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Information on EC 3.4.21.38 - coagulation factor XIIa
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3.4.21.38 coagulation factor XIIaSpecify your search results
Word Map
- 3.4.21.38
- kininogen
- clot
- platelet
- thrombin
- thrombosis
- plasminogen
- bradykinin
-
anticoagulant
-
bleeding
- thromboplastin
-
fibrinolysis
- fibrinogen
- prothrombin
- hereditary
- heparin
- fibrin
- antithrombin
- plasmin
- kinin
-
procoagulant
- angioedema
-
hemostasis
- viii
-
kallikrein-kinin
-
amidolytic
-
autoactivation
- zymogen
- willebrand
- kaolin
-
thromboembolic
-
antithrombotic
- c1-inhibitor
- fxia
-
d-dimers
-
c1-inh
- hypercoagulability
-
antiphospholipid
-
thrombin-antithrombin
- c1s
-
fletcher
-
2-antiplasmin
-
fibrinopeptide
-
euglobulins
- c1-esterase
- thrombophilia
- synthesis
- drug development
- medicine
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recalcification
-
recalcified
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blood-contacting
-
bradykinin-mediated
- icatibant
The enzyme appears in viruses and cellular organisms
Reaction Schemes
selective cleavage of Arg-/-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa
Synonyms
factor xii, hageman factor, fxiia, factor xiia, coagulation factor xii, activated factor xii, prekallikrein activator, beta-factor xiia, blood coagulation factor xii, coagulation factor xiia, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alphaFXIIa
beta-FXIIa
blood coagulation factor XII
blood-coagulation factor XII, activated beta
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-
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blood-coagulation factor XIIabeta
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-
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blood-coagulation factor XIIf
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-
-
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coagulation factor XII
coagulation factor XIIa
factor XII
factor XII Osaka
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abnormal factor XII with partially defective prekallikrein cleavage activity
factor XIIa
FXII
FXIIa
HAF
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Hageman factor
Hageman factor beta-fragment
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-
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Hageman factor fragment HFf
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Hagemann factor
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kallikreinogen, activator
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prealbumin activator
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prekallikrein activator
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beta-FXIIa
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alpha-FXIIa when cleaved by plasma kallikrein forms Factor beta-XIIa
factor XII
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FXII
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FXII
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FXII is a zymogen of the proteolytically active FXIIa that plays a role in thrombus stabilization by enhancing clot formation and in inflammation by enhancing bradykinin formation
Hageman factor
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
selective cleavage of Arg-/-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY
75216-42-1
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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
factor XII + H2O
factor XIIa + ?
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the enzyme undergoes autoactivation to alpha-fXIIa in the presence of polyphosphate
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-
?
Nalpha-benzoyl-Ile-Glu(-OR)-Gly-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-Ile-Glu(-OR)-Gly-Arg + 4-nitroaniline
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-
?
factor VII + H2O
factor VIIa
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bovine factor VII, a single Arg-Ile bond in factor VII is cleaved and the single chain form of factor VII is converted into a two-chain molecule
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-
?
factor XI + H2O
factor XIa + ?
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cleavage of an internal peptide bond in each of the two precursor chains
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?
factor XI + H2O
factor XIa + ?
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691466, 696541, 696931, 696939, 697877, 699180, 700245, 717423, 732402, 752492, 753067, 753351, 754124, 755579, 755586
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-
?
prekallikrein + H2O
kallikrein + kallikrein prepeptide
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?
prekallikrein + H2O
kallikrein + kallikrein prepeptide
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cleavage of a single peptide bond
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-
?
prekallikrein + H2O
kallikrein + kallikrein prepeptide
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cleavage of a single peptide bond
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-
?
prekallikrein + H2O
kallikrein + kallikrein prepeptide
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cleavage of a single peptide bond
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?
additional information
?
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surface-catalyzed conversion of the blood zymogen factor XII, i.e. FXII or Hageman factor, to the enzyme FXIIa vis autoactivation is not specific for anionic surfaces. Surface activation is moderated by the protein composition of the fluid phase in which FXII autoactivation occurs by what appears to be a protein adsorption-competition effect. Contact activation of plasma coagulation is potentiated by assembly of activation-complex proteins, i.e. FXII, FXI, prekallikrein, and high-molecular-weight kininogen, directly onto activating surfaces (procoagulants) through specific protein/surface interactions, method evaluation, modelling and value of modeling hypotheticals, adsorption and coagulation kinetics, overview
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?
additional information
?
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surface-catalyzed conversion of the blood zymogen factor XII, i.e. FXII or Hageman factor, to the enzyme FXIIa vis autoactivation is not specific for anionic surfaces. Surface activation is moderated by the protein composition of the fluid phase in which FXII autoactivation occurs by what appears to be a protein adsorption-competition effect. Contact activation of plasma coagulation is potentiated by assembly of activation-complex proteins, i.e. FXII, FXI, prekallikrein, and high-molecular-weight kininogen, directly onto activating surfaces (procoagulants) through specific protein/surface interactions, method evaluation, modelling and value of modeling hypotheticals, adsorption and coagulation kinetics, overview
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?
additional information
?
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surface-catalyzed conversion of the blood zymogen factor XII, i.e. FXII or Hageman factor, to the enzyme FXIIa vis autoactivation is not specific for anionic surfaces. Surface activation is moderated by the protein composition of the fluid phase in which FXII autoactivation occurs by what appears to be a protein adsorption-competition effect. Contact activation of plasma coagulation is potentiated by assembly of activation-complex proteins, i.e. FXII, FXI, prekallikrein, and high-molecular-weight kininogen, directly onto activating surfaces (procoagulants) through specific protein/surface interactions, method evaluation, modelling and value of modeling hypotheticals, adsorption and coagulation kinetics, overview
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?
additional information
?
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participation of the Hageman factor-dependent system in the inflammatory response to pseudomonal infections, due to the initiation of the system by bacterial elastase
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?
additional information
?
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increased levels of activated coagulation factor XIIa are associated with coronary heart disease, sepsis, and diabetes
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?
additional information
?
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roles of enzyme as a modulator of cellular adhesion, migration and vascularization
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?
additional information
?
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changes of plasma variations of different types of XIIa measured followed by thrombolytic therapy of patients with acute ST-elevation myocardial infarction
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?
additional information
?
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changes of plasma variations of different types of XIIa measured followed by thrombolytic therapy of patients with acute ST-elevation myocardial infarction
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?
additional information
?
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FXIIa, but not FXII, binds in a Zn2+-independent manner to immobilized fibronectin, the binding of FXIIa to fibronectin is inhibited by gelatine and fibrin but not by heparin
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?
additional information
?
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FXII autoactivates by contact with a variety of artificial or biologic negatively charged surfaces (contact activation), resulting in blood coagulation and activation of the inflammatory kallikrein-kinin and complement systems
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?
additional information
?
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FXII plays a functional role in thrombus formation and stabilization during stroke, FXII is an essential component of pathologic thrombus formation but not of physiologic hemostasis
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?
additional information
?
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coagulation factor XII is a liver-derived serine protease involved in fibrinolysis, coagulation, and inflammation, regulation of FXII expression by TGF-beta-1, a multifunctional cytokine, overview
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?
additional information
?
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hemodynamic and sympathoadrenal responses to coagulation beta-FXIIa or related new pressor protein, NPP, mechanism of action of NPP/beta-FXIIa, overview. New pressor protein, NPP, is an extrarenal, approximately 30 kDa anionic enzyme that potently elevates blood pressure (BP), heart rate (HR) and sympathoadrenal catecholamines in bioassays
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-
?
additional information
?
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-
surface-catalyzed conversion of the blood zymogen factor XII, i.e. FXII or Hageman factor, to the enzyme FXIIa vis autoactivation is not specific for anionic surfaces. Surface activation is moderated by the protein composition of the fluid phase in which FXII autoactivation occurs by what appears to be a protein adsorption-competition effect. Contact activation of plasma coagulation is potentiated by assembly of activation-complex proteins, i.e. FXII, FXI, prekallikrein, and high-molecular-weight kininogen, directly onto activating surfaces (procoagulants) through specific protein/surface interactions, method evaluation, modelling and value of modeling hypotheticals, adsorption and coagulation kinetics, overview
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?
additional information
?
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usage of measurement of prekallkrein hydrolysis to kallikrein by activated factor XII at test hydrophilic clean glass and hydrophobic silanized glass surfaces in the presence of bovine serum albumin, BSA. Activation after contact of the zymogen FXII with a test hydrophobic surface to activated FXII occurs only if putatively adsorbed FXIIa is competitively displaced by BSA, overview. An anionic hydrophilic surface is not a necessary cofactor for FXIIa-mediated hydrolysis of PK, and PK hydrolysis does not need to occur by an activation complex assembled directly on an anionic, activating surface. Contact activation of FXII (autoactivation) is not specific to anionic hydrophilic surfaces. Protein-adsorption competition is an essential feature that must be included in any comprehensive mechanism of surface-induced blood coagulation. Activation of zymogen FXII to FXIIa by autoactivation
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?
additional information
?
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enzyme contributes to pathologic clotting through the intrinsic pathway
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?
additional information
?
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FXII plays a functional role in thrombus formation and stabilization during stroke, FXII is an essential component of pathologic thrombus formation but not of physiologic hemostasis
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?
additional information
?
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blood pressure and heart rate estimated in bioassay rats after intravenous bolus of the activated beta-fragment of human coagulation factor XIIa
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?
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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
factor XI + H2O
factor XIa + ?
-
-
-
-
?
additional information
?
-
-
participation of the Hageman factor-dependent system in the inflammatory response to pseudomonal infections, due to the initiation of the system by bacterial elastase
-
-
?
additional information
?
-
-
increased levels of activated coagulation factor XIIa are associated with coronary heart disease, sepsis, and diabetes
-
?
additional information
?
-
-
roles of enzyme as a modulator of cellular adhesion, migration and vascularization
-
-
?
additional information
?
-
-
FXIIa, but not FXII, binds in a Zn2+-independent manner to immobilized fibronectin, the binding of FXIIa to fibronectin is inhibited by gelatine and fibrin but not by heparin
-
-
?
additional information
?
-
-
FXII autoactivates by contact with a variety of artificial or biologic negatively charged surfaces (contact activation), resulting in blood coagulation and activation of the inflammatory kallikrein-kinin and complement systems
-
-
?
additional information
?
-
-
FXII plays a functional role in thrombus formation and stabilization during stroke, FXII is an essential component of pathologic thrombus formation but not of physiologic hemostasis
-
-
?
additional information
?
-
-
coagulation factor XII is a liver-derived serine protease involved in fibrinolysis, coagulation, and inflammation, regulation of FXII expression by TGF-beta-1, a multifunctional cytokine, overview
-
-
?
additional information
?
-
-
hemodynamic and sympathoadrenal responses to coagulation beta-FXIIa or related new pressor protein, NPP, mechanism of action of NPP/beta-FXIIa, overview. New pressor protein, NPP, is an extrarenal, approximately 30 kDa anionic enzyme that potently elevates blood pressure (BP), heart rate (HR) and sympathoadrenal catecholamines in bioassays
-
-
?
additional information
?
-
-
enzyme contributes to pathologic clotting through the intrinsic pathway
-
-
?
additional information
?
-
-
FXII plays a functional role in thrombus formation and stabilization during stroke, FXII is an essential component of pathologic thrombus formation but not of physiologic hemostasis
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diisopropyl phosphofluoridate