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Information on EC 3.4.21.22 - coagulation factor IXa
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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 enzyme appears in viruses and cellular organisms
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, 
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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
-
-
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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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
37316-87-3
-
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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
-
-
?
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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
-
-
?
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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
-
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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+
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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-