml bovine serum albumin, 33% ethylene glycol, and 5 mM Ca2+, at 22°C
21.4
L-Leu-Gly-L-Arg-4-nitroanilide
-
wild type enzyme, in 0.02 M Tris-HCl (pH 7.5) buffer containing 0.1 M NaCl, 0.1 mg/ml bovine serum albumin, 33% ethylene glycol, and 5 mM Ca2+, at 22°C
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
the catalytic efficiency kcat/Km, of phospholipid vesicles containing 20 or 35% phosphatidylethanolamine and no phosphatidylserine is 5.5fold higher than that of vesicles containing 1% phosphatidylserine and no phosphatidylethanolamine
additional information
additional information
-
the catalytic efficiency kcat/Km, of phospholipid vesicles containing 20 or 35% phosphatidylethanolamine and no phosphatidylserine is 5.5fold higher than that of vesicles containing 1% phosphatidylserine and no phosphatidylethanolamine
-
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
1.5
Factor X
-
mutant Y94F/A95aK/K98T/Y177F/I213V/E219G, FX activation in presence of FVIIIa
-
2.825
Factor X
-
wild type enzyme, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
4.163
Factor X
-
mutant enzyme E410H, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
4.326
Factor X
-
mutant enzyme E410N, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
4.374
Factor X
-
mutant enzyme E410L, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
4.693
Factor X
-
mutant enzyme E410A, in the absence of factor VIIIa, at pH 7.4 and 37°C
-
5.33
Factor X
-
mutant Y94F/K98T/Y177F/I213V/E219, FX activation in presence of FVIIIa
-
18.17
Factor X
-
mutant Y94F/A95aK/K98T/Y177F/I213V/E219G, FX activation in absence of FVIIIa
-
55
Factor X
-
mutant Y94F/K98T/Y177F/I213V/E219, FX activation in absence of FVIIIa
-
25000
Factor X
-
FIXa/FXa chimera in which the 39-loop of the protease is replaced with the corresponding loop of FXa, in TBS containing 0.1 mg/ml bovine serum albumin, 0.1% polyethylene glycol (PEG) 8000, and 5 mM Ca2+, at 22°C, pH not specified in the publication
-
42800
Factor X
-
mutant enzyme E410N, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
49000
Factor X
-
wild type enzyme, in TBS containing 0.1 mg/ml bovine serum albumin, 0.1% polyethylene glycol (PEG) 8000, and 5 mM Ca2+, at 22°C, pH not specified in the publication
-
49800
Factor X
-
mutant enzyme E410A, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
51600
Factor X
-
mutant enzyme E410L, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
52900
Factor X
-
mutant enzyme E410H, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
54500
Factor X
-
wild type enzyme, in the presence of factor VIIIa, at pH 7.4 and 37°C
-
9.3
L-Leu-Gly-L-Arg-4-nitroanilide
-
wild type enzyme, in 0.02 M Tris-HCl (pH 7.5) buffer containing 0.1 M NaCl, 0.1 mg/ml bovine serum albumin, 33% ethylene glycol, and 5 mM Ca2+, at 22°C
14.6
L-Leu-Gly-L-Arg-4-nitroanilide
-
FIXa/FXa chimera in which the 39-loop of the protease is replaced with the corresponding loop of FXa, in 0.02 M Tris-HCl (pH 7.5) buffer containing 0.1 M NaCl, 0.1 mg/ml bovine serum albumin, 33% ethylene glycol, and 5 mM Ca2+, at 22°C
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
0.0005
(2-carbamimidoylbenzo[b]thiophen-4-yloxy)phenylacetic acid methyl ester
-
pH and temperature not specified in the publication
0.000003
(2-carbamimidoylbenzo[b]thiophen-6-yloxy)thiophen-2-ylacetic acid ethyl ester
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0000008
(2E)-3-[(7S)-7-[2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-10-yl]prop-2-enoic acid
-
pH and temperature not specified in the publication
0.00048
(2R)-N-1,3-benzothiazol-5-yl-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
0.000018
(2R)-N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
0.01422
(2S)-N-1,3-benzothiazol-5-yl-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
0.00082
(2S)-N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
0.0000006
(7S)-2-methyl-7-phenyl-7-[4-(4H-1,2,4-triazol-4-yl)benzamido]-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
pH and temperature not specified in the publication
0.0000025
(7S)-2-methyl-7-phenyl-7-[[5-(4H-1,2,4-triazol-4-yl)pyridine-2-carbonyl]amino]-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
pH and temperature not specified in the publication
0.0000086
(7S)-7-[2-chloro-4-(1H-tetrazol-1-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
pH and temperature not specified in the publication
0.0000006
(7S)-7-[2-chloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxylic acid
-
pH and temperature not specified in the publication
0.0000012
(7S)-7-[2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamido]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indole-10-carboxamide
-
pH and temperature not specified in the publication
0.0000063 - 0.0000348
1-(3-chloro-4-[[(2R)-2,8-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]carbamoyl]phenyl)-1H-benzimidazole-5-carboxylic acid
0.0000045
2,6-dichloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)-N-[(2R)-8-methyl-2-[3-(trifluoromethyl)phenyl]-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]benzamide
-
pH and temperature not specified in the publication
0.0000125
2,6-dichloro-N-((R)-2-((S)-1-hydroxyethyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl)-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000102 - 0.0000121
2,6-dichloro-N-[(2R)-10-hydroxy-2,7-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
0.0000102
2,6-dichloro-N-[(2R)-2,8-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000105
2,6-dichloro-N-[(2R)-2-(3,4-difluorophenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000031 - 0.0000066
2,6-dichloro-N-[(2R)-2-(3-fluorophenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
0.0000042
2,6-dichloro-N-[(2R)-2-(4-fluorophenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000018
2,6-dichloro-N-[(2R)-8-methyl-2-(3-methylphenyl)-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.000005
2,6-dichloro-N-[(2R)-8-methyl-2-[1-(propan-2-yl)-1H-1,2,3-triazol-4-yl]-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000117 - 0.0002676
2,6-dichloro-N-[(3R)-3,7-dimethyl-2,3,4,9-tetrahydro-1H-carbazol-3-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
0.00515
2-(2-carbamimidoylbenzo[b]thiophen-4-yloxy)propionic acid methyl ester
-
pH and temperature not specified in the publication
0.0001
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenyl-N-(4-[3-(trifluoromethyl)-1H-pyrazol-1-yl]phenyl)propanamide
-
-
0.00039
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenyl-N-[4-(4-phenyl-1H-imidazol-1-yl)phenyl]propanamide
-
-
0.00173
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-cyanophenyl)-3-phenylpropanamide
-
-
0.00058
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-methylphenyl)-3-phenylpropanamide
-
-
0.00025
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-phenoxyphenyl)-3-phenylpropanamide
-
-
0.00093
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(4-[(6-chloropyridazin-3-yl)sulfamoyl]phenyl)-3-phenylpropanamide
-
-
0.0096
2-(5-carbamimidoyl-1-benzothiophen-3-yl)-N-(5-fluoro-2-methylphenyl)-3-phenylpropanamide
-
-
0.00066
2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenyl-N-(2'-sulfamoylbiphenyl-4-yl)propanamide
-
-
0.00027
2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenyl-N-[4-(5-phenyl-1H-imidazol-4-yl)phenyl]propanamide
-
-
0.0067
2-(5-carbamimidoyl-1H-indol-3-yl)-N-(2'-sulfamoylbiphenyl-4-yl)acetamide
-
-
0.00031
2-(5-carbamimidoyl-1H-indol-3-yl)-N-(4-ethylphenyl)-3-phenylpropanamide - 1H-benzimidazole
-
(1:1)
0.00024
2-(7-carbamimidoylnaphthalen-1-yl)-N-[2-(1-ethoxyethenyl)cyclohexyl]-3-phenylpropanamide
-
-
0.00043
2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)-N-ethylcyclohexanecarboxamide
-
-
0.0035
2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylic acid
-
-
0.00095
2-amidino-4-iodobenzothiophene
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.000003
2-chloro-N-[(2R)-2-(3-methoxyphenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000021 - 0.0000069
2-chloro-N-[(2R)-8-methyl-2-phenyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
0.0000051 - 0.0000084
2-chloro-N-[(7S)-10-cyclopropyl-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
0.0000024 - 0.0000029
2-chloro-N-[(7S)-10-[(E)-(hydroxyimino)methyl]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
0.0000026 - 0.0000055
2-chloro-N-[(7S)-2-methyl-7-phenyl-10-(2,2,2-trifluoro-1-hydroxyethyl)-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
0.0000024
2-chloro-N-[(7S)-2-methyl-7-phenyl-10-(2H-tetrazol-5-yl)-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
pH and temperature not specified in the publication
0.00029
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenyl-N-[4-(pyrrolidin-1-ylcarbonyl)phenyl]acetamide
-
pH and temperature not specified in the publication
0.00001
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (1,3-dimethyl-1H-pyrazol-5-yl)carbamate
-
pH and temperature not specified in the publication
0.000007
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2,4-difluorophenyl)carbamate
-
pH and temperature not specified in the publication
0.000007
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2,6-difluorophenyl)carbamate
-
pH and temperature not specified in the publication
0.000005
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2-fluorophenyl)carbamate
-
pH and temperature not specified in the publication
0.000008
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2-methylphenyl)carbamate
-
pH and temperature not specified in the publication
0.000002
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (2-[[(2-methylpropyl)amino]methyl]phenyl)carbamate
-
pH and temperature not specified in the publication
0.000012
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (3,5-dimethyl-1,2-oxazol-4-yl)carbamate
-
pH and temperature not specified in the publication
0.000008
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (3,5-dimethyl-1H-pyrazol-4-yl)carbamate
-
pH and temperature not specified in the publication
0.000025
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (3-fluorophenyl)carbamate
-
pH and temperature not specified in the publication
0.000008
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (4-fluorophenyl)carbamate
-
pH and temperature not specified in the publication
0.000005
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl (4-methoxyphenyl)carbamate
-
pH and temperature not specified in the publication
0.00001
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl phenylcarbamate
-
pH and temperature not specified in the publication
0.000003
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [1,3-dimethyl-5-[(propan-2-ylamino)methyl]-1H-pyrazol-4-yl]carbamate
-
pH and temperature not specified in the publication
0.000005
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [1-methyl-3-[(methylamino)methyl]-1H-pyrazol-5-yl]carbamate
-
pH and temperature not specified in the publication
0.000004
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-(aminomethyl)phenyl]carbamate
-
pH and temperature not specified in the publication
0.000003
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-(piperazin-1-ylmethyl)phenyl]carbamate
-
pH and temperature not specified in the publication
0.000008
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-[(dimethylamino)methyl]phenyl]carbamate
-
pH and temperature not specified in the publication
0.000003
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-[(methylamino)methyl]phenyl]carbamate
-
pH and temperature not specified in the publication
0.000009
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [3-(methoxymethyl)-1-methyl-1H-pyrazol-5-yl]carbamate
-
pH and temperature not specified in the publication
0.00001
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [4-[(4-methylpiperazin-1-yl)methyl]phenyl]carbamate
-
pH and temperature not specified in the publication
0.000004
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [4-[2-(dimethylamino)ethoxy]phenyl]carbamate
-
pH and temperature not specified in the publication
0.000005
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethyl [5-[(ethylamino)methyl]-1,3-dimethyl-1H-pyrazol-4-yl]carbamate
-
pH and temperature not specified in the publication
0.00017
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N,2-diphenylacetamide
-
pH and temperature not specified in the publication
0.00014
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-(2-methoxyphenyl)-2-phenylacetamide
-
pH and temperature not specified in the publication
0.00013
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-(3-methoxyphenyl)-2-phenylacetamide
-
pH and temperature not specified in the publication
0.00014
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-(4-methoxyphenyl)-2-phenylacetamide
-
pH and temperature not specified in the publication
0.001
2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-N-[2-(dimethylamino)ethyl]-2-phenylacetamide
-
pH and temperature not specified in the publication
0.00198
2-[(2-carbamimidoyl-1-benzothiophen-6-yl)oxy]-2-(4-fluorophenyl)acetamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0000155
2-[(2-carbamimidoyl-6-fluoro-1-benzothiophen-4-yl)oxy]-2-phenylethyl phenylcarbamate
-
pH and temperature not specified in the publication
0.0000044
2-[(2-carbamimidoyl-6-fluoro-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-(aminomethyl)phenyl]carbamate
-
pH and temperature not specified in the publication
0.0000081
2-[(2-carbamimidoyl-6-fluoro-1-benzothiophen-4-yl)oxy]-2-phenylethyl [2-[(dimethylamino)methyl]phenyl]carbamate
-
pH and temperature not specified in the publication
0.0049
3-(1-[4-(1H-benzimidazol-1-yl)phenyl]-2-oxopyrrolidin-3-yl)-1-benzothiophene-5-carboximidamide
-
-
0.000028
3-(2-carbamimidoylbenzo[b]thiophen-6-yloxy)-3-(4-chlorophenyl)propionic acid methyl ester
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.000063
3-(2-[4-(1H-benzimidazol-1-yl)phenyl]-1-benzyl-2-oxoethyl)-1-benzothiophene-5-carboximidamide
-
-
0.000074
3-(4-aminophenyl)-N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)propanamide
-
-
0.000075
3-(4-aminophenyl)-N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)propanamide
-
-
0.0000027 - 0.0000138
3-[(7R)-7-[2-chloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamido]-2-methyl-7-phenyl-4a,6,7,8,9,10a-hexahydropyrido[1,2-a]indol-10-yl]propanoic acid
0.000059
3-[3-([4-(1H-benzimidazol-1-yl)phenyl]amino)-2-(5-carbamimidoyl-1H-indol-3-yl)-3-oxopropyl]benzoic acid
-
-
0.00066
4-(([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)methyl)-N-[5-(methylsulfonyl)-1H-benzimidazol-2-yl]benzamide
-
-
0.000036
4-(2-carbamimidoylbenzo[b]thiophen-6-yloxy)-4-(4-chlorophenyl) butyric acid methyl ester
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0015
4-(benzyloxy)-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00037
4-([[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy](phenyl)acetyl]amino)-N,N-dimethylbenzamide
-
pH and temperature not specified in the publication
2
4-cyano-2-fluoro-N-(10-hydroxy-2,7-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl)benzamide
-
pH and temperature not specified in the publication
0.0016
4-phenyl-1-benzothiophene-2-sulfinimidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00027
4-[phenyl(3-phenyl[1,2,4]oxadiazol-5-yl)methoxy]benzo[b]thiophene-2-carboxamidine
-
pH and temperature not specified in the publication
0.0059
5-(3,4-dimethoxyphenyl)benzo[b]thiophene-2-carboxamidine
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0019
5-(benzyloxy)-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.008
5-phenyl-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0216
6-(2-phenylethoxy)-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.000031
6-(3-chloro-4-fluorobenzyloxy)benzo[b]thiophene-2-carboxamidine
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00035
6-(pyridin-3-ylmethoxy)-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00035
6-(thiophen-2-ylmethoxy)benzo[b]thiophene-2-carboxamidine
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0038
6-benzyloxybenzo[b]thiophene-2-carboxamidine
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0072
6-[(2-chlorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.023
6-[(2-fluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0269
6-[(2-methoxybenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00045
6-[(3,4-difluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0009
6-[(3-chlorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00068
6-[(3-fluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00045
6-[(3-methoxybenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.000075
6-[(4-chloro-3-fluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00045
6-[(4-chlorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0007
6-[(4-fluorobenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00025
6-[(4-methoxybenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0009
6-[(4-methylbenzyl)oxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0113
6-[1-(4-fluorophenyl)ethoxy]-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00042
ethyl 1-[4-([[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy](phenyl)acetyl]amino)phenyl]-1H-imidazole-2-carboxylate
-
pH and temperature not specified in the publication
0.00853
ethyl 2-([2-(5-carbamimidoyl-1,1-dioxido-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
0.0019
ethyl 2-([2-(5-carbamimidoyl-1-benzofuran-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
0.00012
ethyl 2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
0.0119
ethyl [(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]acetate
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0038
ethyl [(2-carbamimidoyl-1-benzothiophen-6-yl)oxy]acetate
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.000011
ethyl [4-[([2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylethoxy]carbonyl)amino]-3,5-dimethyl-1H-pyrazol-1-yl]acetate
-
pH and temperature not specified in the publication
0.0005
methyl (1R)-2-(2-[2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
0.00028
methyl (1S,2R)-2-(2-[(2R)-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
0.0413
methyl (1S,2R)-2-(2-[(2S)-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
0.00031
methyl (1S,2R)-2-(2-[2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]hydrazino)cyclohexanecarboxylate
-
-
0.00014
methyl 2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
0.00034
methyl 2-([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxylate
-
-
0.0084
methyl 3-([[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy](phenyl)acetyl]amino)propanoate
-
pH and temperature not specified in the publication
0.0113
methyl 4-[[(2-carbamimidoyl-1-benzothiophen-6-yl)oxy]methyl]benzoate
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00002
methyl [(2-carbamimidoyl-1-benzothiophen-6-yl)oxy](4-chlorophenyl)acetate
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00004
methyl [(2-carbamimidoyl-1-benzothiophen-6-yl)oxy](4-fluorophenyl)acetate
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.00028
N-(2-amino-2-oxoethyl)-2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxamide
-
-
0.00027
N-(4-[3-([4-(1H-benzimidazol-1-yl)phenyl]amino)-2-(5-carbamimidoyl-1H-indol-3-yl)-3-oxopropyl]phenyl)benzamide
-
-
0.00078
N-1,3-benzothiazol-5-yl-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
0.0019
N-1H-benzimidazol-2-yl-3-([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)benzamide
-
-
0.00093
N-1H-benzimidazol-2-yl-4-([2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanoyl]amino)benzamide
-
-
0.032
N-benzyl-2-([2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanoyl]amino)cyclohexanecarboxamide
-
-
0.00039
N-benzyl-2-[(2-carbamimidoyl-1-benzothiophen-4-yl)oxy]-2-phenylacetamide
-
pH and temperature not specified in the publication
0.0000016
N-[(7S)-10-(5-aminopyridin-3-yl)-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
-
pH and temperature not specified in the publication
9
N-[2-(5,6-dimethyl-1H-benzimidazol-2-yl)ethyl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
pH and temperature not specified in the publication
0.00036
N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1-methyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
0.000063
N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-phenylpropanamide
-
-
0.0003
N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-2-(6-carbamimidoyl-1H-indol-1-yl)-3-phenylpropanamide
-
-
0.00023
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-naphthalen-1-ylpropanamide
-
-
0.000098
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)-3-phenylpropanamide
-
-
0.00024
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1-benzothiophen-3-yl)butanamide
-
-
0.00075
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-2-methylpropanamide
-
-
0.00013
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-(4-[(phenylsulfonyl)amino]phenyl)propanamide
-
-
0.0038
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-cyclohexylpropanamide
-
-
0.000098
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-naphthalen-2-ylpropanamide
-
-
0.0012
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-3-pyridin-3-ylpropanamide
-
-
0.00024
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)-4-phenylbutanamide
-
-
0.00016
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)butanamide
-
-
0.00048
N-[4-(1H-benzimidazol-1-yl)phenyl]-2-(5-carbamimidoyl-1H-indol-3-yl)propanamide
-
-
0.00013
N-[4-(1H-benzimidazol-2-yl)phenyl]-2-benzyl-3-(5-carbamimidoyl-1H-indol-3-yl)propanamide
-
-
0.00025
N-[4-(1H-benzimidazol-2-yl)phenyl]-3-(5-carbamimidoyl-1H-indol-3-yl)-4-phenylbutanamide
-
-
0.000021
[(2-carbamimidoyl-1-benzothiophen-6-yl)oxy](4-fluorophenyl)acetic acid
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0000063
1-(3-chloro-4-[[(2R)-2,8-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]carbamoyl]phenyl)-1H-benzimidazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0000105
1-(3-chloro-4-[[(2R)-2,8-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]carbamoyl]phenyl)-1H-benzimidazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0000348
1-(3-chloro-4-[[(2R)-2,8-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]carbamoyl]phenyl)-1H-benzimidazole-5-carboxylic acid
-
pH and temperature not specified in the publication
0.0000102
2,6-dichloro-N-[(2R)-10-hydroxy-2,7-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000121
2,6-dichloro-N-[(2R)-10-hydroxy-2,7-dimethyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000031
2,6-dichloro-N-[(2R)-2-(3-fluorophenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000066
2,6-dichloro-N-[(2R)-2-(3-fluorophenyl)-8-methyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000117
2,6-dichloro-N-[(3R)-3,7-dimethyl-2,3,4,9-tetrahydro-1H-carbazol-3-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0002676
2,6-dichloro-N-[(3R)-3,7-dimethyl-2,3,4,9-tetrahydro-1H-carbazol-3-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000021
2-chloro-N-[(2R)-8-methyl-2-phenyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000059
2-chloro-N-[(2R)-8-methyl-2-phenyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000069
2-chloro-N-[(2R)-8-methyl-2-phenyl-1,2,3,4-tetrahydropyrido[1,2-b]indazol-2-yl]-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
-
pH and temperature not specified in the publication
0.0000051
2-chloro-N-[(7S)-10-cyclopropyl-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
pH and temperature not specified in the publication
0.000008
2-chloro-N-[(7S)-10-cyclopropyl-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
pH and temperature not specified in the publication
0.0000084
2-chloro-N-[(7S)-10-cyclopropyl-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
pH and temperature not specified in the publication
0.0000024
2-chloro-N-[(7S)-10-[(E)-(hydroxyimino)methyl]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
pH and temperature not specified in the publication
0.0000029
2-chloro-N-[(7S)-10-[(E)-(hydroxyimino)methyl]-2-methyl-7-phenyl-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
pH and temperature not specified in the publication
0.0000026
2-chloro-N-[(7S)-2-methyl-7-phenyl-10-(2,2,2-trifluoro-1-hydroxyethyl)-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
pH and temperature not specified in the publication
0.0000055
2-chloro-N-[(7S)-2-methyl-7-phenyl-10-(2,2,2-trifluoro-1-hydroxyethyl)-6,7,8,9-tetrahydropyrido[1,2-a]indol-7-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
-
pH and temperature not specified in the publication
0.0000027
3-[(7R)-7-[2-chloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamido]-2-methyl-7-phenyl-4a,6,7,8,9,10a-hexahydropyrido[1,2-a]indol-10-yl]propanoic acid
-
pH and temperature not specified in the publication
0.0000138
3-[(7R)-7-[2-chloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamido]-2-methyl-7-phenyl-4a,6,7,8,9,10a-hexahydropyrido[1,2-a]indol-10-yl]propanoic acid
-
pH and temperature not specified in the publication
0.0008
6-(3,4-dimethoxyphenyl)-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.0242
6-(3,4-dimethoxyphenyl)-1-benzothiophene-2-carboximidamide
-
in 50 mM Tris, 100 mM NaCl, 5 mM CaCl2, 0.5% (w/v) PEG6000 (pH 7.4), at 22°C
0.119
Na+
wild type enzyme FIXa, in the presence of 185 mM Na+ and 5 mM Ca2+
0.179
Na+
mutant enzyme FIXagamma225P, in the presence of 185 mM Na+ and 5 mM Ca2+
0.0000025
supersulfated low molecular weight heparin
-
mutant enzyme R170A, using factor X as substrate, at pH 7.4, 22°C
-
0.000003
supersulfated low molecular weight heparin
-
wild type enzyme, using factor X as substrate, at pH 7.4, 22°C
-
0.0000039
supersulfated low molecular weight heparin
-
mutant enzyme N178A, using factor X as substrate, at pH 7.4, 22°C
-
0.0000042
supersulfated low molecular weight heparin
-
mutant enzyme N129A, using factor X as substrate, at pH 7.4, 22°C
-
0.00001
supersulfated low molecular weight heparin
-
mutant enzyme K132A, using factor X as substrate, at pH 7.4, 22°C
-
0.000017
supersulfated low molecular weight heparin
-
mutant enzyme R165A, using factor X as substrate, at pH 7.4, 22°C
-
0.000072
supersulfated low molecular weight heparin
-
mutant enzyme K126A, using factor X as substrate, at pH 7.4, 22°C
-
0.00017
supersulfated low molecular weight heparin
-
mutant enzyme R233A, using factor X as substrate, at pH 7.4, 22°C
-
0.00001
unmodified low molecular weight heparin
-
mutant enzyme N129A, using factor X as substrate, at pH 7.4, 22°C
-
0.000012
unmodified low molecular weight heparin
-
mutant enzyme R170A, using factor X as substrate, at pH 7.4, 22°C
-
0.000012
unmodified low molecular weight heparin
-
wild type enzyme, using factor X as substrate, at pH 7.4, 22°C
-
0.0000141
unmodified low molecular weight heparin
-
mutant enzyme N178A, using factor X as substrate, at pH 7.4, 22°C
-
0.000049
unmodified low molecular weight heparin
-
mutant enzyme K132A, using factor X as substrate, at pH 7.4, 22°C
-
0.00016
unmodified low molecular weight heparin
-
mutant enzyme R165A, using factor X as substrate, at pH 7.4, 22°C
-
0.00032
unmodified low molecular weight heparin
-
mutant enzyme K126A, using factor X as substrate, at pH 7.4, 22°C
-
0.00147
unmodified low molecular weight heparin
-
mutant enzyme R233A, using factor X as substrate, at pH 7.4, 22°C
-
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
0.0022
2-chloro-N-[3-methyl-1-(4-methyl-2-nitrophenyl)pyrrolidin-3-yl]-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000047
N-[(3R)-1-(3-amino-4,5-dichloro-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000032
N-[(3R)-1-(3-amino-4-chloro-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000036
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1-methyl-2-oxo-1,2-dihydropyrimidin-5-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000015
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1-methyl-5-oxo-1,5-dihydro-4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000018
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1-methyl-6-oxo-1,6-dihydropyridin-3-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000013
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(1H-imidazo[4,5-b]pyridin-1-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000033
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(3-methyl-1H-1,2,4-triazol-1-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000031
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.003
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(pyrimidin-2-yl)benzamide
Homo sapiens
IC50 above 0.003 mM, at pH 8.0 and 25°C
0.000026
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(pyrimidin-5-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000045
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-[3-(difluoromethyl)-4H-1,2,4-triazol-4-yl]benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000013
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-[4-(2-hydroxyethyl)-1H-imidazol-1-yl]benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000032
N-[(3R)-1-(3-amino-4-chloro[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-4-(1H-benzimidazol-1-yl)-2-chlorobenzamide
Homo sapiens
at pH 8.0 and 25°C
0.000172
N-[(3R)-1-(3-amino-4-fluoro-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000041
N-[(3R)-1-(3-amino-5-methyl[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000098
N-[1-(3-amino-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000018 - 0.000062
N-[1-(3-amino-5-methyl-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
0.000089
N-[1-(3-amino[1,2]oxazolo[5,4-c]pyridin-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.000018
N-[1-(3-amino-5-methyl-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
0.00005
N-[1-(3-amino-5-methyl-1,2-benzoxazol-7-yl)pyrrolidin-3-yl]-2-chloro-4-(4H-1,2,4-triazol-4-yl)benzamide
Homo sapiens
at pH 8.0 and 25°C
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
-
relative coagulation and amidolytic activities of recombinant wild-type and mutant enzymes, 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
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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
-
-
-
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
-
factor IXa binds specifically to the surface of endothelial cells
brenda
additional information
-
binding of a subpopulation of platelets to the enzyme is activated by the protease-activated receptor-1, PAR-1, requirring both release of calcium from internal stores and influx of extracellular calcium, overview
brenda
factor IX circulates in plasma as a single chain inactive zymogen
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
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
factor IXa is a critical enzyme for the formation of stable blood clots
malfunction
-
hemophilia B is an inherited X-linked recessive bleeding disorder, due to a defect in human factor IX
Show AA Sequence and Transmembrane Helices (1176 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
44000
57000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
the fully active enzyme consists of a light and a heavy chain held together by a single disulfie bond
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
activation by purified factor X activator from the venom of Russells Vipe cleaving fIX after Arg180 to generate active enzyme fIXaalpha
proteolytic modification
proteolytic cleavages at two peptide bonds after Arg145 and Arg180 by either one of two physiological activators, the factor VIIa-tissue factor complex or factor XIa, leads to removal of the activation peptide and conversion of fIX to a fully active enzyme consisting of a light and a heavy chain held together by a single disulfie bond
proteolytic modification
-
purified factor IX is activated with human factor XIa
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
activated mutant K98T, sitting drop vapor diffusion method, using 0.1 M MES (pH 6.5) and 18-24% (w/v) PEG6000
hanging drop vapor diffusion method, using 0.25 M ammonium acetate, 19.5% (w/v) PEG 3350
of a recombinant two-domain construct of fIXa in complex with p-benzamidine. The 99-loop on Tyr99 plays a major role in substrate interaction, it may be rearranged in the factor X activation complex
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D47G
-
factor IXaAL, causes lower rates of factor X activation, Asp47 and the cleavage of Arg145-Ala146 are important structural features required for specific, high affinity factor IXa binding to platelets in the presence of factors VIIIa and factor X
E186A
site-directed mutagenesis, the fIXa mutant exhibits normal activity towards a fIXa-specific chromogenic substrate in the presence of Ca2+ with no obvious requirement for Na+ in the reaction, the mutant interacts with factor VIIIa with near normal affinity and catalyzes the activation of factor X in the intrinsic Xase complex with a normal catalytic efficiency
E410A
-
the mutant shows reduced hydrolytic activity and increased in-vitro clotting activity compared to the wild type enzyme
E410H
-
the mutant with reduced hydrolytic activity and increased in-vitro clotting activity has 2.5fold enhanced affinity for the cofactor FVIIIa and induces 5.2fold higher thrombin generation compared to the wild type enzyme
E410L
-
the mutant shows reduced hydrolytic activity and increased in-vitro clotting activity compared to the wild type enzyme
E410N
-
the mutant shows reduced hydrolytic activity and increased in-vitro clotting activity compared to the wild type enzyme
Gla-domainless factor IXa
20000times lower kacat for factor X hydrolysis than wild-type
H185A
site-directed mutagenesis, the fIXa mutant exhibits normal activity towards a fIXa-specific chromogenic substrate in the presence of Ca2+ with no obvious requirement for Na+ in the reaction, the mutant interacts with factor VIIIa with near normal affinity and catalyzes the activation of factor X in the intrinsic Xase complex with a normal catalytic efficiency
K126A
K132A
K265A
-
no change in binding of anti fIX monoclonal antibodies CLB-fIX 14 and CLB-fIX 13
K98T
the variant demonstrates a 2fold improvement in kcat/KM value for Pefa9 as compared to the wild type enzyme
K98T/R150A/I213V
the mutations result in a 4fold increase in kinetic efficiency compared with the wild type enzyme
N129A
N178A
N346D
-
no change in binding of anti fIX monoclonal antibodies CLB-fIX 14, no binding of anti fIX monoclonal antibody CLB-fIX 13
R143A
4times lower kcat for factor X hydrolysis than wild-type Gla-domainless factor IXa
R145H
-
factor IXaCH, causes lower rates of factor X activation, Asp47 and the cleavage of Arg145-Ala146 are important structural features required for specific, high affinity factor IXa binding to platelets in the presence of factors VIIIa and factor X
R147A
3times lower kcat for factor X hydrolysis than wild-type Gla-domainless factor IXa
R150
similar kcat for factor X hydrolysis as wild-type Gla-domainless factor IXa
R150A
the mutation reduces potential autolysis in the 148-loop during production and leads to reduced activity compared to the wild type enzyme
R150A/I213V
the variant shows increases in the catalytic efficiency for amidolytic activity when the target substrate is either Pefa9 or Pefa10 with 1.5fold and 1.2fold increases, respectively
R165A
R170A
-
the mutation slightly (0.5fold) reduces supersulfated low molecular weight heparin affinity
R188A
site-directed mutagenesis, the fIXa mutant exhibits normal activity towards a fIXa-specific chromogenic substrate in the presence of Ca2+ with no obvious requirement for Na+ in the reaction, the mutant interacts with factor VIIIa with near normal affinity and catalyzes the activation of factor X in the intrinsic Xase complex with a normal catalytic efficiency
R233A
-
the mutation dramatically (14fold) reduces supersulfated low molecular weight heparin affinity
rFIXa104A
recombinant FIXa alanine point mutation in loop 2 of the EGF2 domain
rFIXa105A
recombinant FIXa alanine point mutation in loop 2 of the EGF2 domain
rFIXa107A
recombinant FIXa alanine point mutation in loop 2 of the EGF2 domain
rFIXa89A
recombinant FIXa alanine point mutation in loop 1 of the EGF2 domain
rFIXa90A
recombinant FIXa alanine point mutation in loop 1 of the EGF2 domain
rFIXa91A
recombinant FIXa alanine point mutation in loop 1 of the EGF2 domain
rFIXa94A
recombinant FIXa alanine point mutation in loop 1 of the EGF2 domain
V16I/I21/V R150A
the variant results in a negligible increase in activity compared with the V16I/R150A variant
V16I/K98T/I213V
the mutations result in a 4fold increase in kinetic efficiency compared with the wild type enzyme
V16I/K98T/I213V/R150A
the mutations result in a 6fold increase in kinetic efficiency compared with the wild type enzyme
V16I/K98T/R150A
the mutant shows enhancements in activity leading to a 2.5fold increased kinetic efficiency compared with the wild type enzyme
V16I/K98T/Y177T/I213V
the variant reduces the kinetic efficiency to the 4fold increase that is also observed with the K98T/R150A/I213V variant
V16I/R150A
the variant shows no increase in the kcat/KM value for Pefa9 as compared to the wild type enzyme
Y94F/A95aK/K98T/Y177F/I213V/E219G
-
about 6fold increased catalytic efficence compared to plasma-derived activated coagulation factor IX, higher clotting activity than wild type FIXa
Y94F/K98T
-
increased catalytic efficence compared to plasma-derived activated coagulation factor IX, higher clotting activity than wild type FIXa
Y94F/K98T/Y177F
-
increased catalytic efficence compared to plasma-derived activated coagulation factor IX, higher clotting activity than wild type FIXa
Y94F/K98T/Y177F/I213V/E219G
-
about 17fold increased catalytic efficence compared to plasma-derived activated coagulation factor IX, higher clotting activity than wild type FIXa
additional information
K126A
-
site-directed mutagenesis, mutation in the heparin-binding exosite, the mutant shows reduced activity and altered tenase complex formation kinetics compared to the wild-type enzyme
K126A
-
the mutation dramatically (11fold) reduces supersulfated low molecular weight heparin affinity
K132A
-
site-directed mutagenesis, surface residue mutation, the mutant shows reduced activity and altered tenase complex formation kinetics compared to the wild-type enzyme
K132A
-
the mutation dramatically (20fold) reduces supersulfated low molecular weight heparin affinity
N129A
-
site-directed mutagenesis, surface residue mutation, the mutant shows reduced activity and altered tenase complex formation kinetics compared to the wild-type enzyme
N129A
-
the mutation moderately (5fold) reduces supersulfated low molecular weight heparin affinity
N178A
-
site-directed mutagenesis, mutation in the heparin-binding exosite, the mutant shows reduced activity and altered tenase complex formation kinetics compared to the wild-type enzyme
N178A
-
the mutant shows wild type affinity towards supersulfated low molecular weight heparin
R165A
-
site-directed mutagenesis, mutation in the heparin-binding exosite, the mutant shows reduced activity and altered tenase complex formation kinetics compared to the wild-type enzyme
R165A
-
the mutation moderately (5fold) reduces supersulfated low molecular weight heparin affinity
additional information
the modulatory effect of heparin can be completely abrogated by mutating a single amino acid residue in the 99-loop region of the extended fIXa active site cleft outside of the heparin binding exosite, overview
additional information
-
an FIXa/FXa chimera in which the 39-loop of the protease is replaced with the corresponding loop of FXa cleaves a FIXa-specific chromogenic substrate with normal catalytic efficiency, however, the mutant exhibits about 5fold enhanced reactivity with antothrombin specifically in the absence of the cofactor, heparin. The FIXa mutant activates factor X with about 4fold decreased kcat and about 2fold decreased Km, although the mutant interacts normally with factor VIIIa
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.05 M imidazole buffer, pH 6.0, 0.2 M NaCl, no loss of activity after several months
-
22°C, recombinant human FIX in soybean seeds, 6 years, no loss of activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
heparin Sepharose column chromatography and Q Sepharose column chromatography
Q-Sepharose of column, affinity purification with heparin sepharose, gel filtration
recombinant wild-type and mutant enzymes from HEK-293 cells by anion exchange and heparin affinity chromatography
recombinant wild-type and mutant enzymes from HEK-293 cells by immunoaffinity and anion exchange chromatogaphy
recombinant wild-type and mutant factor IXa, immunoaffinity chromatography using HPC4 monoclonal antibodies
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
target of therapy in thrombotic disorders, application of a complementary oliconucleotide antidote to RB006, a aptamer-based inhibitor to factor IXa, return factor IX activity to its baseline levels
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujikawa, K.; Legaz, M.E.; Kato, H.; Davie, E.W.
The mechanism of activation of bovine factor IX (Christmas factor) by bovine factor XIa (activated plasma thromboplastin antecedent)
Biochemistry
13
4508-4516
1974
Bos taurus
brenda
Thompson, A.R.
Structure, function and molecular defects of factor IX
Blood
67
565-572
1986
Homo sapiens
brenda
Van Dieijen, G.; Janssen-Claessen, T.
Purification of coagulation factors and preparation of reagents for chromogenic substrate assays
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
390-394
1986
Bos taurus
-
brenda
Osterud, B.; Bouma, B.N.; Griffin, J.H.
Human blood coagulation factor IX
J. Biol. Chem.
253
5946-5951
1978
Homo sapiens
brenda
Sturzebecher, J.; Kopetzki, E.; Bode, W.; Hopfner, K.P.
Dramatic enhancement of the catalytic activity of coagulation factor IXa by alcohols
FEBS Lett.
412
295-300
1997
Homo sapiens
brenda
Morita, T.; Fukudome, K.; Miyata, T.; Iwanaga, S.
gamma-Carboxylglutamic acid (Gla)-domainless blood coagulation factor IXa species: preparation and properties
J. Biochem.
110
990-996
1991
Bos taurus
brenda
London, F.S.; Walsh, P.N.
Zymogen factor IX potentiates factor IXa-catalyzed activation
Biochemistry
39
9850-9858
2000
Homo sapiens
brenda
Hopfner, K.P.; Lang, A.; Karcher, A.; Sichler, K.; Kopetzki, E.; Barndstetter, H.; Huber, R.; Bode, W.; Engh, R.A.
Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding
Structure Fold. Des.
7
989-996
1999
Homo sapiens
brenda
Fay, P.J.; Koshibu, K.; Mastri, M.
The A1 and the A2 subunits of factor VIIIa synergistically stimulate factor IXa catalytic activity
J. Biol. Chem.
274
15401-15406
1999
Homo sapiens
brenda
Ahmed, S.S.; Rawala-Sheikh, R.; Monroe, D.M.; Roberts, H.R.; Walsh, P.N.
Comparative platelet binding and kinetic studies with normal and variant factor IXa molecules
J. Biol. Chem.
265
20907-20911
1990
Homo sapiens
brenda
Blostein, M.D.; Rigby, A.C.; Furie, B.C.; Furie, B.; Gilbert, G.E.
Amphipathic helices support function of blood coagulation factor IXa
Biochemistry
39
12000-12006
2000
Homo sapiens
brenda
Falls, L.A.; Furie, B.; Furie, B.C.
Role of phosphatidylethanolamine in assembly and function of the factor IXa-factor VIIIa complex on membrane surfaces
Biochemistry
39
13216-13222
2000
Homo sapiens
brenda
Ahmad, S.S.; Walsh, P.N.
Coordinate binding studies of the substrate (factor X) with the cofactor (factor VIII) in the assembly of the factor X activating complex on the activated platelet surface
Biochemistry
41
11269-11276
2002
Homo sapiens
brenda
Bedsted, T.; Swanson, R.; Chuang, Y.J.; Bock, P.E.; Bjork, I.; Olson, S.T.
Heparin and calcium ions dramatically enhance antithrombin reactivity with factor IXa by generating new interaction exosites
Biochemistry
42
8143-8152
2003
Homo sapiens
brenda
Bajaj, S.P.; Schmidt, A.E.; Mathur, A.; Padmanabhan, K.; Zhong, D.; Mastri, M.; Fay, P.J.
Factor IXa:factor VIIIa interaction. helix 330-338 of factor ixa interacts with residues 558-565 and spatially adjacent regions of the a2 subunit of factor VIIIa
J. Biol. Chem.
276
16302-16309
2001
Homo sapiens (P00740)
brenda
Wilkinson, F.H.; London, F.S.; Walsh, P.N.
Residues 88-109 of factor IXa are important for assembly of the factor X activating complex
J. Biol. Chem.
277
5725-5733
2002
Homo sapiens
brenda
Yang, L.; Manithody, C.; Olson, S.T.; Rezaie, A.R.
Contribution of basic residues of the autolysis loop to the substrate and inhibitor specificity of factor IXa
J. Biol. Chem.
278
25032-25038
2003
Homo sapiens (P00740)
brenda
Blostein, M.D.; Furie, B.C.; Rajotte, I.; Furie, B.
The Gla domain of factor IXa binds to factor VIIIa in the tenase complex
J. Biol. Chem.
278
31297-31302
2003
Homo sapiens
brenda
Wiebe, E.M.; Stafford, A.R.; Fredenburgh, J.C.; Weitz, J.I.
Mechanism of catalysis of inhibition of factor IXa by antithrombin in the presence of heparin or pentasaccharide
J. Biol. Chem.
278
35767-35774
2003
Homo sapiens
brenda
Rohlena, J.; Kolkman, J.A.; Boertjes, R.C.; Mertens, K.; Lenting, P.J.
Residues Phe342-Asn346 of activated coagulation factor IX contribute to the interaction with low density lipoprotein receptor-related protein
J. Biol. Chem.
278
9394-9401
2003
Homo sapiens
brenda
Rusconi, C.P.; Scardino, E.; Layzer, J.; Pitoc, G.A.; Ortel, T.L.; Monroe, D.; Sullenger, B.A.
RNA aptamers as reversible antagonists of coagulation factor IXa
Nature
419
90-94
2002
Homo sapiens
brenda
Panteleev, M.A.; Saenko, E.L.; Ananyeva, N.M.; Ataullakhanov, F.I.
Kinetics of Factor X activation by the membrane-bound complex of Factor IXa and Factor VIIIa
Biochem. J.
381
779-794
2004
Homo sapiens
brenda
Yang, X.; Walsh, P.N.
An ordered sequential mechanism for Factor IX and Factor IXa binding to platelet receptors in the assembly of the Factor X-activating complex
Biochem. J.
390
157-167
2005
Homo sapiens
brenda
Neuenschwander, P.F.
Exosite occupation by heparin enhances the reactivity of blood coagulation factor IXa
Biochemistry
43
2978-2986
2004
Homo sapiens
brenda
Batt, D.G.; Qiao, J.X.; Modi, D.P.; Houghton, G.C.; Pierson, D.A.; Rossi, K.A.; Luettgen, J.M.; Knabb, R.M.; Jadhav, P.K.; Wexler, R.R.
5-Amidinoindoles as dual inhibitors of coagulation factors IXa and Xa
Bioorg. Med. Chem. Lett.
14
5269-5273
2004
Homo sapiens
brenda
Qiao, J.X.; Cheng, X.; Modi, D.P.; Rossi, K.A.; Luettgen, J.M.; Knabb, R.M.; Jadhav, P.K.; Wexler, R.R.
5-Amidinobenzo[b]thiophenes as dual inhibitors of factors IXa and Xa
Bioorg. Med. Chem. Lett.
15
29-35
2005
Homo sapiens
brenda
Lu, G.; Broze, G.J.; Krishnaswamy, S.
Formation of factors IXa and Xa by the extrinsic pathway: differential regulation by tissue factor pathway inhibitor and antithrombin III
J. Biol. Chem.
279
17241-17249
2004
Homo sapiens
brenda
Butenas, S.; Orfeo, T.; Gissel, M.T.; Brummel, K.E.; Mann, K.G.
The significance of circulating factor IXa in blood
J. Biol. Chem.
279
22875-22882
2004
Homo sapiens
brenda
Yang, X.; Chang, Y.J.; Lin, S.W.; Walsh, P.N.
Identification of residues Asn89, Ile90, and Val107 of the factor IXa second epidermal growth factor domain that are essential for the assembly of the factor X-activating complex on activated platelets
J. Biol. Chem.
279
46400-46405
2004
Homo sapiens (P00740)
brenda
Schmidt, A.E.; Stewart, J.E.; Mathur, A.; Krishnaswamy, S.; Bajaj, S.P.
Na+ site in blood coagulation factor IXa: effect on catalysis and factor VIIIa binding
J. Mol. Biol.
350
78-91
2005
Homo sapiens (P00740)
brenda
Ndonwi, M.; Broze, G.; Bajaj, S.P.
The first epidermal growth factor-like domains of factor Xa and factor IXa are important for the activation of the factor VII-tissue factor complex
J. Thromb. Haemost.
3
112-118
2005
Homo sapiens
brenda
London, F.S.; Marcinkiewicz, M.; Walsh, P.N.
PAR-1-stimulated factor IXa binding to a small platelet subpopulation requires a pronounced and sustained increase of cytoplasmic calcium
Biochemistry
45
7289-7298
2006
Homo sapiens
brenda
Misenheimer, T.M.; Buyue, Y.; Sheehan, J.P.
The heparin-binding exosite is critical to allosteric activation of factor IXa in the intrinsic tenase complex: the role of arginine 165 and factor X
Biochemistry
46
7886-7895
2007
Homo sapiens
brenda
Neuenschwander, P.F.; Williamson, S.R.; Nalian, A.; Baker-Deadmond, K.J.
Heparin modulates the 99-loop of factor IXa: effects on reactivity with isolated Kunitz-type inhibitor domains
J. Biol. Chem.
281
23066-23074
2006
Homo sapiens (P00740)
brenda
Gale, A.J.; Radtke, K.P.; Cunningham, M.A.; Chamberlain, D.; Pellequer, J.L.; Griffin, J.H.
Intrinsic stability and functional properties of disulfide bond-stabilized coagulation factor VIIIa variants
J. Thromb. Haemost.
4
1315-1322
2006
Homo sapiens
brenda
Scheiflinger, F.; Dockal, M.; Rosing, J.; Kerschbaumer, R.J.
Enhancement of the enzymatic activity of activated coagulation factor IX by anti-factor IX antibodies
J. Thromb. Haemost.
6
315-322
2008
Homo sapiens
brenda
Yang, L.; Gopalakrishna, K.; Manithody, C.; Rezaie, A.R.
Expression, purification and characterization of factor IX derivatives using a novel vector system
Protein Expr. Purif.
50
196-202
2006
Homo sapiens (P00740)
brenda
Gopalakrishna, K.; Rezaie, A.R.
The influence of sodium ion binding on factor IXa activity
Thromb. Haemost.
95
936-941
2006
Homo sapiens
brenda
Zoegg, T.; Brandstetter, H.
Activation mechanisms of coagulation factor IX
Biol. Chem.
390
391-400
2009
Homo sapiens
brenda
Yang, Y.H.; Chien, D.; Wu, M.; FitzGerald, J.; Grossman, J.M.; Hahn, B.H.; Hwang, K.K.; Chen, P.P.
Novel autoantibodies against the activated coagulation factor IX (FIXa) in the antiphospholipid syndrome that interpose the FIXa regulation by antithrombin
J. Immunol.
182
1674-1680
2009
Homo sapiens
brenda
Becker, R.C.; Oney, S.; Becker, K.C.; Sullenger, B.
Antidote-controlled antithrombotic therapy targeting factor IXa and von Willebrand factor
Ann. N. Y. Acad. Sci.
1175
61-70
2009
Homo sapiens
brenda
Gettins, P.G.; Olson, S.T.
Activation of antithrombin as a factor IXa and Xa inhibitor involves mitigation of repression rather than positive enhancement
FEBS Lett.
583
3397-3400
2009
Homo sapiens
brenda
Kim, W.H.; Kim, J.S.; Kim, J.S.; Yoon, Y.; Lee, G.M.
Effect of Ca2+ and Mg2+ concentration in culture medium on the activation of recombinant factor IX produced in Chinese hamster ovary cells
J. Biotechnol.
142
275-278
2009
Homo sapiens
brenda
Hartmann, R.; Dockal, M.; Kammlander, W.; Panholzer, E.; Nicolaes, G.A.; Fiedler, C.; Rosing, J.; Scheiflinger, F.
Factor IX mutants with enhanced catalytic activity
J. Thromb. Haemost.
7
1656-1662
2009
Homo sapiens
brenda
Zgg, T.; Brandstetter, H.
Structural basis of the cofactor- and substrate-assisted activation of human coagulation factor IXa
Structure
17
1669-1678
2009
Homo sapiens (P00740), Homo sapiens
brenda
Hosseini, S.; Zomorodipour, A.; Jalal, R.; Sabouni, F.; Ataei, F.
A study of the expression of functional human coagulation factor IX in keratinocytes using a nonviral vector regulated by K14 promoter
Appl. Biochem. Biotechnol.
162
1599-1611
2010
Homo sapiens
brenda
Misenheimer, T.M.; Sheehan, J.P.
The regulation of factor IXa by supersulfated low molecular weight heparin
Biochemistry
49
9997-10005
2010
Homo sapiens
brenda
Yang, L.; Manithody, C.; Qureshi, S.H.; Rezaie, A.R.
Role of the residues of the 39-loop in determining the substrate and inhibitor specificity of factor IXa
J. Biol. Chem.
285
28488-28495
2010
Homo sapiens
brenda
Wang, S.; Beck, R.; Blench, T.; Burd, A.; Buxton, S.; Malic, M.; Ayele, T.; Shaikh, S.; Chahwala, S.; Chander, C.; Holland, R.; Merette, S.; Zhao, L.; Blackney, M.; Watts, A.
Studies of benzothiophene template as potent factor IXa (FIXa) inhibitors in thrombosis
J. Med. Chem.
53
1465-1472
2010
Homo sapiens
brenda
Wang, S.; Beck, R.; Burd, A.; Blench, T.; Marlin, F.; Ayele, T.; Buxton, S.; Dagostin, C.; Malic, M.; Joshi, R.; Barry, J.; Sajad, M.; Cheung, C.; Shaikh, S.; Chahwala, S.; Chander, C.; Baumgartner, C.; Holthoff, H.P.; Murray, E.; Blackney, M.; Giddings, A.
Structure based drug design: development of potent and selective factor IXa (FIXa) inhibitors
J. Med. Chem.
53
1473-1482
2010
Homo sapiens
brenda
Chang, L.; Yang, C.; Chua, A.; Lin, Y.; Lai, S.
Sustained release of transgenic human factor IX: Preparation, characterization, and in vivo efficacy
Mol. Pharm.
8
1767-1774
2011
Homo sapiens
brenda
Johnson, D.J.; Langdown, J.; Huntington, J.A.
Molecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-A structure of the ternary complex
Proc. Natl. Acad. Sci. USA
107
645-650
2010
Homo sapiens (P00740)
brenda
Wu, H.; Xu, X.; Zhang, L.; Shen, D.; Peng, L.; Zhang, Y.; Song, J.
Mg(II)-induced binding of factor IX-binding protein from the venom of Agkistrodon Halys Pallas with factor Xa
Toxicon
55
1358-1364
2010
Homo sapiens
brenda
Cunha, N.; Murad, A.; Ramos, G.; Maranhao, A.; Brgido, M.; Araujo, A.; Lacorte, C.; Aragao, F.; Covas, D.; Fontes, A.; Souza, G.; Vianna, G.; Rech, E.
Accumulation of functional recombinant human coagulation factor IX in transgenic soybean seeds
Transgenic Res.
20
841-855
2011
Homo sapiens (P00740), Homo sapiens
brenda
Venkateswarlu, D.
Structural insights into the interaction of blood coagulation co-factor VIIIa with factor IXa: a computational protein-protein docking and molecular dynamics refinement study
Biochem. Biophys. Res. Commun.
452
408-414
2014
Homo sapiens
brenda
Branchini, A.; Campioni, M.; Mazzucconi, M.; Biondo, F.; Mari, R.; Bicocchi, M.; Bernardi, F.; Pinotti, M.
Replacement of the Y450 (c234) phenyl ring in the carboxyl-terminal region of coagulation factor IX causes pleiotropic effects on secretion and enzyme activity
FEBS Lett.
587
3249-3253
2013
Homo sapiens
brenda
Sullenger, B.; Woodruff, R.; Monroe, D.M.
Potent anticoagulant aptamer directed against factor IXa blocks macromolecular substrate interaction
J. Biol. Chem.
287
12779-12786
2012
Homo sapiens
brenda
Geng, Y.; Verhamme, I.M.; Messer, A.; Sun, M.F.; Smith, S.B.; Bajaj, S.P.; Gailani, D.
A sequential mechanism for exosite-mediated factor IX activation by factor XIa
J. Biol. Chem.
287
38200-38209
2012
Homo sapiens
brenda
Yang, L.; Rezaie, A.R.
Residues of the 39-loop restrict the plasma inhibitor specificity of factor IXa
J. Biol. Chem.
288
12692-12698
2013
Bos taurus, Mus musculus
brenda
Bloem, E.; Meems, H.; van den Biggelaar, M.; Mertens, K.; Meijer, A.B.
A3 domain region 1803-1818 contributes to the stability of activated factor VIII and includes a binding site for activated factor IX
J. Biol. Chem.
288
26105-26111
2013
Homo sapiens
brenda
Wakabayashi, H.; Fay, P.J.
Replacing the factor VIII C1 domain with a second C2 domain reduces factor VIII stability and affinity for factor IXa
J. Biol. Chem.
288
31289-31297
2013
Homo sapiens
brenda
Neuenschwander, P.F.; Deadmond, K.J.; Zepeda, K.; Rutland, J.
Correlation of factor IXa subsite modulations with effects on substrate discrimination
J. Thromb. Haemost.
10
382-389
2012
Homo sapiens
brenda
Majumder, R.; Koklic, T.; Sengupta, T.; Cole, D.; Chattopadhyay, R.; Biswas, S.; Monroe, D.; Lentz, B.R.
Soluble phosphatidylserine binds to two sites on human factor IXa in a Ca2+ dependent fashion to specifically regulate structure and activity
PLoS ONE
9
e100006
2014
Homo sapiens
brenda
Kristensen, L.H.; Olsen, O.H.; Blouse, G.E.; Brandstetter, H.
Releasing the brakes in coagulation factor IXa by co-operative maturation of the substrate-binding site
Biochem. J.
473
2395-2411
2016
Homo sapiens (P00740)
brenda
Meng, D.; Andre, P.; Bateman, T.J.; Berger, R.; Chen, Y.H.; Desai, K.; Dewnani, S.; Ellsworth, K.; Feng, D.; Geissler, W.M.; Guo, L.; Hruza, A.; Jian, T.; Li, H.; Metzger, J.; Parker, D.L.; Reichert, P.; Sherer, E.C.; Smith, C.J.; Sonatore, L.M.; Tschirret-Guth, R.; Wu, J.; Xu, J.; Zhang, T.; Campeau, L.C.; Orr,
Development of a novel tricyclic class of potent and selective FIXa inhibitors
Bioorg. Med. Chem. Lett.
25
5437-5443
2015
Homo sapiens
brenda
Sakurada, I.; Endo, T.; Hikita, K.; Hirabayashi, T.; Hosaka, Y.; Kato, Y.; Maeda, Y.; Matsumoto, S.; Mizuno, T.; Nagasue, H.; Nishimura, T.; Shimada, S.; Shinozaki, M.; Taguchi, K.; Takeuchi, K.; Yokoyama, T.; Hruza, A.; Reichert, P.; Zhang, T.; Wood, H.B.; Nakao, K.; Furusako, S.
Discovery of novel aminobenzisoxazole derivatives as orally available factor IXa inhibitors
Bioorg. Med. Chem. Lett.
27
2622-2628
2017
Homo sapiens (P00740)
brenda
Kitazawa, T.; Shima, M.
Emicizumab, a humanized bispecific antibody to coagulation factors IXa and X with a factor VIIIa-cofactor activity
Int. J. Hematol.
111
20-30
2018
Homo sapiens
brenda
Perot, E.; Enjolras, N.; Le Quellec, S.; Indalecio, A.; Girard, J.; Negrier, C.; Dargaud, Y.
Expression and characterization of a novel human recombinant factor IX molecule with enhanced in vitro and in vivo clotting activity
Thromb. Res.
135
1017-1024
2015
Homo sapiens
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.4.21.22)
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
