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
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Subunits
Subunits on EC 3.4.21.5 - thrombin
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dimer
additional information
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x * 49400, SDS-PAGE, recombinant enzyme containing the 20400 Da Trx tag
dimer
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1 * 4600, A chain, + 1 * 32000, B chain, reduced alpha-thrombin, SDS-PAGE
additional information
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structure analysis, 2 of several recognition domains are the fibrinogen recognition site or anion binding exosite I formed by a loop of residues Arg67-Ile82, and the heparin binding site or anion binding exosite II localized at the C-terminus of the B-chain, localization and structure of recognition sites and insertion loops within the enzyme molecule, interaction with ligands, receptors and substrates, overview
additional information
structure molecular modeling of mutant DELTAK9 enzyme
additional information
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Staphylococcus aureus staphylocoagluase activates proenzyme without proteolysis. Staphylocoagulase-enzyme complex forms a dimer that binds fibrinogen with dissociation constant of 8-34 nM
additional information
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conformational transition from a low activity Na+-free, slow enzyme form to a high activity Na+-bound, fast enzyme form, overview, the Na+-free enzyme is in inactive conformation, Trp215. Arg187, and Arg221 are involved