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
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3.4.21.5
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platelet
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anticoagulant
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heparin
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thrombosis
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bleeding
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endothelial
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artery
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thromboplastin
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collagen
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agonist
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thromboembolism
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coronary
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procoagulant
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adp
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antithrombotic
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venous
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fibrinolysis
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thrombus
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hemorrhage
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hemostatic
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hirudin
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plasminogen
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antiplatelet
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thrombomodulin
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protease-activated
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arachidonic
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plasmin
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thromboxane
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intravascular
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viii
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d-dimers
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atrial
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thrombocytopenia
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aspirin
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aptamer
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hypercoagulability
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willebrand
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warfarin
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percutaneous
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p-selectin
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rivaroxaban
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platelet-rich
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unfractionated
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coagulopathy
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prothrombotic
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embolism
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haemostasis
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diagnostics
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analysis
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hemophilia
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biotechnology
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thrombolytic
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nutrition
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synthesis
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clopidogrel
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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
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Posttranslational Modification
Posttranslational Modification on EC 3.4.21.5 - thrombin
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proteolytic modification
side-chain modification
additional information
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Staphylococcus aureus staphylocoagluase activates proenzyme without proteolysis. Staphylocoagulase-enzyme complex forms a dimer that binds substrate fibrinogen with dissociation constant of 8-34 nM
proteolytic modification
activation of recombinant wild-type and mutant DELTAK9 prothrombins by Taipan snake venom treatment
proteolytic modification
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activation of the recombinant wild-type and mutant enzymes by snake venom enzyme ecarin
proteolytic modification
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prothrombin requires activation by proteolytic cleavage, clevage sites are R155, R271, and R286, in vitro activation by Taipan snake venom
proteolytic modification
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the zymogen can be activated via different pathways, the pre2 pathway: cleavage at Arg271 and prethrombin 2 of prothrombin by the membrane-bound factor Xa alone, the meizo pathway: factor Va directs prothrombin activation by factor Xa through the meizothrombin pathway, characterized by initial cleavage at Arg320, the prothrombinase complex is responsible for activation, overview
proteolytic modification
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wild-type and mutant enzyme activation by the prothrombinase complex
proteolytic modification
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activation of prothrombin through cleavage by tissue factor, can be blocked with a TF-neutralizing antibody and TF-siRNA
proteolytic modification
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active thrombin is generated from thrombinogen by proteolytic cleavage
proteolytic modification
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recombinant mutant prothrombins are activated through proteolytic cleavage using crude venom from Echis carinatus and 1:100 dilution of venom from Agkistrodon acutus in the presence of 10 mM benzamidine and 10 mM CaCl2
proteolytic modification
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activation of prothrombin by snake venom from Oxyuranus scutellatus
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the A chain contains no carbohydrate, the B chain contains 3.5% neutral sugar, 2.6% glucosamine, and 1.5% sialic acid