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
3.4.21.5 thrombinAdvanced search results
results (
results (KM Value
KM Value on EC 3.4.21.5 - thrombin
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.000178
thrombin-activatable fibrinolysis inhibitor
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presence of thrombomodulin, Km(app) value
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0.00033
D-Phe-Pro-Arg-4-nitroanilide
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wild type enzyme, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM NaCl
0.00088
D-Phe-Pro-Arg-4-nitroanilide
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wild type enzyme, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM choline chloride
0.0029
D-Phe-Pro-Arg-4-nitroanilide
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mutant enzyme N143P, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM NaCl
0.013
D-Phe-Pro-Arg-4-nitroanilide
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mutant enzyme N143P, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM choline chloride
0.004
D-Phe-Pro-Lys-4-nitroanilide
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wild type enzyme, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM NaCl
0.0064
D-Phe-Pro-Lys-4-nitroanilide
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mutant enzyme N143P, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM NaCl
0.04
D-Phe-Pro-Lys-4-nitroanilide
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wild type enzyme, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM choline chloride
0.072
D-Phe-Pro-Lys-4-nitroanilide
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mutant enzyme N143P, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM choline chloride
0.017
D-Phe-Pro-Phe-4-nitroanilide
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wild type enzyme, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mN NaCl
0.033
D-Phe-Pro-Phe-4-nitroanilide
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mutant enzyme N143P, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mN NaCl
0.04
D-Phe-Pro-Phe-4-nitroanilide
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mutant enzyme N143P, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM choline chloride
0.11
D-Phe-Pro-Phe-4-nitroanilide
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wild type enzyme, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM choline chloride
0.0031
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
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in the presence of 0.01 mM hirudin-(54-65)
0.0039
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
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wild type enzyme, in Tris-HCl (pH 7.5) with 1.0 M NaCl and dithiothreitol, at 22°C
0.0059
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
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mutant enzyme R67C/I82C, in Tris-HCl (pH 7.5) with 0.2 M NaCl, at 22°C
0.0059
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
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wild type enzyme, in Tris-HCl (pH 7.5) with 0.2 M NaCl, at 22°C
0.0064
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
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wild type enzyme, in Tris-HCl (pH 7.5) with 0.2 M NaCl and dithiothreitol, at 22°C
0.0088
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
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wild type enzyme, in Tris-HCl (pH 7.5) with 0.2 M choline chloride, at 22°C
0.0106
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
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mutant enzyme R67C/I82C, in Tris-HCl (pH 7.5) with 0.2 M choline chloride, at 22°C
0.0121
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
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in the presence of 0.01 mM HD22
0.0143
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
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in the presence of 0.01 mM HD1
0.0287
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
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mutant enzyme E217C/K224C, in Tris-HCl (pH 7.5) with 1.0 M NaCl and dithiothreitol, at 22°C
0.062
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
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mutant enzyme E217C/K224C, in Tris-HCl (pH 7.5) with 0.2 M NaCl, at 22°C
0.0956
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
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mutant enzyme E217C/K224C, in Tris-HCl (pH 7.5) with 0.2 M NaCl and dithiothreitol, at 22°C
0.298
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
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mutant enzyme E217C/K224C, in Tris-HCl (pH 7.5) with 0.2 M choline chloride, at 22°C
0.1471
di-L-Glu-L-Pro-L-Arg-4-nitroanilide
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in the presence of 0.01 mM hirudin-(54-65)
0.435
S-2366
37°C, pH not specified in the publication, plasma-derived human thrombin FII
0.464
S-2366
37°C, pH not specified in the publication, recombinant human thrombin FII
0.0117
tosyl-Gly-Pro-Arg-4-nitroanilide
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in the presence of 0.01 mM hirudin-(54-65)
additional information
additional information
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thermodynamic analysis of enzyme structure
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additional information
additional information
thermodynamic analysis of enzyme structure
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additional information
additional information
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kinetics of mutant enzymes, overview
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additional information
additional information
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ratios of kcat/KM for substrates fibrinogen, PAR1, PAR4, protein C and RAP and comparison with human enzyme
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additional information
additional information
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ratios of kcat/KM for substrates fibrinogen, PAR1, PAR4, protein C and RAP and comparison with human enzyme
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additional information
additional information
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allosteric model based on the kinetic scheme using free enzyme mutant R77aA and the K+ bound F form of the mutant, Michaelis-Menten kinetics, kinetic modeling, overview
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additional information
additional information
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stopped flow kinetics of Na+ binding to thrombin, overview
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additional information
additional information
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ultra-rapid kinetics of Na+-binding to wild-type and mutant S195A thrombin
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additional information
additional information
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fibrinogen hydrolysis kinetics, kinetic model, overview
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