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Information on EC 3.4.21.5 - thrombin
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3.4.21.5 thrombinSpecify your search results
Word Map
- 3.4.21.5
- platelet
-
anticoagulant
- heparin
- thrombosis
- bleeding
- endothelial
- artery
- thromboplastin
- agonist
- collagen
-
antithrombotic
- venous
- adp
- thromboembolism
- coronary
-
procoagulant
-
fibrinolysis
- thrombus
- plasminogen
-
hemostatic
- hirudin
- hemorrhage
-
antiplatelet
-
thromboxane
-
protease-activated
-
intravascular
- aptamer
- thrombomodulin
-
d-dimers
-
arachidonic
- atrial
- plasmin
- willebrand
- thrombocytopenia
- aspirin
- viii
- warfarin
- coagulopathy
- hypercoagulability
-
p-selectin
-
prothrombotic
-
haemostasis
- embolism
-
platelet-rich
-
percutaneous
-
unfractionated
- rivaroxaban
- diagnostics
- analysis
-
thrombolytic
- clopidogrel
- hemophilia
- medicine
- biotechnology
- nutrition
- synthesis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
Synonyms
thrombin, alpha-thrombin, factor iia, fibrinogenase, beta-thrombin, activated factor ii, alphath, thrombin-c, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-thrombin
factor IIa
fibrinogenase
alpha-thrombin
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
-
-
-
-
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
mechanism, modeling
-
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
active site and P1' interactions, overview
-
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
Asp189 is involved in substrate recognition
-
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
catalytic tetrad, composed of His57, Asp102, Ser195, and Ser214, at the bottom of a canyon-like cleft shaping the catalytic pocket, further regulation of specificity by recognition domains along with insertion loops
-
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
reaction mechanism, substrate binding, preference at positions P1-P4, molecular modeling of enzyme-substrate complex
-
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
serine protease
-
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
serine protease, for substrate binding P1 and P2 residues must be compatible with the geometry and chemistry of S1 and S2 specificity sites in thrombin, a glycine in P5 position is necessary for conserved substrate conformation, the hydrophobic residues, which occupy the aryl binding site of the enzyme determine the substrate conformation further away from the catalytic residues
-
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
serine protease, mechanism and substrate binding
-
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
two active site loops, residues 214-222 and residues 126-132, undergo decreases in solvent accessibility due to steric contacts with substrate. Two regions outside the active site undergo solvent protection upon substrate binding
-
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
two active site loops, residues 214-222 and residues 126-132, undergo decreases in solvent accessibility due to steric contacts with substrate. Two regions outside the active site undergo solvent protection upon substrate binding
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CAS REGISTRY NUMBER
COMMENTARY
9002-04-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ac-Gly-Gly-Val-Arg-7-amido-4-methylcoumarin + H2O
Ac-Gly-Gly-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Ac-Leu-Gly-Val-Arg-7-amido-4-methylcoumarin + H2O
Ac-Leu-Gly-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Ac-Nle-Thr-Leu-Arg-7-amido-4-methylcoumarin + H2O
Ac-Nle-Thr-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Ac-Nle-Thr-Pro-Arg-7-amido-4-methylcoumarin + H2O
Ac-Nle-Thr-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Ac-Val-Thr-Pro-Arg-7-amido-4-methylcoumarin + H2O
Ac-Val-Thr-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Ala-Ala-Pro-Phe + 4-nitroaniline
-
synthetic chromogenic substrate
-
?
beta-Ala-Gly-Arg-4-nitroanilide + H2O
beta-Ala-Gly-Arg + 4-nitroaniline
-
-
-
?
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide + H2O
D-Phe-L-pipecolyl-L-Arg + 4-nitroaniline
-
-
-
?
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
-
i.e. S-2238
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine-4-nitroaniline
-
-
?
di-L-Glu-L-Pro-L-Arg-4-nitroanilide + H2O
di-L-Glu-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
factor VIII mutant D392A/D394A + H2O
?
-
reduction in specific activity similar to a severe hemophilia phenotype. No cleavage at R740, while cleavage at R372 is not affected
-
?
factor VIII mutant Q370E/I371P/V374F/A375S + H2O
?
-
-
mutation to P3-P3' residues flanking Arg740, 98% of the activtiy with wild-type
?
factor VIII mutant Q370S/I371P/V374F/A375Q + H2O
?
-
-
mutation to P3-P3' residues flanking Arg1689, 14% of the activtiy with wild-type
?
factor VIII mutant R372H + H2O
?
-
naturally occuring mutation in hemophilia A patients. About 80fold decrease in cleavage rate compared to wild-type substrate, cleavage at H372-S373 bond
-
?
factor VIII(341-376) peptide + H2O
?
-
cleavage of Arg372 involving exosite II, the heparin binding site
-
?
factor XIII V34L mutant + H2O
activated factor XIII V34L mutant + ?
-
binding structure and interaction analysis, mutant substrate, a polymorphism exists within the activation peptide segment at the P4 position of FXIII resulting in substitution V34L, FXIII V34L occurs in approximately 30% of the human population worldwide, overview
-
?
Fc-[GRPS]-PEG + H2O
?
-
ferrocene-labelled tetrapeptide with a polyethylene glycol linker
-
?
Fc-[RFSRPQL]-PEG + H2O
?
-
ferrocene-labelled heptapeptide with a polyethylene glycol linker
-
?
fibrin I-plasma factor XIII complex + H2O
activation peptide + fibrinopeptide B
-
-
-
?
GLVPRGVNL + H2O
GLVPR + GVNL
-
residues 33-41 of factor XIII with mutation V34L
-
?
HD-cyclohexylglycyl-Ala-Arg-4-nitroanilide + H2O
HD-cyclohexylglycyl-Ala-Arg + 4-nitroaniline
-
assay method optimization with synthetic substrate HD-cyclohexylglycyl-Ala-Arg-4-nitroanilide, overview
-
?
N-(4-tosyl)-Gly-L-Pro-L-Arg-4-nitroanilide + H2O
N-(4-tosyl)-Gly-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Arg 4-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Arg + 4-nitrophenol
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Lys 4-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Lys + 4-nitrophenol
-
-
-
?
PAR1 peptide + H2O
?
protease-activated receptor I peptide fragment, amino acid sequence
-
?
pro-factor XIII + H2O
factor XIII
-
activation by cleavage at Arg37 leading to blood coagulation
-
?
protease-activated receptor + H2O
activated protease-activated receptor + ?
-
activation
-
?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
-
activation
-
?
protease-activated receptor 4 + H2O
activated PAR-4 + ?
-
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-4, overview
-
?
protease-activated receptor-1 + H2O
activated PAR-1
-
i.e. PAR-1, activation, major thrombin receptor
product induces connective tissue growth factor production, a fibroblast mitogen, which promotes extracellular matrix protein production
?
protein G + H2O
?
thrombin is able to cleave protein G, within its alpha-helix when a suitable cleavage sequence for the enzyme is introduced into this region. Thrombin is only cleaving within the alpha-helix when it is in an unfolded state. The introduction of destabilizing mutations within the protein increases the efficiency of cleavage by the enzyme
-
?
proteinase-activated receptor 1 + H2O
?
-
alpha-thrombin may not effectively catalyze proteinase-activated receptor 1-(1-41) generation
-
?
proteinase-activated receptor 4 + H2O
?
-
alpha-thrombin may not effectively catalyze proteinase-activated receptor 4-(1-47) generation
-
?
tosyl-Gly-L-Pro-L-Arg-4-nitroanilide + H2O
tosyl-Gly-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
TVELQGLVPRGVNL + H2O
TVELQGLVPR + GVNL
-
residues 28-41 of factor XIII with mutation V34L
-
?
ADAMTS-13 + H2O
?
-
proteolysis of ADAMTS-13 by thrombin causes an 8fold reduction in its affinity for von Willebrand factor VWF that contributes to its loss of VWF-cleaving function, physiologic function, overview
-
?
ADAMTS-13 + H2O
?
-
inactivation by cleavage at R257 and R1176, substrate is the plasma metalloprotease, a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13, no activity with R257A and R1176H ADAMTS-13 mutants
-
?
D-Phe-L-Pro-L-Arg-4-nitroanilide + H2O
D-Phe-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
D-Phe-L-Pro-L-Arg-4-nitroanilide + H2O
D-Phe-L-Pro-L-Arg + 4-nitroaniline
-
-
-
?
D-Phe-L-Pro-L-Phe-4-nitroanilide + H2O
D-Phe-L-Pro-L-Phe + 4-nitroaniline
-
-
-
?
D-Phe-L-Pro-L-Phe-4-nitroanilide + H2O
D-Phe-L-Pro-L-Phe + 4-nitroaniline
-
-
-
?
D-Phe-Pro-Arg-4-nitroanilide + H2O
D-Phe-Pro-Arg + 4-nitroaniline
-
-
-
?
D-Phe-Pro-Arg-4-nitroanilide + H2O
D-Phe-Pro-Arg + 4-nitroaniline
-
synthetic chromogenic substrate
-
?
D-Phe-Pro-Lys-4-nitroanilide + H2O
D-Phe-Pro-Lys + 4-nitroaniline
-
synthetic chromogenic substrate
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
i.e. S2238, synthetic chromogenic substrate
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
-
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
i.e. S2238, synthetic chromogenic substrate
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
i.e. S2238, synthetic chromogenic substrate
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
i.e. S2238, synthetic chromogenic substrate
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
i.e. S2238, synthetic chromogenic substrate
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
i.e. S2238, synthetic chromogenic substrate
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
i.e. S2238, synthetic chromogenic substrate
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
i.e. S2238, synthetic chromogenic substrate
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
i.e. S2238, synthetic chromogenic substrate
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide is S2238
-
?
factor VIII + H2O
?
-
-
proteolysis occurs at residues Arg372 and Arg740 in the facto VIII heavy chain and Arg1689 in the factor VIII light chain. The sequences at Arg740 and Arg1689 are more optimal for thrombin cleavage than at Arg372. Rates of thrombin cleavage at Arg372 are increased about 10fold and about 3fold compared with wild-type factor VIII when replaced with P3-P3' residues flanking Arg740 or Arg1689, respectively, and these values parallel increased rates of A2 subunit generation and procofactor activation. Positioning of more optimal residues flanking Arg372 abrogates the need for initial cleavage at Arg740 to facilitate this step
?
factor VIII + H2O
?
-
activation by cleavage of Arg372, Arg74, and Arg1689 involving exosite II, the heparin binding site
-
?
factor VIII + H2O
?
-
activation by cleavage of Arg372, Arg74, and Arg1689, plays a fundamental role in the amplification of the coagulation cascade
-
?
factor VIII + H2O
factor VIIIa + propeptide
-
high affinity site in A1 subunit of substrate, dependent on Na+-bound form of enzyme. Moderate affinity site in A2 subunit, independent of Na+-state of enzyme
-
?
factor XII + H2O
activated factor XII + ?
-
activated factor XII cross-links fibrin molecules and stabilizes the fibrin clot
-
?
factor XIII + H2O
activated factor XIII + ?
-
the enzyme is involved in the coagulation cascade, overview
-
?
factor XIII + H2O
activated factor XIII + ?
-
binding structure and interaction analysis, wild-type substrate, overview
-
?
Fibrinogen + H2O
?
-
cleavage of four Arg-Gly peptide bonds, the enzyme is involved in the final step in the coagulation of mammalian blood
-
?
Fibrinogen + H2O
?
-
the fully reversible interaction of alpha-thrombin with glycoprotein Ibalpha supports the association with platelets of a proteolytically active enzyme that may contribute to activation
-
?
Fibrinogen + H2O
?
-
in intact human erythrocyte leucemia cells thrombin activates adenylate cyclase
-
?
fibrinogen + H2O
fibrin + ?
-
the enzyme mediates the conversion of fibrinogen to fibrin
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
-
669516, 704797, 707320, 707506, 707511, 707652, 707672, 707944, 707960, 708032, 708154, 708178, 708248, 708363, 708811, 708816, 709043, 709050, 709074, 709109, 709161, 709242, 709437, 709468, 709588, 710103, 710224, 710402, 710594, 710604, 710610, 710634, 717085, 717199, 732938
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
proteolytic activation
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
proteolytic activation
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
proteolytic activation
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
proteolytic activation
fibrinopeptide A D49 binds to thrombin R67
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
strongly inverse solvent isotope effects on reaction
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
oxidation impairs the capacity of isolated fibrinogen to form a fibrin clot under the effect of thrombin
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
from human and salmon
-
?
fibrinogen 1 + H2O
fibrin 1 + fibrinopeptide A + fibrinopeptide B
-
-
-
?
fibrinogen 1 + H2O
fibrin 1 + fibrinopeptide A + fibrinopeptide B
-
-
-
?
fibrinogen 1 + H2O
fibrin 1 + fibrinopeptide A + fibrinopeptide B
-
human, composed of 2 gamma-chains, gamma A and gamma'
fibrin 1 contains a low affinity binding site in the E doamin, and a high affinity binding site at residues 408-427 of the gamma'-chain, sequence VRPEHPAETEYDSLYPEDDL, for thrombin exosites, binding study, overview
?
fibrinogen 2 + H2O
fibrin 2 + fibrinopeptide A + fibrinopeptide B
-
-
-
?
fibrinogen 2 + H2O
fibrin 2 + fibrinopeptide A + fibrinopeptide B
-
-
-
?
fibrinogen 2 + H2O
fibrin 2 + fibrinopeptide A + fibrinopeptide B
-
human, composed of 2 gamma-chains, gamma A and gamma'
fibrin 2 contains a low affinity binding site in the E doamin, and a high affinity binding site at residues 408-427 of the gamma'-chain, sequence VRPEHPAETEYDSLYPEDDL, for thrombin exosites, binding study, overview
?
galectin-8 + H2O
?
-
although intact isoform G8L stimulates neutrophil adhesion to substrate more efficiently than isoform G8M, the activity of isoform G8L but not that of isoform G8M decreases on thrombin digestion, overview
-
?
galectin-8 + H2O
?
-
cleavage site is -IAPRT- residing within the linker peptide, isoforms with the longest linker peptide, galectin-8L and galectin-9L, are highly susceptible to thrombin cleavage, whereas the predominant isoforms, galectin-8M and galectin-9M, and other members of human galectin family so far examined are resistant to thrombin, overview, human and murine substrates, and recombinant GST-tagged wild-type and mutant substrate, sbstrate specificity, overview
-
?
galectin-9 + H2O
?
-
thrombin treatment almost completely abolishes eosinophil chemoattractant activity of isoform G9L, overview
-
?
galectin-9 + H2O
?
-
cleavage site is -PRPRG- residing within the linker peptide, isoforms with the longest linker peptide, galectin-8L and galectin-9L, are highly susceptible to thrombin cleavage, whereas the predominant isoforms, galectin-8M and galectin-9M, and other members of human galectin family so far examined are resistant to thrombin, overview, human and murine substrates, and recombinant GST-tagged wild-type and mutant substrate, sbstrate specificity, overview
-
?
protease-activated receptor 1 + H2O
?
-
endothelial protein C receptor-dependent cleavage of PAR-1 on vascular endothelial cells, the enzyme exhibts anti-inflammatory activity
-
?
protease-activated receptor 1 + H2O
?
-
endothelial protein C receptor-dependent cleavage of PAR-1
-
?
protease-activated receptor 1 + H2O
?
-
thrombin inhibits the tumor necrosis factor-alpha-mediated expression of secretory group IIA phospholipase A2-IIA through the cleavage of protease-activated receptor 1, the EPCR-dependent cleavage of protease-activated receptor 1by thrombin increases the phosphorylation of extracellular signalregulated kinase 1/2
-
?
protease-activated receptor-1 + H2O
?
-
PAR-1 is the major mediator of thrombin signalling and is involved in platelet activation, smooth muscle cells migration and proliferation, PAR-1 activation also regulates many aspects of endothelial cell biology and has been involved in vascular development
-
?
protease-activated receptor-1 + H2O
?
-
fibrin-bound thrombin, specific cleavage by thrombin at the extracellular N-terminus
-
?
protein C + H2O
?
-
the mutation E229K shifts the substrate specificity of thrombin by 130fold to favor the activation of the anticoagulant substrate protein C over the procoagulant substrate fibrinogen
-
?
protein C + H2O
?
-
mutation E229A substantially shifts thrombin's specificity in favour of the anticoagulant substrate, protein C
-
?
protein C zymogen + H2O
activated protein C + propeptide
-
activated protein C has a regulatory function in inhibiting thrombin activation, overview
-
?
protein C zymogen + H2O
activated protein C + propeptide
-
on vascular endothelial cells
-
?
S2238 + H2O
?
-
fibrin-bound thrombin activity, measured by selective chromogenic substrate S2238
-
?
thrombin-activatable fibrinolysis inhibitor + H2O
?
-
mutant variants with variants in the amino acids surrounding the scissile R92-A93 bond such as P91S, R92K, and S90P exhibit specific impairment of activation by thrombin or thrombin/thrombomodulin
-
?
tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
?
tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
?
tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
?
additional information
?
-
determination of enzyme activity by active site titration with 4-nitrophenyl guanidino-benzoate
-
?
additional information
?
-
-
enzyme stimulates a marked increase in inositol phosphate accumulation, which is fully mimicked by a selective PAR1 activating peptide. Mitogenic effect of enzyme involves activation of PDGF or EGF receptors and a Gi/o-dependent activation of phosphoinositide 3-kinase. Enzyme stimulates phosphatidylinositol-3,4,5-triphosphate mass accumulation
-
?
additional information
?
-
-
thrombin is a multifunctional trypsin-like protease that plays a role in the blood coagulation system, stimulates platelet aggregation, and promotes its own generation through the activation of factor XI and cofactors V and VII
-
?
additional information
?
-
-
when binding to thrombomodulin, thrombin can activate the protein C to regulate coagulation by inhibiting thrombin generation
-
?
additional information
?
-
the enzyme shows no factor XIII activation activity
-
?
additional information
?
-
-
determination of residues involved in ligand binding, overview, interaction with receptors glycoprotein Ibalpha GpIb and protease-activated receptor I PARI in platelet membrane, thrombin recognition domains and insertion loops are responsible for substrate specificity determination and interaction with inhibitors, unique within serine proteases, thrombin can be at the same time very efficient and specific for different substrates and inhibitors, overview
-
?
additional information
?
-
interaction with receptors glycoprotein Ibalpha GpIb and protease-activated receptor 1, i.e. PAR1, in platelet membrane
-
?
additional information
?
-
-
interaction with receptors glycoprotein Ibalpha GpIb and protease-activated receptor 1, i.e. PAR1, in platelet membrane
-
?
additional information
?
-
-
structural requirements for enzyme activity
-
?
additional information
?
-
-
substrate specificity, peptide substrate library scanning
-
?
additional information
?
-
-
enzyme deficienxy leads to umbilical cord bleeding at birth, development of hematoma, diminished vitamin K-dependent clotting factor, thrombocytopenia, and at least to lethal retroperitoneal bleeding
-
?
additional information
?
-
-
enzyme exerts pro-inflammatory and profibrotic effects via proteolytic activation of the major thrombin receptor
-
?
additional information
?
-
-
enzyme is important in blood coagulation
-
?
additional information
?
-
-
enzyme plays a pivotal role in hemostasis, thrombosis, cell differentiation, and is involved in the activation of many cell types and platelets
-
?
additional information
?
-
-
enzyme stimulates platelets and exposure of phosphatidylserine on the external surface
-
?
additional information
?
-
-
a hirudin-like pentapeptide from the COOH terminus of factor Va heavy chain regulates the rate and pathway for prothrombin activation, prothrombinase complex regultion, overview
-
?
additional information
?
-
-
Na+ binding to thrombin is an interaction at the basis of the procoagulant and prothrombotic roles of the enzyme in the blood
-
?
additional information
?
-
-
the ligand occupancy of endothelial protein C receptor by caveolin-1 switches the protease-activated receptor 1-dependent signaling specificity of thrombin from a permeability-enhancing to a barrier-protective response in endothelial cells, overview
-
?
additional information
?
-
-
thrombin is initially implicated in hemostasis and fibrin clot formation, and is also involved in cell biology since the discovery of its major receptor, the protease-activated receptor-1, PAR-1, fibrin-adsorbed thrombin interacts with endothelial progenitor cells via the thrombin receptor PAR-1, overview
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
both thrombin and thrombin receptor agonist peptide enhance the permeability barrier of HPAEC cells, both exhibit a potent barrier protective effect when cells are treated with inactive mutant S195A of protein C prior to stimulation. Thrombin exhibits a potent cytoprotective activity in the lipopolysaccharide-induced permeability and tumor necrosis factor alpha-induced apoptosis and adhesion assays in the protein C mutant S195A treated cells. Treatment with the cholesterol depleting molecule methyl-beta-cyclodextrin eliminates the protective effect
-
?
additional information
?
-
-
both thrombin and thrombin receptor agonist peptides initiate proinflammatory responses in cells. The occupancy of endothelial protein C receptor by the inactive protein C mutant S195A switches the receptor PAR-1-dependent signaling specificity of thrombin leading to thrombin inhibition of the expression of cell surface adhesion molecules CCAM-I, ICAM-I and E-selectin as well as the binding of neutrophils to tumor necrosis factor alpha-activated endothelial cells. Both thrombin and thrombin receptor agonist peptides activate Rac I and inhibit the activation of RhoA and nuclear factor kappaB pathways in response to tumor necrosis factor alpha in cells pretreated with protein C mutant S195A
-
?
additional information
?
-
-
in cell cultures of HUVEC and HPAEC cells, low concentrations of thrombin or of receptor PAR-1 agonist peptide induce significant anti-inflammatory activities. Relatively high concentration of thrombin or of PAR-1 agonist peptide show pro-inflammatory activities. The direct anti-inflammatory effects of low concentrations of thrombin are dependent on the activation of PAR-1 and PI3 kinase
-
?
additional information
?
-
-
treatment of platelets with thrombin or ADP induces activation and mitochondrial association of active proapoptotic proteins Bid, Bax, and Bak. Thrombin evokes mitochondrial membrane depolarization, which is attenuated by catalase
-
?
additional information
?
-
-
citrullinated fibrinogen is no substrate. Thrombin does not catalyze the conversion of citrullinated fibrinogen to fibrin or relase fibrinopeptide A or fibrinopeptide B
-
?
additional information
?
-
-
protein context, as well as the identity of amino acids at protease cleavage sites, dictate protease specificity
-
?
additional information
?
-
-
thrombin is generated by proteolysis of its precursor prothrombin at sites of injury
-
?
additional information
?
-
-
determination of the extended substrate recognition profile. The consensus recognition sequence is, P2-Pro, P1-Arg, P19-Ser/Ala/Gly/Thr, P29-not acidic and P39-Arg. Residue P39-arginine in thrombin substrates lacking a P2-proline plays an important role. Upon insertion of the consensus sequence obtained in a linker region between two Escherichia coli thioredoxin molecules, mutations of P2-Pro and P39-Arg lead to an approximate 20fold and 14fold reduction, respectively in the rate of cleavage. Mutating both Pro and Arg results in a drop in cleavage of 200-400 times. No natural substrates display the obtained consensus sequence but represent sequences that show only 1-30% of the optimal cleavage rate for thrombin. Major effects on cleavage efficiency are also observed for residues as far away as 4 amino acids from the cleavage site. Insertion of an aspartic acid in position P4 results in a drop in cleavage by a factor of almost 20 times
-
?
additional information
?
-
although differences between the two thrombin (FIIa) preparations using ecarin cleavage are observed, FIIa derived from recombinant human FII administered to human would likely be very similar in activity and function as FIIa formed from endogenous FII
-
?
additional information
?
-
-
although differences between the two thrombin (FIIa) preparations using ecarin cleavage are observed, FIIa derived from recombinant human FII administered to human would likely be very similar in activity and function as FIIa formed from endogenous FII
-
?
additional information
?
-
electropositive regions at a distance from the active site, so called exosites, are of major importance for the cleavage by human thrombin. Addition of these regions enhance the cleavage rate by more than fifty fold. The enhancement is highly dependent on the sequence of the actual cleavage site. A minimal site that shows poor activity by itself can be cleaved as efficiently as an optimal cleavage site when presented together with these negatively charged regions. Sites conforming closely to the optimal site are only minimally enhanced by the addition of these regions
-
?
additional information
?
-
-
electropositive regions at a distance from the active site, so called exosites, are of major importance for the cleavage by human thrombin. Addition of these regions enhance the cleavage rate by more than fifty fold. The enhancement is highly dependent on the sequence of the actual cleavage site. A minimal site that shows poor activity by itself can be cleaved as efficiently as an optimal cleavage site when presented together with these negatively charged regions. Sites conforming closely to the optimal site are only minimally enhanced by the addition of these regions
-
?
additional information
?
-
-
nestin gene expression is regulated by the thrombin-mediated transactivation of EGFR in serum-deprived primary cultures of vascular smooth muscle cells. Upon binding of thrombin, regulator PAR-1 induces c-Src resulting in direct intracellular phosphorylation of EGFR and in the extracellular activation of the matrix metalloprotease MMP-2-mediated shedding of HB-epidermal growth factor
-
?
additional information
?
-
-
the presence of thrombin induces a significant increase in matrix metalloprotease-9 activity and also increases its mRNA expression in primary astrocytes. Thrombin-induced matrix metalloprotease-9 production is inhibited by the selective inhibitor of protease-activated receptor PAR-1, SCH 79797 and by PDS98059
-
?
additional information
?
-
-
enzyme stimulates platelets and exposure of phosphatidylserine on the external surface
-
?
additional information
?
-
-
following activation of platelets by thrombin, 26 proteins exhibit statistically significant differences. Deregulated proteins include proteins of the coagulation system and integrin signalling
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADAMTS-13 + H2O
?
-
proteolysis of ADAMTS-13 by thrombin causes an 8fold reduction in its affinity for von Willebrand factor VWF that contributes to its loss of VWF-cleaving function, physiologic function, overview
-
-
?
factor VIII + H2O
?
-
activation by cleavage of Arg372, Arg74, and Arg1689, plays a fundamental role in the amplification of the coagulation cascade
-
?
factor XII + H2O
activated factor XII + ?
-
activated factor XII cross-links fibrin molecules and stabilizes the fibrin clot
-
-
?
factor XIII + H2O
activated factor XIII + ?
-
the enzyme is involved in the coagulation cascade, overview
-
-
?
galectin-8 + H2O
?
-
although intact isoform G8L stimulates neutrophil adhesion to substrate more efficiently than isoform G8M, the activity of isoform G8L but not that of isoform G8M decreases on thrombin digestion, overview
-
-
?
galectin-9 + H2O
?
-
thrombin treatment almost completely abolishes eosinophil chemoattractant activity of isoform G9L, overview
-
-
?
pro-factor XIII + H2O
factor XIII
-
activation by cleavage at Arg37 leading to blood coagulation
-
?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
-
activation
-
-
?
protease-activated receptor-1 + H2O
activated PAR-1
-
i.e. PAR-1, activation, major thrombin receptor
product induces connective tissue growth factor production, a fibroblast mitogen, which promotes extracellular matrix protein production
?
proteinase-activated receptor 1 + H2O
?
-
alpha-thrombin may not effectively catalyze proteinase-activated receptor 1-(1-41) generation
-
-
?
proteinase-activated receptor 4 + H2O
?
-
alpha-thrombin may not effectively catalyze proteinase-activated receptor 4-(1-47) generation
-
-
?
Fibrinogen + H2O
?
-
cleavage of four Arg-Gly peptide bonds, the enzyme is involved in the final step in the coagulation of mammalian blood
-
-
?
Fibrinogen + H2O
?
-
the fully reversible interaction of alpha-thrombin with glycoprotein Ibalpha supports the association with platelets of a proteolytically active enzyme that may contribute to activation
-
-
?
Fibrinogen + H2O
?
-
in intact human erythrocyte leucemia cells thrombin activates adenylate cyclase
-
-
?
fibrinogen + H2O
fibrin + ?
-
the enzyme mediates the conversion of fibrinogen to fibrin
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
-
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
-
704797, 707320, 707506, 707511, 707652, 707672, 707944, 707960, 708032, 708154, 708178, 708248, 708363, 708811, 708816, 709043, 709050, 709074, 709109, 709161, 709242, 709437, 709468, 709588, 710103, 710224, 710402, 710594, 710604, 710610, 710634, 717085, 717199
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
proteolytic activation
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
oxidation impairs the capacity of isolated fibrinogen to form a fibrin clot under the effect of thrombin
-
-
?
fibrinogen 1 + H2O
fibrin 1 + fibrinopeptide A + fibrinopeptide B
-
-
-
?
fibrinogen 1 + H2O
fibrin 1 + fibrinopeptide A + fibrinopeptide B
-
-
-
?
fibrinogen 2 + H2O
fibrin 2 + fibrinopeptide A + fibrinopeptide B
-
-
-
?
fibrinogen 2 + H2O
fibrin 2 + fibrinopeptide A + fibrinopeptide B
-
-
-
?
protease-activated receptor 1 + H2O
?
-
endothelial protein C receptor-dependent cleavage of PAR-1 on vascular endothelial cells, the enzyme exhibts anti-inflammatory activity
-
-
?
protease-activated receptor 1 + H2O
?
-
thrombin inhibits the tumor necrosis factor-alpha-mediated expression of secretory group IIA phospholipase A2-IIA through the cleavage of protease-activated receptor 1, the EPCR-dependent cleavage of protease-activated receptor 1by thrombin increases the phosphorylation of extracellular signalregulated kinase 1/2
-
-
?
protease-activated receptor-1 + H2O
?
-
PAR-1 is the major mediator of thrombin signalling and is involved in platelet activation, smooth muscle cells migration and proliferation, PAR-1 activation also regulates many aspects of endothelial cell biology and has been involved in vascular development
-
-
?
protein C zymogen + H2O
activated protein C + propeptide
-
activated protein C has a regulatory function in inhibiting thrombin activation, overview
-
-
?
protein C zymogen + H2O
activated protein C + propeptide
-
on vascular endothelial cells
-
-
?
additional information
?
-
-
enzyme stimulates a marked increase in inositol phosphate accumulation, which is fully mimicked by a selective PAR1 activating peptide. Mitogenic effect of enzyme involves activation of PDGF or EGF receptors and a Gi/o-dependent activation of phosphoinositide 3-kinase. Enzyme stimulates phosphatidylinositol-3,4,5-triphosphate mass accumulation
-
-
?
additional information
?
-
-
thrombin is a multifunctional trypsin-like protease that plays a role in the blood coagulation system, stimulates platelet aggregation, and promotes its own generation through the activation of factor XI and cofactors V and VII
-
-
?
additional information
?
-
-
enzyme deficienxy leads to umbilical cord bleeding at birth, development of hematoma, diminished vitamin K-dependent clotting factor, thrombocytopenia, and at least to lethal retroperitoneal bleeding
-
?
additional information
?
-
-
enzyme exerts pro-inflammatory and profibrotic effects via proteolytic activation of the major thrombin receptor
-
?
additional information
?
-
-
enzyme is important in blood coagulation
-
?
additional information
?
-
-
enzyme plays a pivotal role in hemostasis, thrombosis, cell differentiation, and is involved in the activation of many cell types and platelets
-
?
additional information
?
-
-
enzyme stimulates platelets and exposure of phosphatidylserine on the external surface
-
?
additional information
?
-
-
a hirudin-like pentapeptide from the COOH terminus of factor Va heavy chain regulates the rate and pathway for prothrombin activation, prothrombinase complex regultion, overview
-
-
?
additional information
?
-
-
Na+ binding to thrombin is an interaction at the basis of the procoagulant and prothrombotic roles of the enzyme in the blood
-
-
?
additional information
?
-
-
the ligand occupancy of endothelial protein C receptor by caveolin-1 switches the protease-activated receptor 1-dependent signaling specificity of thrombin from a permeability-enhancing to a barrier-protective response in endothelial cells, overview
-
-
?
additional information
?
-
-
thrombin is initially implicated in hemostasis and fibrin clot formation, and is also involved in cell biology since the discovery of its major receptor, the protease-activated receptor-1, PAR-1, fibrin-adsorbed thrombin interacts with endothelial progenitor cells via the thrombin receptor PAR-1, overview
-
-
?
additional information
?
-
-
both thrombin and thrombin receptor agonist peptide enhance the permeability barrier of HPAEC cells, both exhibit a potent barrier protective effect when cells are treated with inactive mutant S195A of protein C prior to stimulation. Thrombin exhibits a potent cytoprotective activity in the lipopolysaccharide-induced permeability and tumor necrosis factor alpha-induced apoptosis and adhesion assays in the protein C mutant S195A treated cells. Treatment with the cholesterol depleting molecule methyl-beta-cyclodextrin eliminates the protective effect
-
-
?
additional information
?
-
-
both thrombin and thrombin receptor agonist peptides initiate proinflammatory responses in cells. The occupancy of endothelial protein C receptor by the inactive protein C mutant S195A switches the receptor PAR-1-dependent signaling specificity of thrombin leading to thrombin inhibition of the expression of cell surface adhesion molecules CCAM-I, ICAM-I and E-selectin as well as the binding of neutrophils to tumor necrosis factor alpha-activated endothelial cells. Both thrombin and thrombin receptor agonist peptides activate Rac I and inhibit the activation of RhoA and nuclear factor kappaB pathways in response to tumor necrosis factor alpha in cells pretreated with protein C mutant S195A
-
-
?
additional information
?
-
-
in cell cultures of HUVEC and HPAEC cells, low concentrations of thrombin or of receptor PAR-1 agonist peptide induce significant anti-inflammatory activities. Relatively high concentration of thrombin or of PAR-1 agonist peptide show pro-inflammatory activities. The direct anti-inflammatory effects of low concentrations of thrombin are dependent on the activation of PAR-1 and PI3 kinase
-
-
?
additional information
?
-
-
treatment of platelets with thrombin or ADP induces activation and mitochondrial association of active proapoptotic proteins Bid, Bax, and Bak. Thrombin evokes mitochondrial membrane depolarization, which is attenuated by catalase
-
-
?
additional information
?
-
-
thrombin is generated by proteolysis of its precursor prothrombin at sites of injury
-
-
?
additional information
?
-
-
nestin gene expression is regulated by the thrombin-mediated transactivation of EGFR in serum-deprived primary cultures of vascular smooth muscle cells. Upon binding of thrombin, regulator PAR-1 induces c-Src resulting in direct intracellular phosphorylation of EGFR and in the extracellular activation of the matrix metalloprotease MMP-2-mediated shedding of HB-epidermal growth factor
-
-
?
additional information
?
-
-
the presence of thrombin induces a significant increase in matrix metalloprotease-9 activity and also increases its mRNA expression in primary astrocytes. Thrombin-induced matrix metalloprotease-9 production is inhibited by the selective inhibitor of protease-activated receptor PAR-1, SCH 79797 and by PDS98059
-
-
?
additional information
?
-
-
enzyme stimulates platelets and exposure of phosphatidylserine on the external surface
-
?
additional information
?
-
-
following activation of platelets by thrombin, 26 proteins exhibit statistically significant differences. Deregulated proteins include proteins of the coagulation system and integrin signalling
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
K+
Na+
additional information
K+
-
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+
-
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+
-
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+
-
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+
-
two-step mechanism of Na+ binding to thrombin resolved by ultra-rapid kinetics
Na+
-
Na+ activates thrombin by securing the correct orientation of the Glu192-Gly193 peptide bond, which is likely flipped in the absence of cation
additional information
-
mutants show reduced specificity for monovalent cations compared to the wild-type enzyme
additional information
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R)-2-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-cyclohexyl-2-oxoethanaminium chloride
-
-
(1R)-2-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-cyclopentyl-2-oxoethanaminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-oxo-3-phenylpropan-2-aminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-oxobutan-2-aminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-oxopropan-2-aminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-3,3-dimethyl-1-oxobutan-2-aminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-3-cyclohexyl-1-oxopropan-2-aminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-aminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-4,4-dimethyl-1-oxopentan-2-aminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-4-methyl-1-oxopentan-2-aminium chloride
-
-
(2S)-1-(1,3-benzodioxol-5-ylacetyl)-N-(thiophen-2-ylmethyl)pyrrolidine-2-carboxamide
-
-
(2S)-1-[(2R)-2-amino-3-(1,3-benzodioxol-5-yl)propanoyl]-N-methylpyrrolidine-2-carboxamide
-
-
(2S)-1-[(2R)-2-amino-3-(1,3-benzodioxol-5-yl)propanoyl]-N-propylpyrrolidine-2-carboxamide
-
-
(2S)-1-[(2R)-2-amino-3-(4-chlorophenyl)propanoyl]-N-(thiophen-2-ylmethyl)pyrrolidine-2-carboxamide
-
-
(2S)-1-[(2R)-2-amino-3-(4-chlorophenyl)propanoyl]-N-propylpyrrolidine-2-carboxamide
-
-
(2S)-1-[(2R)-2-amino-3-cyclohexylpropanoyl]-N-methylpyrrolidine-2-carboxamide
-
-
(2S)-1-[(2R)-2-aminobutanoyl]-N-(4-carbamimidoylbenzyl)pyrrolidine-2-carboxamide
-
-
(2S)-1-[(2R)-2-cyclohexyl-2-hydroxyacetyl]-N-(2-methoxyethyl)pyrrolidine-2-carboxamide
-
-
(2S)-1-[3-(4-chlorophenyl)propanoyl]-N-(2-methoxyethyl)pyrrolidine-2-carboxamide
-
-
(2S)-1-[3-(4-chlorophenyl)propanoyl]-N-(thiophen-2-ylmethyl)pyrrolidine-2-carboxamide
-
-
(3E)-N-(1,3-benzodioxol-5-yl)-2-[(4-carbamimidoylphenyl)amino]-4-(4-hydroxy-3-methoxyphenyl)but-3-enamide
-
-
(E)-2-(3-aminophenyl)-N-(3-[[1-(1-benzothiophen-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)ethenesulfonamide
-
89% inhibition at 0.01 mM
(E)-2-(3-bromophenyl)-N-[3-[2-(3-chlorobenzyl)-2H-tetrazol-5-yl]phenyl]ethenesulfonamide
-
19% inhibition at 0.01 mM
(E)-2-(3-chlorophenyl)-N-(3-[[1-(1H-indol-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)ethenesulfonamide
-
76% inhibition at 0.01 mM
(E)-2-(3-chlorophenyl)-N-(3-[[1-(pyridin-3-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)ethenesulfonamide
-
24% inhibition at 0.01 mM
(E)-2-(3-chlorophenyl)-N-(3-[[1-(thiophen-3-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)ethenesulfonamide
-
59% inhibition at 0.01 mM
(E)-2-(3-fluorophenyl)-N-(3-[[1-(pyridin-3-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)ethenesulfonamide
-
29% inhibition at 0.01 mM
(E)-2-(3-nitrophenyl)-N-(3-[[1-(pyridin-3-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)ethenesulfonamide
-
30% inhibition at 0.01 mM
(E)-N-(3-[[1-(1,3-benzothiazol-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-(3-chlorophenyl)ethenesulfonamide
-
81% inhibition at 0.01 mM
(E)-N-(3-[[1-(1,3-benzothiazol-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-(3-nitrophenyl)ethenesulfonamide
-
81% inhibition at 0.01 mM
(E)-N-(3-[[1-(1-benzothiophen-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-(3-chlorophenyl)ethenesulfonamide
-
94% inhibition at 0.01 mM
(E)-N-(3-[[1-(1-benzothiophen-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-(3-fluorophenyl)ethenesulfonamide
-
88% inhibition at 0.01 mM
(E)-N-(3-[[1-(1-benzothiophen-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-(3-nitrophenyl)ethenesulfonamide
-
94% inhibition at 0.01 mM
(E)-N-(3-[[1-(1-benzothiophen-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-[3-(trifluoromethyl)phenyl]ethenesulfonamide
-
91% inhibition at 0.01 mM
(E)-N-(3-[[1-(1H-indol-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-(3-nitrophenyl)ethenesulfonamide
-
82% inhibition at 0.01 mM
(E)-N-(3-[[1-(3-chlorobenzyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-(3-chlorophenyl)ethenesulfonamide
-
50% inhibition at 0.01 mM
(E)-N-(3-[[1-(pyridin-3-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-[3-(trifluoromethyl)phenyl]ethenesulfonamide
-
42% inhibition at 0.01 mM
(E)-N-[3-([1-[(2-bromothiophen-3-yl)methyl]-1H-1,2,3-triazol-4-yl]methoxy)phenyl]-2-(3-chlorophenyl)ethenesulfonamide
-
73% inhibition at 0.01 mM
(E)-N-[3-[(1-benzyl-1H-1,2,3-triazol-4-yl)methoxy]phenyl]-2-(3-chlorophenyl)ethenesulfonamide
-
63% inhibition at 0.01 mM
(E)-N-[3-[2-(3-chlorobenzyl)-2H-tetrazol-5-yl]phenyl]-2-(3-chlorophenyl)ethenesulfonamide
-
5% inhibition at 0.01 mM
(E)-N-[3-[2-(3-chlorobenzyl)-2H-tetrazol-5-yl]phenyl]-2-(3-fluorophenyl)ethenesulfonamide
-
76% inhibition at 0.01 mM
(E)-N-[3-[2-(3-chlorobenzyl)-2H-tetrazol-5-yl]phenyl]-2-(3-methoxyphenyl)ethenesulfonamide
-
7% inhibition at 0.01 mM
(E)-N-[3-[2-(3-chlorobenzyl)-2H-tetrazol-5-yl]phenyl]-2-(3-methylphenyl)ethenesulfonamide
-
77% inhibition at 0.01 mM
(E)-N-[3-[2-(3-chlorobenzyl)-2H-tetrazol-5-yl]phenyl]-2-(3-nitrophenyl)ethenesulfonamide
-
46% inhibition at 0.01 mM
(E)-N-[3-[2-(3-chlorobenzyl)-2H-tetrazol-5-yl]phenyl]-2-[3-(trifluoromethyl)phenyl]ethenesulfonamide
-
32% inhibition at 0.01 mM
1-(2-amino-2-cyclohexyl-acetyl)-pyrrolidine-2-carboxylic acid isobutyl-amide
-
-
1-(2-cyclohexyl-2-phenylmethanesulfonylamino-acetyl)-pyrrolidine-2-carboxylic acid methylamide
-
-
1-(methylsulfonyl)-4-[N-(naphthalen-2-ylsulfonyl)glycyl-3-carbamimidoylphenylalanyl]piperazine
-
-
1-[2-amino-3-(4-chloro-phenyl)-propionyl]-pyrrolidine-2-carboxylic acid methylamide
-
-
1-[N-(naphthalen-2-ylsulfonyl)glycyl-4-carbamimidoyl-L-phenylalanyl]piperidine
-
-
1-[N-[2-(amidino-N'-methylaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(2-[4-methylphenyl]ethylamino)pyrazinone
-
-
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-chloro-3-[2,2-difluoro-2-phenylethylamino]pyrazinone
-
-
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-cyano-3-[2,2-difluoro-2-phenylethylamino]pyrazinone
-
-
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(2,2-diphenylethylamino)pyrazinone
-
-
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(2-[2,4-difluorophenyl]ethylamino)pyrazinone
-
-
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(2-[3,4-difluorophenyl]ethylamino)pyrazinone
-
-
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(2-[4-trifluoromethylphenyl]ethylamino)pyrazinone
-
-
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(2-[5-indanyl]ethylamino)pyrazinone
-
-
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(3,4-dimethoxyphenylethylamino)pyrazinone
-
-
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(4-ethylphenethylamino)pyrazinone
-
-
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(4-fluorophenethylamino)pyrazinone
-
-
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(4-methoxyphenethylamino)pyrazinone
-
-
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-[2,2-difluoro-2-phenylethylamino]pyrazinone
-
RWJ-671818
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-[2-(1-naphthalene)ethyl]aminopyrazinone
-
-
15-TBA15/TBA29/sulf-Gal-AuNPs
-
most effective conjugated gold nanoparticle constructed with 15 thrombin-binding aptamers, comprising TBA15 and 15 TBA29 molecules, per AuNP. These exhibit, because of their particularly flexible conformation and multivalency, an ultrahigh binding affinity toward thrombin and thus extremely high anticoagulant/inhibitory potency
-
2-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-2-oxoethanaminium chloride
-
-
2-[(3-carbamimidoylphenyl)amino]-2-(2,3-dimethoxyphenyl)-N-(diphenylmethyl)acetamide
-
-
2-[(3-carbamimidoylphenyl)amino]-2-(3,4-diphenoxyphenyl)-N-(naphthalen-1-ylmethyl)acetamide
-
-
2-[(3-carbamimidoylphenyl)amino]-2-(3-ethoxy-4-hydroxyphenyl)-N-hexylacetamide
-
-
2-[(3-carbamimidoylphenyl)amino]-N-(3,4-dimethoxybenzyl)-2-[3-(4-methylphenoxy)phenyl]acetamide
-
-
2-[(3-carbamimidoylphenyl)amino]-N-(4-methylbenzyl)-2-[3-(4-methylphenoxy)phenyl]acetamide
-
-
2-[(3-carbamimidoylphenyl)amino]-N-(diphenylmethyl)-2-(3-ethoxy-4-methoxyphenyl)acetamide
-
-
2-[(4-carbamimidoylphenyl)amino]-2-(3-methoxy-4-phenoxyphenyl)-N-(4-methylbenzyl)acetamide
-
-
2-[(4-carbamimidoylphenyl)amino]-2-(3-methoxy-4-phenoxyphenyl)-N-(naphthalen-2-ylmethyl)acetamide
-
-
2-[(4-carbamimidoylphenyl)amino]-N-[2-(3,4-dimethoxyphenyl)ethyl]-2-(3-methoxy-4-phenoxyphenyl)acetamide
-
-
3-(benzyl(2-(4-carbamimidoylbenzyl)-4-methyl-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-7-yl)amino)-3-oxopropanoic acid
-
112400fold selectivity for thrombin over trypsin, 52450fold selectivitiy for thrombin over factor Xa
3-(benzyl(2-(4-carbamimidoylbenzyl)-4-methyl-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-7-yl)amino)-4-oxobutanoic acid
-
1131fold selectivity for thrombin over trypsin, 2427fold selectivitiy for thrombin over factor Xa
3-carboxy-2-methyl-1-benzofuran-5,6-diyl disulfate
-
about 70% inhibition at 2.6 mM
3-carboxy-5-methoxy-2-methyl-1-benzofuran-6-yl sulfate
-
about 80% inhibition at 2.6 mM
3-carboxy-6-methoxy-2-methyl-1-benzofuran-5-yl sulfate
-
about 40% inhibition at 2.6 mM
3-[(2S)-3-(4-benzylpiperidin-1-yl)-2-[(naphthalen-2-ylsulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
-
4-carbamimidoyl-N-[3-[(naphthalen-2-yloxy)sulfonyl]propanoyl]phenylalanyl-L-proline
-
-
4-methyl-1-[N-(naphthalen-2-ylsulfonyl)glycyl-3-carbamimidoylphenylalanyl]piperidine
-
-
4-methylphenyl 3-[[(2S)-3-(4-carbamimidoylphenyl)-1-(2-methoxypyrrolidin-1-yl)-1-oxopropan-2-yl]amino]-3-oxopropane-1-sulfonate
-
-
4-[(1R,3aS,4S,8aS,8bS)-2-(1,3-benzodioxol-5-ylmethyl)-1-cyclopropyl-3a,8a,8b-trimethyl-3-oxodecahydropyrrolo[3,4-a]pyrrolizin-4-yl]benzenecarboximidamide
-
-
4-[(1R,3aS,4S,8aS,8bS)-2-(1,3-benzodioxol-5-ylmethyl)-1-ethyl-3a,8a,8b-trimethyl-3-oxodecahydropyrrolo[3,4-a]pyrrolizin-4-yl]benzenecarboximidamide
-
-
4-[(1R,3aS,4S,8aS,8bS)-2-(4-chlorobenzyl)-3a,8a,8b-trimethyl-3-oxo-1-(propan-2-yl)decahydropyrrolo[3,4-a]pyrrolizin-4-yl]benzenecarboximidamide
-
-
4-[(1R,3aS,4S,8aS,8bS)-2-(4-methoxybenzyl)-3a,8a,8b-trimethyl-3-oxo-1-(propan-2-yl)decahydropyrrolo[3,4-a]pyrrolizin-4-yl]benzenecarboximidamide
-
-
4-[(1S,3aS,4R,6aS)-5-(1,3-benzodioxol-5-ylmethyl)-4-ethyl-2,3,3,3a,6a-pentamethyl-6-oxooctahydropyrrolo[3,4-c]pyrrol-1-yl]benzenecarboximidamide
-
-
4-[(2S)-2-[(naphthalen-2-ylsulfonyl)amino]-3-oxo-3-(piperidin-1-yl)propyl]benzenecarboximidamide
-
-
4-[(2S)-3-(4-acetylpiperazin-1-yl)-2-[(naphthalen-2-ylsulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
-
4-[(3aS,4S,7R,8aS,8bR)-2-(1,3-benzodioxol-5-ylmethyl)-7-hydroxy-3a,8a,8b-trimethyl-1,3-dioxodecahydropyrrolo[3,4-a]pyrrolizin-4-yl]benzenecarboximidamide
-
-
5,6-dihydroxy-2-methyl-1-benzofuran-3-carboxylic acid
-
about 20% inhibition at 2.6 mM
5-hydroxy-6-methoxy-2-methyl-1-benzofuran-3-carboxylic acid
-
about 25% inhibition at 2.6 mM
activated protein C
-
activated protein C has a regulatory function in inhibiting thrombin activation, overview
-
amino[4-([[1-(3,3-dimethylbutanoyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
-
amino[4-([[1-(3-cyclohexylpropanoyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
-
amino[4-([[1-(3-cyclopentylpropanoyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
-
amino[4-([[1-(3-methylbutanoyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
-
amino[4-([[1-(3-phenylpropanoyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
-
amino[4-([[1-(4-methylpentanoyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
-
amino[4-([[1-(cyclohexylacetyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
-
amino[4-([[1-(cyclopentylacetyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
-
amino[4-[([[(2S)-1-butanoylpyrrolidin-2-yl]carbonyl]amino)methyl]phenyl]methaniminium chloride
-
-
amino[4-[([[(2S)-1-propanoylpyrrolidin-2-yl]carbonyl]amino)methyl]phenyl]methaniminium chloride
-
-
angiomax
-
conjugation of angiomax to a 5'-amino oligonucleotide and assembly into a two-dimensional DNA lattice for observation of the binding of thrombins to the DNA lattice. Use of the functionalized DNA lattices as a platform for investigation of biomolecular interactions such as drug-protein, protein-protein, DNA-RNA, and DNA-protein interactions in the nano- and subnanoscales
anti-thrombin
-
human, enhanced in presence of heparin and dermatan sulfate, hirudin(54-65) peptide protects
-
ARH-067637
-
the prodrug AZD-0837 is bioactively converted into the direct thrombin inhibitor ARH-067637
Asp-Tyr-Asp-Tyr-Gln
-
a pentapeptide encompassing amino acid sequence 695–699 from the C-terminus of the heavy chain of factor Va inhibits prothrombin activation by prothrombinase in a competitive manner with respect to substrate, mechanism, overview
AZD-0837
-
direct thrombin inhibitor, the prodrug AZD-0837 is bioactively converted into the direct thrombin inhibitor ARH-067637
benzyloxycarbonyl-D-Dpa-Pro-Mpg(OPh)2
-
tripeptide acyl (alpha-aminoalkyl)phosphonate inhibitor, acts via formation of a metastable pentacoordinated phosphorus intermediate that is non-covalently bound to Ser195, inhibition mechanism
Cds03
-
CdsO3 binds to exosite II of thrombin to allosterically disrupt the catalytic apparatus resulting in inhibition
-
D-phenylalanyl-L-prolyl-L-arginyl-L-prolylglycine
-
complete inhibition at 20 mM
dermatan sulfate
-
isolated from skin of Raja radula, in presence of heparin cofactor II or antithrombin. Dermatan sulfate from ray skin catalyzes the thrombin inhibition by heparin cofactor II or antithrombin primarily by forming a dermatan sulfate-inhibitor complex more reactive than the free inhibitor towards the protease
diethyl [([[(3-carbamimidoylphenyl)amino](3,4-diphenoxyphenyl)acetyl]amino)methyl]phosphonate
-
-
diethyl [([[(4-carbamimidoylphenyl)amino](4-phenoxyphenyl)acetyl]amino)methyl]phosphonate
-
-
diethyl [([[2-(benzyloxy)phenyl][(3-carbamimidoylphenyl)amino]acetyl]amino)methyl]phosphonate
-
-
dipetalogastin II
-
strong inhibitor, fron the assassin bug Dipetalogaster maximus
-
dipetarudin
-
cloning and purification of the chimeric inhibitor composed of the N-terminal head structure of dipetalogastin II and the exosite 1 blcking segment of hirudin, connected through a five glycine linker, MW 7560
-
DNA aptamer 15-TBA
-
a thrombin-binding aptamer that binds to thrombin exosites, noncompetitive inhibition type
-
DNA aptamer 31-TBA
-
a thrombin-binding aptamer that binds to thrombin exosites, competitive inhibition type
-
DV23
-
i.e. SDQGDVAEPKMHKTAPPFDFEAIPEEYLDDES, a variegin variant, a fast, tight-binding, competitive inhibitor
DV23K10R
-
i.e. SDQGDVAEPRMHKTAPPFDFEAIPEEYLDDES, a variegin variant, a fast, tight-binding, competitive inhibitor
DV24
-
i.e. SDQGDVAEPKMHKTAPPFDFEAIPEEYLDDES, a variegin variant, a fast, tight-binding, competitive inhibitor
DV24H12A
-
i.e. SDQGDVAEPKMAKTAPPFDFEAIPEEYLDDES, a variegin variant, a fast, tight-binding, competitive inhibitor
DV24K10R
-
i.e. SDQGDVAEPRMHKTAPPFDFEAIPEEYLDDES, a variegin variant, a fast, tight-binding, competitive inhibitor
DV24K10RYphos
-
i.e. SDQGDVAEPRMHKTAPPFDFEAIPEEYphosLDDES, a variegin variant, a fast, tight-binding, competitive inhibitor
DV24K10RYsulf
-
i.e. SDQGDVAEPRMHKTAPPFDFEAIPEEYsulfLDDE, a variegin variant, a fast, tight-binding, competitive inhibitor
DV24Yphos
-
i.e. SDQGDVAEPKMHKTAPPFDFEAIPEEYphosLDDE, a variegin variant, a fast, tight-binding, competitive inhibitor
DV24Ysulf
-
i.e. SDQGDVAEPKMHKTAPPFDFEAIPEEYsulfLDDE, a variegin variant, a fast, tight-binding, competitive inhibitor
EP21
-
i.e. SDQGDVAEPKMHKTAPPFDFEAIPEEYLDDES, a variegin variant, a slow, tight-binding, competitive inhibitor
EP25
-
i.e. SDQGDVAEPKMHKTAPPFDFEAIPEEYLDDES, a variegin variant, a slow, tight-binding, competitive inhibitor
EP25A22E
-
i.e. SDQGDVAEPKMHKTAPPFDFEEIPEEYLDDES, a variegin variant, a fast, tight-binding, competitive inhibitor
ethyl 2-(benzyl(2-(4-carbamimidoylbenzyl)-4-methyl-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-7-yl)amino)-2-oxoacetate
-
1188fold selectivity for thrombin over trypsin, 537fold selectivitiy for thrombin over factor Xa
ethyl N-[(2-[[(4-carbamimidoylphenyl)amino]methyl]-1-methyl-1H-benzimidazol-5-yl)carbonyl]-N-pyridin-2-yl-b-alaninate
-
-
factor VIII(716-731) peptide
-
thrombin binding sequence is GDYYEDSYEDISAYLL, competitive
-
FeSO4
-
incubation of thrombin with iron sulfate in a final concentration of 0.2 mM for 25-35 min is followed by the loss of thrombin activity, the effect of reversibility depends on the time (0-100 min) of thrombin preincubation with iron. Inactivation of thrombin occurs immediately after addition of Fe2+ ions in high doses
fibrin gamma'-peptides
-
sulfated and non-sulfated peptide sequences of the gamma'-chains of human fibrin 1 and 2, overview, competitive
-
fibrinogen 2
-
more potent inhibition compared to fibrinogen 1, down-regulation of thromin production
-
fibrinogen gamma'(408-427) peptide
-
of the gamma'-domain, thrombin binding sequence is VRPEHPAETEYDSLYPEDDL, competitive
-
formyl-L-Asp-L-Phe methyl ester
-
biphasic inhibition, 80% inhibition at 2.52 mM, inhibition is reversible
fucosylated chondroitin sulfate
-
from sea cucumber Ludwigothurea grisea, chemical composition, native or desulfated, carboxyl-reduced, or defucosylated, inhibitory potential in anticoagulation assay, overview, presence of antithrombin or heparin cofactor II is required for inhibition, inhibition of thrombin generation by thromboplastin
-
glycoprotein Ibalpha(1-282) peptide
-
binds to exosite II of the enzyme, inhibits activation of factor VIII to more than 70%
-
glycoprotein Ibalpha(268-282) peptide
-
binds to exosite II of the enzyme, inhibits activation of factor VIII and cleavage of factor VIII(341-376) peptide to more than 70%
-
glycosaminoglycan AD4
-
shows only small inhibitory activity toward thrombin and the inhibition does not proceed beyond 40% inhibition
-
glycosaminoglycan AD9
-
shows only small inhibitory activity toward thrombin and the inhibition does not proceed beyond 40% inhibition
-
GR166081
-
5-[5-(4-hydroxy-phenyl)-2-oxo-3,3a,8,8a,tetrahydro-2H-indeno[2,1-b]furan-3-yl]-pentanamidine
GR167088
-
5-[5-(4-methoxy-phenyl)-2-oxo-3,3a,8,8a-tetrahydro-2H-indeno[2,1-b]furan-3-yl]-pentanamide
GR179849
-
4-[3-(4-carbamidoyl-butyl)-2-oxo-1,2,3,3a,8,8a-hexahydro-cyclopenta[a]inden-5-yl]-N,N-diethylbenzamide
HD1-22
-
bivalent fusion aptamer consisiting of 15-base spanning DNA aptamer HD1 which specifically inhibits the procoagulant functions of thrombin, and aptamer HD22 which binds to exosite 2 of thrombin, interconnected by a poly-dA linker. Aptamer HD1-22 prolongs clotting times of the thrombin time, activated partial thromboplastin time, ecarin clotting time, and lag-time of the tissue factor triggered thrombin generation assay. thrombin-induced platelet aggregation is more effectively inhibited by HD1-22 than by bivalirudin. The anticoagulant activities of HD1-22 are fully reversed by addition of antidote-oligodeoxynucleotides
-
hemalin
-
protein of about 20 kDa, isolated from a midgut cDNA library from the hard tick Haemaphysalis longicornis. Hemalin delays bovine plasma clotting time and inhibits both thrombin-induced fibrinogen clotting and platelet aggregation. Hemalin may play a role in tick blood feeding
-
hirudin(53-64) peptide
-
thrombin binding sequence is NGDFEEIPEEYL, competitive
-
hirulog-1
-
i.e. bivalirudin or DFPRPGGGGNGDFEEIPEEYL, a variegin variant, a fast, tight-binding, competitive inhibitor
human GPIBalpha(269-287) peptide
-
thrombin binding sequence is DEGDTDLYDYYPEEDTEGD, competitive
-
human heparin cofactor II(56-75) peptide
-
thrombin binding sequences are GEEDDDYLDLE and EDDDYIDIVD, competitive
-
human PAR1(52-69) peptide
-
thrombin binding sequence is YEPFWEDEEKNESGLTEY, competitive
-
inhibitor from Dipetalogaster maximus
-
a bloodsucking bug, anticoagulant inhibitor, biochemical characterization: slow, tight-binding, N-terminal amino acid sequencing, molecular mass of the four components each about 12 kDa, 9304.7 anti-IU/mg protein
-
isorhamnetin 3-O-(6-O-alpha-L-rhamnopyranosyl)-beta-D-glucopyranoside
-
slight inhibition
kaempferol 3-O-(2-O-alpha-L-rhamnopyranosyl)-beta-D-glucopyranoside
-
slight inhibition
methyl (3S)-1-[3-carbamimidoyl-N-(naphthalen-2-ylsulfonyl)phenylalanyl]-2-oxopiperidine-3-carboxylate
-
-
methyl (3S)-1-[3-carbamimidoyl-N-(naphthalen-2-ylsulfonyl)phenylalanyl]piperidine-3-carboxylate
-
-
methyl N-[(4-tert-butylphenyl)sulfonyl]glycyl-3-carbamimidoyl-L-phenylalaninate
-
-
methyl N-[[2-(benzyloxy)phenyl][(3-carbamimidoylphenyl)amino]acetyl]-3-(phenyldisulfanyl)alaninate
-
-
methyl N-[[4-(hydroxymethyl)-2,3,6-trimethylphenyl]sulfonyl]glycyl-3-carbamimidoyl-L-phenylalaninate
-
-
methyl S-benzyl-N-[[(3-carbamimidoylphenyl)amino](2,3-dimethoxyphenyl)acetyl]cysteinate
-
-
methyl S-benzyl-N-[[(4-carbamimidoylphenyl)amino](2-fluoro-4,5-dimethoxyphenyl)acetyl]cysteinate
-
-
MH18
-
i.e. SDQGDVAEPKMHKTAPPFDFEAIPEEYLDDES, a variegin variant, a fast, tight-binding, noncompetitive inhibitor
MH18H12A
-
i.e. SDQGDVAEPKMAKTAPPFDFEAIPEEYLDDES, a variegin variant, a fast, tight-binding, noncompetitive inhibitor
MH18Ysulf
-
i.e. SDQGDVAEPKMHKTAPPFDFEAIPEEYsulfLDDES, a variegin variant, a fast, tight-binding, noncompetitive inhibitor
MH22
-
i.e. SDQGDVAEPKMHKTAPPFDFEAIPEEYLDDES, a variegin variant, a fast, tight-binding, noncompetitive inhibitor
MH22A22E
-
i.e. SDQGDVAEPKMHKTAPPFDFEEIPEEYLDDES, a variegin variant, a fast, tight-binding, noncompetitive inhibitor
N-(4-carbamimidoylbenzyl)-2-(1-[[(4-chloro-2-methoxyphenyl)sulfonyl]amino]-4-methyl-2-oxo-1,2-dihydropyridin-3-yl)acetamide
-
13fold selectivity for thrombim over trypsin
N-(4-carbamimidoylbenzyl)-2-(1-[[2-(2,5-dimethylphenyl)ethyl]amino]-4-methyl-2-oxo-1,2-dihydropyridin-3-yl)acetamide
-
23fold selectivity for thrombim over trypsin
N-(4-carbamimidoylbenzyl)-2-(4-methyl-1-[[2-(2-methylphenyl)ethyl]amino]-2-oxo-1,2-dihydropyridin-3-yl)acetamide
-
42fold selectivity for thrombim over trypsin
N-(4-carbamimidoylbenzyl)-2-[4-methyl-2-oxo-1-[(2-phenylethyl)amino]-1,2-dihydropyridin-3-yl]acetamide
-
16fold selectivity for thrombim over trypsin
N-alpha-(2-naphthylsulfonyl-glycyl)-4-amidinophenylalanine-piperidine
i.e. alpha-NAPAP
N-benzyl-2-[(4-carbamimidoylphenyl)amino]-2-(3-methoxy-4-phenoxyphenyl)acetamide
-
-
N-[(1R)-2-[(2S)-2-[(4-carbamimidoylbenzyl)carbamoyl]azetidin-1-yl]-1-cyclohexyl-2-oxoethyl]glycine
-
-
N-[3-[2-(3-chlorobenzyl)-2H-tetrazol-5-yl]phenyl]methanesulfonamide
-
45% inhibition at 0.01 mM
N-[4-[amino(iminio)methyl]benzyl]-1-[(2R)-2-ammonio-2-cyclohexylacetyl]-L-prolinamide dichloride
-
-
N-[4-[amino(iminio)methyl]benzyl]-1-[(2R)-2-ammonio-3,3-dimethylbutanoyl]-L-prolinamide dichloride
-
-
N-[4-[amino(iminio)methyl]benzyl]-1-[(2R)-2-ammonio-3-methylbutanoyl]-L-prolinamide dichloride
-
-
N-[4-[amino(iminio)methyl]benzyl]-1-[(2R)-2-ammonio-3-phenylpropanoyl]-L-prolinamide dichloride
-
-
N-[4-[amino(iminio)methyl]benzyl]-1-[(2R)-2-ammonio-4,4-dimethylpentanoyl]-L-prolinamide dichloride
-
-
N-[4-[amino(iminio)methyl]benzyl]-1-[(2R)-2-ammonio-4-methylpentanoyl]-L-prolinamide dichloride
-
-
N-[4-[amino(iminio)methyl]benzyl]-1-[(2R)-2-ammoniobutanoyl]-L-prolinamide dichloride
-
-
naphthalen-2-yl 3-[[(2S)-3-(4-carbamimidoylphenyl)-1-oxo-1-(piperazin-1-yl)propan-2-yl]amino]-3-oxopropane-1-sulfonate
-
-
propan-2-yl N-(naphthalen-2-ylsulfonyl)glycyl-3-carbamimidoyl-D-phenylalaninate
-
-
RA-1008
-
a synthetic, low-molecular cyanopeptide-analogue inhibitor, binding structure and inhibition mechanism, overview
RA-1014
-
a synthetic, low-molecular cyanopeptide-analogue inhibitor, binding structure and inhibition mechanism, overview
RGD-hirudin
-
recombinant hirudin containing the RGD motif which competitively inhibits the binding of fibrinogen to GP IIb/IIIa on platelets. Specific anti-thrombin activity of RGD-hirudin is 12000 ATU/mg and equivalent to native hirudin, and it addiotionally inhibits platelet aggregation
-
RWJ-50353
-
carboxylated derivative of RWJ-51438, benzothiazole-activated inhibitor
RWJ-51438
-
benzothiazole-activated inhibitor, binds to His57 of the enzyme via hydrogen bond, the carboxylate substituent on the benzothiazole group forms salt bridges with Lys60F NZ and the NZ of the symmetry-related residues Lys236 and Lys240, which introduces steric effects that perturb the 60A-60I insertion loop, especially at residues Trp60D and Phe60H
sodium 3-(2-carboxyethyl)-6-methoxy-2-methyl-1-benzofuran-5-yl sulfate
-
about 35% inhibition at 2.6 mM
sodium 3-(5-hydroxy-6-methoxy-2-methyl-1-benzofuran-3-yl)propanoate
-
about 40% inhibition at 2.6 mM
sulfated fucan
-
from brown seaweed Ascophylum nodosum, chemical composition, inhibitory potential in anticoagulation assay, inhibition of thrombin generation by thromboplastin
-
sulfated glycoprotein Ibalpha(268-282) peptide
-
sulfated at all tyrosine residues, binds to exosite II of the enzyme, inhibits activation of factor VIII and cleavage of factor VIII(341-376) peptide to more than 70%
-
sulfated polysaccharides from green algae
-
8 different variants of Codium sp., Caulerpa okamura, Caulerpa brachypus, Monostroma nitidum and Monostrum latissimum, composition overview, inhibition is mediated by heparin cofactor HCII, hirudin(54-65) peptide protects partially, HD22, a ssDNA aptamer, also protects, allosteric inhibition mechanism
-
suramin
i.e. 8, 8'-[carbonylbis[imino-3,1-phenylenecarbonylimino(4-methyl-3,1-phenylene)carbonylimino]]bis-1,3,5-naphthalenetrisulfonic acid, non-competitive inhibitor of human alpha-thrombin activity over fibrinogen
thrombin-binding aptamer
-
a consensus DNA 15-mer that binds specifically to human alpha-thrombin at nanomolar concentrations and inhibits its procoagulant functions. A a modified thrombin-binding aptamer, containing a 5'-5' inversion-of-polarity site, is more stable and to possesses a higher thrombin affinity than its unmodified counterpart
-
Thrombomodulin
-
complex formation on endothelial cell surfaces blocks thrombin activity
-
thrombomodulin(408-426) peptide
-
thrombin binding sequence is GDYYEDSYEDISAYLL, competitive
-
tinzaparin
-
a low-molecular-weight heparin, an effective inhibitor of thrombin generation and thrombin activity in plasma
-
variegin
-
i.e. SDQGDVAEPKMHKTAPPFDFEAIPEEYLDDES, isolated from the tropical bont tick, the molecule exhibits a unique two-modes inhibitory property on thrombin active site, i.e. competitive before cleavage, noncompetitive after cleavage, overview. Mechanism of thrombin inhibition by disrupting the charge relay system, a fast, tight-binding, competitive inhibitor
[4-[([[(2S)-1-acetylpyrrolidin-2-yl]carbonyl]amino)methyl]phenyl](amino)methaniminium chloride
-
-
[6-chloro-3-(2,2-difluoro-2-phenyl-ethylamino)-2-oxo-2H-pyrazin-1-yl]acetic acid
-
-
[amino(4-[[([(2S)-1-[(2R)-2-ammoniopropanoyl]pyrrolidin-2-yl]carbonyl)amino]methyl]phenyl)methylidene]ammonium dichloride
-
-
antithrombin
wild-type and mutant DELTAK9, the mutant shows 20fold lower susceptibility than the wild-type
-
antithrombin
-
presence of dermatan sulfate increases the rate constant for inhibition by forming a dermatan sulfate-antithrombin complex more reactive than free antithrombin towards thrombin
-
AR-H067637
-
selective direct thrombin inhibitor, AZD0837 is bioconverted to its active form AR-H067637
argatroban
-
i.e. (2R,4R)-1-[(2S)-5(diaminomethylideneamino)-2-[[(3R)-3-methyl-1,2,3,4-tetrahydroquinolin-8-yl]sulfonylamino]pentanoyl]-4-methyl-piperidine-2-carboxylic acid
argatroban
-
thrombin inhibition by argatroban improves neurological outcomes and provides neuroprotection against acute events after subarachnoid hemorrhage such as blood-brain barrier disruption, brain edema, and cell death
AZD0837
-
AZD0837 is the prodrug of ARH06737, a potent, competitive, reversible inhibitor of free and fibrin-bound thrombin
dabigatran
-
comparison of thrombin inhibitors dabigatran and enoxaparin in unilateral total knee arthroplasty patients after surgery. Dabigatran shows inferior efficacy to enoxaparin. Bleeding rates are similar, and no drug-related hepatic illness has been recognized
dabigatran
-
i.e. N-[2-(4-amidinophenylaminomethyl)-1-methyl-1H-benzimidazol-5-ylcarbonyl]-N-(2-pyridinyl)-beta-alanine, direct thrombin inhibitor, dabigatran inhibits thrombin-induced cell proliferation at concentrations of 50-1000 ng/ml
dabigatran
-
BIBR 953, potent competitive and reversible inhibitor of thrombin, inhibiting both thrombin activity and generation, dabigatran displays highly selective, rapid, and reversible binding to thrombin8 and potently inhibits platelet aggregation with a concentration that produces 50% inhibition similar to the Ki of thrombin
dabigatran
-
specific, competitive and reversible inhibitor of thrombin, dabigatran binds to the active site of thrombin via hydrophobic interactions and can inhibit both free and fibrin-bound thrombin
dabigatran etexilate
-
the commercial preparation name is Pradaxa, also named BIBR 1048, potent, non-peptidic small molecule that specifically and reversibly inhibits both free and clot-bound thrombin by binding to the active site of thrombin
diisopropyl fluorophosphate
-
unlike alpha-thrombin, beta-thrombin is not protected from inhibition by diisopropyl fluorophosphate in the presence of fibrinogen
enoxaparin
-
comparison of thrombin inhibitors dabigatran and enoxaparin in unilateral total knee arthroplasty patients after surgery. Dabigatran shows inferior efficacy to enoxaparin. Bleeding rates are similar, and no drug-related hepatic illness has been recognized
enoxaparin
-
a low-molecular-weight heparin, an effective inhibitor of thrombin generation and thrombin activity in plasma
heparin
-
from porcine mucosa, inhibitory effect on fluid-phase and surface-bound thrombin in vivo in rabbits and in vitro
heparin
-
from porcine mucosa, inhibitory effect on fluid-phase and surface-bound thrombin in vivo in rabbits and in vitro
heparin
-
unfractionated, high inhibitory potential in anticoagulation assay, inhibition of thrombin generation by thromboplastin
heparin cofactor II
-
inhibitory effect on fluid-phase and surface-bound thrombin
-
heparin cofactor II
-
i.e. HCII, from human plasma, recombinant mutants, mediates enzyme inhibition with heparin, dermatan sulfate and sulfated polysaccharides from green algae Chlorophyta
-
heparin cofactor II
-
inhibitory effect on fluid-phase and surface-bound thrombin
-
heparin cofactor II
-
i.e. HCII, facilitated by heparin or dermatan sulfate in vitro, complex formation, these glycosaminoglycans are cleaved by leukocyte elastase in vivo which alters HCII and their influence on the enzyme in vivo, overview
-
heparin cofactor II
-
HCII, i.e. alpha1-antitrypsin, a serpin cofactor, contains a unique N-terminal extension that binds thrombin exosite 1, the mutant M358R is more active in inhibition of thrombin than the wild-type protein, maximal enhancement of alpha1-PI M358R activity requires the acidic residues between HCII residues 55 and 75
-
heparin cofactor II
-
presence of beta2-glycoprotein I protects thrombin against inactivation by heparin cofactor II. Cleavage of beta2-glycoprotein I at residues K317-T318 abrogates its protective effect
-
heparin cofactor II
-
presence of dermatan sulfate increases the rate constant for inhibition by forming a dermatan sulfate-heparin cofactor II complex more reactive than free heparin cofactor II towards thrombin
-
Hirudin
-
irreversible, direct thrombin inhibitor, competitive to fibrin, noncompetitive to fibrin
-
Hirudin
-
blocks interaction of enzyme with A1 subunit of substrate factor VIII
-
Hirudin
-
hirudin-(54-65) (an analog of the COOH terminus of hirudin), inhibits the exosite 2-mediated interaction of thrombin with immobilized gamma'-peptide
-
inogatran
-
i.e. carboxymethyl-(R)-cyclohexylalanyl-L-piperidine-2-carboxylic acid noragmatine
Intimatan
-
heparin cofactor II agonist, inhibitory effect on fluid-phase and surface-bound thrombin in vivo in rabbits and in vitro
Intimatan
-
heparin cofactor II agonist, inhibitory effect on fluid-phase and surface-bound thrombin in vivo in rabbits and in vitro
melagatran
-
i.e. carboxymethyl-(R)-cyclohexylglycine-L-azetidine-2-carboxylic acid 4-amidinobenzylamine
melagatran
-
reversible, active site directed direct thrombin inhibitor, active form of ximelagatran
melagatran
-
effect of introducing substituted amine residues with increased chain length in the P3 residue of melagatran. The association rate becomes faster when the lipophilicity of the inhibitors is increased. This is coupled to an increased enthalpic component and a corresponding decreased entropic component. The dissociation rates are reduced with an increase in chain length, with only a smaller increase and a decrease in the enthalpic and entropic components, respectively. The affinity increases with an increase in chain length, with similar changes in the enthalpic and entropic components. The interaction of melagatran is the most enthalpy-driven interaction. The orientation of the P1 and P2 parts of the molecules is very similar, but there are significant differences in the interaction between the terminal part of the P3 side chain and the binding pocket
thrombin inhibitor from Naja haje
-
thrombin inhibitor from Naja haje is a noncytotoxic phospholipase A2, mixed-type inhibitor of thrombin, inhibits the fibrinogenolytic and amidolytic activities of thrombin as well as its ability to induce platelet aggregation, it does not hydrolyze thrombin
-
thrombin inhibitor from Naja haje
-
thrombin inhibitor from Naja haje is a noncytotoxic phospholipase A2, mixed-type inhibitor of thrombin, inhibits the fibrinogenolytic and amidolytic activities of thrombin as well as its ability to induce platelet aggregation, it does not hydrolyze thrombin
-
additional information
-
a series of natural flavonoids as thrombin inhibitors, structure-activity relationships, molecular docking, overview
-
additional information
-
heparin and dermatan sulfate use different binding sites of HCII than the Chlorophyta sulfated polysaccharides, which are more effective inhibitors even with recombinant mutant HCII, that is no longer active with heparin and dermatan sulfate, overview
-
additional information
computational modeling, inhibitor binding mechanism, preference of binding of different benzamidine derivatives due to thermodynamic measurements and and hydration in descending order: 4-(2-oxo-1-propyl)benzamidine, 4-ethylbenzamidine, 4-(1-propyl)benzamidine, 4-methylbenzamidine, benzamidine, 4-amidinophenylpyruvate, inhibitors bind to Ser195
-
additional information
-
thrombin-mediated expression of interleukin-6 and CXCL8 is significantly inhibited by LY294002, AKT IV, RO318220, and GF109203X as well as by diphenyleneiodium at the messenger RNA and the protein levels. SB202129 and U0126 also significantly attenuate thrombin-mediated release of interleukin-6 and CXCL8 proteins from human aortic smooth muscle cell
-
additional information
-
the DNA aptamers 15TBA (GGTTGGTGTGGTTGG) and 31TBA (CACTGGTAGGTTGGTGTGGTTGGGGCCAGTG) added to human plasma dose-dependently increase fibrin formation upon exposure to exogenous thrombin, clotting activation by the extrinsic pathway, and activated partial clotting activation by the intrinsic pathway. At the same time, these aptamers do not modify amidolytic activity of thrombin
-
additional information
-
when gammaA/gammaA-fibrinogen is clotted with thrombin in the presence of HD22, gamma#-peptide (H-Val-Arg-Pro-Glu-His-Pro-Ala-Glu-Thr-Glu-Tyr(PO3H2)-Asp-Ser-Leu-Tyr(PO3H2)-Pro-Glu-Asp-Asp-Leu-OH), or prothrombin fragment 2 there is a dose-dependent and saturable decrease in thrombin binding to the resultant fibrin clots. HD22 reduces the affinity of thrombin for gammaA/gammaA-fibrin 6fold and accelerates the dissociation of thrombin from preformed gammaA/gammaA-fibrin clots
-
additional information
-
triazole/tetrazole-based sulfonamides as thrombin inhibitors, evaluation of selectivity and inhibitory potencies, overview. The triazole-based sulfonamides inhibit thrombin more efficiently than the tetrazole counterparts, binding of the triazole-based scaffold is enthalpically driven
-
additional information
-
incorporation of sulfated galactose acid into thrombin-binding aptamer-conjugated gold nanoparticles, TBA-AuNPs, increases the inhibitory potency against thrombin, method development and evaluation, overview. Usage of 15mer and 29mer aptamers and 13 nm gold particles. Reversible binding reaction
-
additional information
-
mechanism of inhibition and design of tunable thrombin inhibitors, structure-based design of 17 variegin variants, differing in potency, kinetics and mechanism of inhibition, in vivo antithrombotic effects of the variegin variants correlate well with their in vitro affinities for thrombin, overview
-
additional information
-
investigation on the effect of thrombin inhibitors on fibrinogen hydrolysis using a turbidimetric assay. There is a close relation between binding and inhibitory modes of the thrombin ligands. Active site- and exosite I-targeted ligands are able to inhibit fibrinogen hydrolysis completely. Macromolecular ligands affect fibrinogen hydrolysis in a competitive manner due to creation of the interacting area comparable to the thrombin-fibrinogen one. Low-molecular ligands probably form nonproductive complex interfering the appropriate orientation of substrate on the thrombin. Exosite II-targeted ligands are capable for only partial inhibition, indicating the fine tuning of the thrombin enzymatic activity via allosteric effects
-
additional information
-
a 12-residue peptide, which binds to an exosite alpha-thrombin and blocks the interaction of alpha-thrombin with fibrinogen and fibrin, competitively inhibits alpha-thrombin-catalyzed release of both fibrinopeptide B and activation peptide from the fibrin I-plasma factor XIII complex
-
additional information
-
binding modes of a new class of orally available thrombin inhibitors based on 4-aminopyrimidine. Two inhibitors based on 4-aminopyridine bind in different ways. One forms a water-mediated hydrogen bond to the active site Ser195, the other induces a rotation of the Ser214-Trp215 peptide plane that is unprecedent in thrombin structures
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
Na+
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+
additional information
-
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000178
thrombin-activatable fibrinolysis inhibitor
-
presence of thrombomodulin, Km(app) value
-
0.00033
D-Phe-Pro-Arg-4-nitroanilide
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
in the presence of 0.01 mM hirudin-(54-65)
0.0039
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
-
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
-
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
-
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
-
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
-
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
-
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
-
in the presence of 0.01 mM HD22
0.0143
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
-
in the presence of 0.01 mM HD1
0.0287
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
-
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
-
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
-
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
-
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
-
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