3.4.21.5: thrombin
This is an abbreviated version!
For detailed information about thrombin, go to the full flat file.
Word Map on EC 3.4.21.5
-
3.4.21.5
-
platelet
-
anticoagulant
-
heparin
-
thrombosis
-
bleeding
-
endothelial
-
artery
-
thromboplastin
-
collagen
-
agonist
-
thromboembolism
-
coronary
-
procoagulant
-
adp
-
antithrombotic
-
venous
-
fibrinolysis
-
thrombus
-
hemorrhage
-
hemostatic
-
hirudin
-
plasminogen
-
antiplatelet
-
thrombomodulin
-
protease-activated
-
arachidonic
-
plasmin
-
thromboxane
-
intravascular
-
viii
-
d-dimers
-
atrial
-
thrombocytopenia
-
aspirin
-
aptamer
-
hypercoagulability
-
willebrand
-
warfarin
-
percutaneous
-
p-selectin
-
rivaroxaban
-
platelet-rich
-
unfractionated
-
coagulopathy
-
prothrombotic
-
embolism
-
haemostasis
-
diagnostics
-
analysis
-
hemophilia
-
biotechnology
-
thrombolytic
-
nutrition
-
synthesis
-
clopidogrel
-
medicine
- 3.4.21.5
- platelet
-
anticoagulant
- heparin
- thrombosis
- bleeding
- endothelial
- artery
- thromboplastin
- collagen
- agonist
- thromboembolism
- coronary
-
procoagulant
- adp
-
antithrombotic
- venous
-
fibrinolysis
- thrombus
- hemorrhage
-
hemostatic
- hirudin
- plasminogen
-
antiplatelet
- thrombomodulin
-
protease-activated
-
arachidonic
- plasmin
-
thromboxane
-
intravascular
- viii
-
d-dimers
- atrial
- thrombocytopenia
- aspirin
- aptamer
- hypercoagulability
- willebrand
- warfarin
-
percutaneous
-
p-selectin
- rivaroxaban
-
platelet-rich
-
unfractionated
- coagulopathy
-
prothrombotic
- embolism
-
haemostasis
- diagnostics
- analysis
- hemophilia
- biotechnology
-
thrombolytic
- nutrition
- synthesis
- clopidogrel
- medicine
Reaction
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B =
Synonyms
activated factor II, alpha-thrombin, alphaTh, beta-thrombin, blood-coagulation factor II, activated, blood-coagulation factor IIa, clotting factor IIa, EC 3.4.4.13, factor IIa, fibrinogenase, thrombase, thrombin, E, thrombin-C, thrombofort, TLE2, topical, tropostasin
ECTree
Advanced search results
Activating Compound
Activating Compound on EC 3.4.21.5 - thrombin
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Ca2+
-
analysis of temperature dependence of pseudo-first order rate constants for enzyme-catalyzed hydrolysis of prothrombin-derived substrates, in presence and absence of Ca2+
D-glucose
-
high glucose enhances thrombin responses through transcriptional upregulation of protease-activated receptor-4, PAR-4, mediated via PKC-beta, -delta, and NFkappaB, in human vascular smooth muscle cells
gamma' peptide
-
extensive interactions between thrombin and the gamma' peptide mediated by electrostatic contacts with residues of exosite II and hydrophobic interactions with a pocket in close proximity to the Na+ binding site, complex structure and binding mode, the gamma' peptide completely overlaps with heparin bound to exosite II, overview
-
heparin
-
extensive interactions between thrombin and the gamma' peptide mediated by electrostatic contacts with residues of exosite II and hydrophobic interactions with a pocket in close proximity to the Na+ binding site, complex structure and binding mode, the gamma' peptide completely overlaps with heparin bound to exosite II, overview
lung thromboplastin activator
-
the activation of bovine prothrombin occurs by bovine lung thromboplastin activator
-
Polyphosphate
-
PolyP, secreted by activated platelets, a highly anionic polymer, polyphosphate plus beta-thrombin accelerates plasma clotting and enhances thrombin generation, kinetics, overview. Thrombin binds with high affinity to immobilized polyphosphate. Polyphosphate accelerates factor XI autoactivation and factor XIa autolysis
protease-activated receptor 3
-
the cleaved form of protease-activated receptor 3, PAR-3, acts as a cofactor for thrombin cleavage and activation of PAR-4 on murine platelets, interaction analysis of thrombin with the extracellular part of PAR-3, overview
-
factor Xa
-
coagulation factor Xa activates thrombin in ischemic neural tissue
-
binding of Na+ serves to stabilize the enzyme in a more open and rigid conformation. Na+-bound enzyme is more stable to denaturation by urea and more resistant to limited proteolysis by subtilisin
Na+
in Na+-free form, enzyme is in an equilibrium between an inert species and an active form, where the addition of Na+ populates the active state
Na+
-
increase in ratio kcat/KM from 0.0018 per mM and s in absence of Na+ to 0.125 per mM and s in presence of saturating concentration of Na+
Na+
-
not activating in wild-type. Mutant K222D, increase in ratio kcat/KM from 0.039 per mM and s in absence of Na+ to 0.069 per mM and s in presence of saturating concentration of Na+
-
defibrination of plasma results in an increased rate of thrombin generation
-
additional information
-
thrombomodulin has no effect on the conformation of the catalytic residue of thrombin
-
additional information
-
not activating: Na+. High activity even in absence of Na+ due to K222D change in amino acids compared to human enzyme
-
additional information
-
in the coagulation cascade, thrombin is activated by the prothrombinase complex which includes factor Va and factor Xa
-