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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Metals Ions
Metals Ions on EC 3.4.21.5 - thrombin
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Ca2+
K+
Na+
additional information
K+
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two ion binding sites per enzyme molecule, binding structure, molecular basis of monovalent cation selectivity, overview, the K+-bound enzyme form shows key differences compared with the Na+-bound structure resulting in different kinetics of activation, overview
Na+
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kinetic mechanism of Na+ binding to thrombin, stopped-flow measurements of intrinsic fluorescence, two-step mechanism with a rapid phase occurring within the dead time of the spectrometer followed by a single-exponential slow phase whose kobs decreases hyperbolically with increasing Na+ concentration, overview
Na+
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the activating effect of Na+ on thrombin is allosteric and depends on the conformational transition from a low activity Na+-free, slow form to a high activity Na+-bound, fast form, overview, the Na+-free enzyme is in inactive conformation, Trp215, Arg187, and Arg221are involved, Na+ binding kinetics of wild-type and mutant enzymes, overview
Na+
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two ion binding sites per enzyme molecule, free thrombin is a Na+-selective enzyme, the K+-bound enzyme form shows key differences compared with the Na+-bound structure resulting in different kinetics of activation, binding structure, overview
Na+
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two-step mechanism of Na+ binding to thrombin resolved by ultra-rapid kinetics
Na+
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Na+ activates thrombin by securing the correct orientation of the Glu192-Gly193 peptide bond, which is likely flipped in the absence of cation
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mutants show reduced specificity for monovalent cations compared to the wild-type enzyme
additional information
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the cation-free enzyme form assumes a conformation where the monovalent cation binding site is completely disordered, the S1 pocket is inaccessible to substrate and binding to exosite I is compromised by an unprecedented shift in the position of the autolysis loop