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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
-
-
-
?
activated protein C + H2O
?
-
-
-
-
?
Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Ala-Ala-Pro-Phe + 4-nitroaniline
-
synthetic chromogenic substrate
-
?
benzoyl-Arg ethyl ester + H2O
benzoyl-Arg + ethanol
-
-
-
-
?
benzoyl-Arg methyl ester + H2O
benzoyl-Arg + methanol
-
-
-
-
?
benzoyl-L-Arg-p-nitroanilide + H2O
benzoyl-L-Arg + p-nitroaniline
-
-
-
-
?
beta-Ala-Gly-Arg-4-nitroanilide + H2O
beta-Ala-Gly-Arg + 4-nitroaniline
-
-
-
-
?
chromozym TH + H2O
? + 4-nitroaniline
-
-
-
-
?
coagulation factor V + H2O
?
-
-
-
?
coagulation factor VIII + H2O
?
-
-
-
?
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide + H2O
D-Phe-L-pipecolyl-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-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
-
i.e. S-2238
-
-
?
D-Phe-Pro-Arg-4-nitroanilide + H2O
D-Phe-Pro-Arg + 4-nitroaniline
D-Phe-Pro-Lys-4-nitroanilide + H2O
D-Phe-Pro-Lys + 4-nitroaniline
D-Phe-Pro-Phe-4-nitroanilide + H2O
D-Phe-Pro-Phe + 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 V (1018) + H2O
?
-
cleavage site is LSPR
-
?
factor V (1545) + H2O
?
-
cleavage site is WYLR
-
?
factor V (709) + H2O
?
-
-
-
?
factor V + H2O
activated factor V + ?
-
activation
-
-
?
factor V + H2O
factor Va + propeptide
-
proteolytic activation
-
?
factor VII (1689) + H2O
?
-
clevage site is QSPR
-
?
factor VII (372) + H2O
?
-
cleavage site is IQIR
-
?
factor VII (740) + H2O
?
-
-
-
?
factor VIII + H2O
activated factor VIII + ?
-
activation
-
-
?
factor VIII + H2O
factor VIIIa + propeptide
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 X + H2O
factor Xa + propeptide
factor XI + H2O
?
-
-
-
?
factor XI + H2O
activated factor XI + ?
-
activation
-
-
?
factor XI + H2O
factor XIa + ?
-
activation by thrombin
-
-
?
factor XI + H2O
factor XIa + propeptide
-
proteolytic activation
-
?
factor XII + H2O
activated factor XII + ?
factor XIII + H2O
?
-
-
-
?
factor XIII + H2O
activated factor XIII + ?
factor XIII + H2O
factor XIIIa + propeptide
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
-
-
-
?
fibrinogen + H2O
fibrin + ?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
fibrinogen 1 + H2O
fibrin 1 + fibrinopeptide A + fibrinopeptide B
fibrinogen 2 + H2O
fibrin 2 + fibrinopeptide A + fibrinopeptide B
fibrinogen A a + H2O
?
-
-
-
?
fibrinogen Aalpha chain + H2O
?
-
-
-
-
?
Fibrinogen Aalpha-chain + H2O
?
-
-
-
?
fibrinogen B b + H2O
?
-
-
-
?
GLVPRGVNL + H2O
GLVPR + GVNL
-
residues 33-41 of factor XIII with mutation V34L
-
-
?
GVVPRGVNL + H2O
GVVPR + GVNL
-
residues 33-41 of factor XIII
-
-
?
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
-
-
?
Meizothrombin + H2O
?
-
cleavage of R155-S156 and R284-T285 bond
-
-
?
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
-
-
-
-
?
p-nitrophenyl-p'-(Nbeta,n-butyl-Nalpha-guanidino)benzoate + H2O
?
-
-
-
-
?
p-nitrophenyl-p'-(Nbeta,n-hexyl-Nalpha-guanidino)benzoate + H2O
?
-
-
-
-
?
p-nitrophenyl-p'-guanidinobenzoate + H2O
?
-
-
-
-
?
PAR1 peptide + H2O
?
protease-activated receptor I peptide fragment, amino acid sequence
-
?
PAR3 + H2O
?
-
protease-activated receptor 3
-
?
Pefachrom tPa + H2O
?
-
-
-
-
?
platelet thrombin receptor peptide + H2O
?
-
-
-
-
?
prethrombin + H2O
?
-
cleavage of R284-T285 bond
-
-
?
pro-factor XIII + H2O
factor XIII
-
activation by cleavage at Arg37 leading to blood coagulation
-
?
profactor V + H2O
factor V
-
human, activation, recombinant
-
?
profactor VIII + H2O
factor VIII
-
human, activation, recombinant
-
?
protease-activated receptor + H2O
?
-
activation
-
-
?
protease-activated receptor + H2O
activated protease-activated receptor + ?
-
activation
-
-
?
protease-activated receptor 1 + H2O
?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
-
activation
-
-
?
protease-activated receptor 3 residues 44-56 + H2O
?
-
-
-
?
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
?
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
?
protease-activated receptor-3 + H2O
?
-
activation
-
-
?
protease-activated receptor-4 + H2O
?
-
activation
-
-
?
protein C + H2O
activated protein C + ?
-
solvent isotope effect study
-
-
?
protein C zymogen + H2O
activated protein C + propeptide
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
-
-
?
protein kinase C + H2O
?
-
activation
-
-
?
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
-
-
?
prothrombin + H2O
?
-
cleavage of R155-S156 and R284-T285 bond
-
-
?
S-thanatin + H2O
?
-
-
-
-
?
spectrozyme TH + H2O
?
-
-
-
-
?
succinyl-AAPR-4-nitroanilide + H2O
succinyl-AAPR + 4-nitroaniline
-
-
-
-
?
thrombin-activable finrinolysis inhibitor + H2O
?
-
i.e. TAFI
-
?
thrombin-activatable fibrinolysis inhibitor + H2O
?
tosyl-Arg ethyl ester + H2O
tosyl-Arg + ethanol
-
-
-
-
?
Tosyl-Arg methyl ester + H2O
Tosyl-Arg + methanol
tosyl-Gly-L-Pro-L-Arg-4-nitroanilide + H2O
tosyl-Gly-L-Pro-L-Arg + 4-nitroaniline
-
-
-
-
?
tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
tosyl-Gly-Pro-Arg + 4-nitroaniline
transmembrane receptor PAR1 + H2O
?
-
-
-
?
TVELQGLVPRGVNL + H2O
TVELQGLVPR + GVNL
-
residues 28-41 of factor XIII with mutation V34L
-
-
?
TVELQGVVPRGVNL + H2O
TVELQGVVPR + GVNL
-
residues 28-41 of factor XIII
-
-
?
additional information
?
-
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
-
-
-
-
?
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
-
-
-
?
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
?
-
-
-
-
?
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
-
proteolytic activation
-
?
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 X + H2O
factor Xa + propeptide
-
-
-
-
?
factor X + H2O
factor Xa + propeptide
-
proteolytic activation
-
?
factor XII + H2O
activated factor XII + ?
-
-
-
-
?
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
-
-
?
factor XIII + H2O
factor XIIIa + propeptide
-
-
-
-
?
factor XIII + H2O
factor XIIIa + propeptide
-
proteolytic activation
-
?
Fibrinogen + H2O
?
-
cleavage of four Arg-Gly peptide bonds
-
-
?
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
?
-
-
-
-
?
Fibrinogen + H2O
?
-
Aalpha chain
-
-
?
Fibrinogen + H2O
?
-
key regulator of blood coagulation
-
-
?
Fibrinogen + H2O
?
-
clotting of fibrinogen
-
-
?
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 + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
the enzyme mediates the conversion of fibrinogen to fibrin
-
-
?
fibrinogen + H2O
fibrin + ?
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
-
thrombin is the key enzyme of coagulation
-
-
?
fibrinogen + H2O
fibrin + ?
-
activation, mechanism, overview
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
-
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
-
-
?
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, 717789, 732938 -
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
-
-
-
?
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
-
-
-
-
?
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
?
fibrinopeptide A + H2O
?
-
-
-
?
fibrinopeptide A + H2O
?
-
-
-
-
?
fibrinopeptide A + H2O
?
-
-
?
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
-
-
?
PAR1 + H2O
?
-
-
-
-
?
PAR1 + H2O
?
-
protease-activated receptor 1
-
?
PAR4 + H2O
?
-
-
-
-
?
PAR4 + H2O
?
-
protease-activated receptor 4
-
?
protease-activated receptor 1 + H2O
?
-
activation
-
-
?
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
?
-
activation
-
-
?
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
?
-
-
-
?
protein C + H2O
?
-
-
-
?
protein C + H2O
?
-
-
-
?
protein C + H2O
?
-
-
-
-
?
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
-
activation
-
-
?
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
-
-
-
-
?
protein C zymogen + H2O
activated protein C + propeptide
-
activation
-
-
?
protein C zymogen + H2O
activated protein C + propeptide
-
on vascular endothelial cells
-
-
?
S2238 + H2O
?
-
a chromogenic substrate
-
-
?
S2238 + H2O
?
-
fibrin-bound thrombin activity, measured by selective chromogenic substrate S2238
-
-
?
spectrozyme-TH + H2O
?
-
-
-
-
?
spectrozyme-TH + H2O
?
-
-
-
-
?
thrombin-activatable fibrinolysis inhibitor + H2O
?
-
i.e. TAFI
-
?
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-Arg methyl ester + H2O
Tosyl-Arg + methanol
-
-
-
-
?
Tosyl-Arg methyl ester + H2O
Tosyl-Arg + methanol
-
-
-
-
?
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
?
-
-
cleavage sites in macromolecular substrates
-
-
?
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
?
-
-
cleavage sites in macromolecular substrates
-
-
?
additional information
?
-
-
cleavage sites in macromolecular substrates
-
-
?
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
?
-
-
Ser195 is the catalytic residue
-
-
?
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
?
-
-
cleavage sites in macromolecular substrates
-
-
?
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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(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-(cyclohexylacetyl)-N-(thiophen-2-ylmethyl)pyrrolidine-2-carboxamide
-
-
(2S)-1-acetyl-N-(3-chlorobenzyl)pyrrolidine-2-carboxamide
-
-
(2S)-1-butanoyl-N-(3-chlorobenzyl)pyrrolidine-2-carboxamide
-
-
(2S)-1-[(2R)-2-amino-2-cyclohexylacetyl]-N-methylpyrrolidine-2-carboxamide
-
-
(2S)-1-[(2R)-2-amino-2-cyclohexylacetyl]-N-propylpyrrolidine-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-(3-chlorobenzyl)pyrrolidine-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
-
-
(2S)-1-[3-(4-chlorophenyl)propanoyl]-N-propylpyrrolidine-2-carboxamide
-
-
(2S)-3-(4-carbamimidoylphenyl)-2-[(naphthalen-2-ylsulfonyl)amino]propanoate
-
-
(2S)-N-(3-chlorobenzyl)-1-(3-methylbutanoyl)pyrrolidine-2-carboxamide
-
-
(2S)-N-(3-chlorobenzyl)-1-(3-phenylpropanoyl)pyrrolidine-2-carboxamide
-
-
(2S)-N-(3-chlorobenzyl)-1-(4-methylpentanoyl)pyrrolidine-2-carboxamide
-
-
(2S)-N-(3-chlorobenzyl)-1-(cyclopentylacetyl)pyrrolidine-2-carboxamide
-
-
(2S)-N-(3-chlorobenzyl)-1-propanoylpyrrolidine-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-(3,3-diphenyl-propionyl)-pyrrolidine-2-carboxylic acid methylamide
-
-
1-(3,3-diphenylpropanoyl)-N-(thiophen-2-ylmethyl)-L-prolinamide
-
-
1-(methylsulfonyl)-4-[N-(naphthalen-2-ylsulfonyl)glycyl-3-carbamimidoylphenylalanyl]piperazine
-
-
1-[(2R)-2-amino-2-cyclohexylacetyl]-N-(2-methoxyethyl)-L-prolinamide
-
-
1-[(2R)-2-amino-2-cyclohexylacetyl]-N-(cyclohexylmethyl)-L-prolinamide
-
-
1-[(2R)-2-amino-2-cyclohexylacetyl]-N-(thiophen-2-ylmethyl)-L-prolinamide
-
-
1-[(2R)-2-amino-4,4-diphenylbutanoyl]-N-(2-methoxyethyl)-L-prolinamide
-
-
1-[(2R)-2-amino-4,4-diphenylbutanoyl]-N-propyl-L-prolinamide
-
-
1-[(9-hydroxy-9H-fluoren-9-yl)acetyl]-N-(thiophen-2-ylmethyl)-L-prolinamide
-
-
1-[2-amino-3-(4-chloro-phenyl)-propionyl]-pyrrolidine-2-carboxylic acid methylamide
-
-
1-[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-(2-hydroxyphenyl)-1H-benzimidazole-5-carboximidamide
-
-
2-(2-oxo-1,2-dihydropyridin-3-yl)-1H-benzimidazole-6-carboximidamide
-
-
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
-
-
2-[2-(benzyloxy)phenyl]-2-[(3-carbamimidoylphenyl)amino]-N-hexylacetamide
-
-
3-(1,3-benzodioxol-5-yl)-D-alanyl-N-(2-methoxyethyl)-L-prolinamide
-
-
3-(3-ethoxy-3-oxopropyl)-6-methoxy-2-methyl-1-benzofuran-5-yl sulfate
-
-
3-(4-carbamimidoylphenyl)-2-oxopropanoic acid
-
-
3-(9-hydroxy-9H-fluoren-9-yl)-D-alanyl-N-(2-methoxyethyl)-L-prolinamide
-
-
3-(9-hydroxy-9H-fluoren-9-yl)-D-alanyl-N-methyl-L-prolinamide
-
-
3-(9-hydroxy-9H-fluoren-9-yl)-D-alanyl-N-propyl-L-prolinamide
-
-
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-(ethoxycarbonyl)-2-methyl-1-benzofuran-5,6-diyl disulfate
-
-
3-(ethoxycarbonyl)-5-methoxy-2-methyl-1-benzofuran-6-yl sulfate
-
-
3-(ethoxycarbonyl)-6-methoxy-2-methyl-1-benzofuran-5-yl sulfate
-
-
3-(hydroxymethyl)-6-methoxy-2-methyl-1-benzofuran-5-ol
-
-
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-cyclohexyl-D-alanyl-N-(2-methoxyethyl)-L-prolinamide
-
-
3-cyclohexyl-D-alanyl-N-propyl-L-prolinamide
-
-
3-[(2S)-3-(4-benzylpiperidin-1-yl)-2-[(naphthalen-2-ylsulfonyl)amino]-3-oxopropyl]benzenecarboximidamide
-
-
4-amidinophenylpyruvate
-
4-carbamimidoyl-N-[3-[(naphthalen-2-yloxy)sulfonyl]propanoyl]phenylalanyl-L-proline
-
-
4-chloro-D-phenylalanyl-N-(2-methoxyethyl)-L-prolinamide
-
-
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-nitrophenyl 2-propyl methylphosphonate
-
-
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
acetyl-(D)Phe-Pro-boroamidine-OH
-
-
acetyl-(D)Phe-Pro-boroArg-OH
-
-
acetyl-(D)Phe-Pro-borohomolysine-OH
-
-
acetyl-(D)Phe-Pro-boroLys-OH
-
-
acetyl-(D)Phe-Pro-boroOrn-OH
-
-
acetyl-L-Asp-L-Phe
-
biphasic inhibition
activated protein C
-
activated protein C has a regulatory function in inhibiting thrombin activation, overview
-
aeruginosin 298-A
-
isolated from Microcystis aeruginosa strain NIES-298
-
aeruginosin 98-B
-
isolated from Microcystis aeruginosa strain NIES-98
-
amentoflavone
-
slight inhibition
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 695699 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
Aspartame
-
L-Asp-L-Phe methyl ester, biphasic inhibition
AZD-0837
-
direct thrombin inhibitor, the prodrug AZD-0837 is bioactively converted into the direct thrombin inhibitor ARH-067637
Baicalin
-
slight inhibition
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
beta-phenyl-D-phenylalanyl-N-(2-methoxyethyl)-L-prolinamide
-
-
beta-phenyl-D-phenylalanyl-N-(3-chlorobenzyl)-L-prolinamide
-
-
beta-phenyl-D-phenylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
-
-
beta-phenyl-D-phenylalanyl-N-(thiophen-2-ylmethyl)-L-prolinamide
-
-
beta-phenyl-D-phenylalanyl-N-methyl-L-prolinamide
-
-
beta-phenyl-D-phenylalanyl-N-propyl-L-prolinamide
-
-
Bovine pancreatic trypsin inhibitor
-
-
butyl 4-carbamimidoyl-N-(naphthalen-2-ylsulfonyl)phenylalaninate
-
-
Cds03
-
CdsO3 binds to exosite II of thrombin to allosterically disrupt the catalytic apparatus resulting in inhibition
-
CH-248
-
i.e. (R)-cyclohexylalanyl-Pro-Arg[CH2OCH2CF3]
chondroitin 6-sulfate
-
low inhibitory potential in anticoagulation assay
CRC 220
-
binding mode to the enzyme, crystal structure
D-Phe-L-Pro-L-Arg-chloromethylketone
-
D-Phe-Pro-Arg
-
potent inhibitor
D-Phe-Pro-Arg-chloromethylketone
D-phenylalanyl-L-prolyl-L-arginyl-L-prolylglycine
-
complete inhibition at 20 mM
D-phenylalanyl-N-(3-chlorobenzyl)-L-prolinamide
-
-
D-phenylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
-
-
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
-
-
dihydromyricetin
-
slight inhibition
diisopropyl fluorophosphate
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
efegatran
-
small site-directed direct thrombin inhibitor
ellagic acid
-
competitive
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
epicatechin
-
slight inhibition
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 3-(5-hydroxy-6-methoxy-2-methyl-1-benzofuran-3-yl)propanoate
-
-
ethyl 5,6-dihydroxy-2-methyl-1-benzofuran-3-carboxylate
-
-
ethyl 5-hydroxy-6-methoxy-2-methyl-1-benzofuran-3-carboxylate
-
-
ethyl 6-hydroxy-5-methoxy-2-methyl-1-benzofuran-3-carboxylate
-
-
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 1
-
down-regulation of thrombin production
-
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
-
galangin
-
slight inhibition
glycerol
-
decreases cleavage rates with n-butyl derivatives
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 AD17
-
-
-
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
-
glycosaminoglycan AE11
-
modest inhibitory effect on thrombin activity
-
glycosaminoglycan AE15
-
-
-
glycosaminoglycan AE29
-
-
-
glycosaminoglycan AE6
-
modest inhibitory effect on thrombin activity
-
glycosaminoglycan CS-D
-
-
-
glycosaminoglycan CS-E
-
-
-
glycosaminoglycan DE17
-
-
-
glycosaminoglycan DE2
-
-
-
glycosaminoglycan DE9
-
-
-
GPRP
-
pseudo-complete inhibition, noncompetitive
GR157368
-
5-(2-oxo-hexahydro-cyclopenta[b]furna-3-yl)-pentanamide
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
H-D-Phe-Pro-Arg-chloromethylketone
-
irreversible thrombin inhibitor
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
-
HD22
-
aptamer, mitogen
-
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
-
hesperetin
-
slight inhibition
hesperidin
-
slight inhibition
hirudin(53-64) peptide
-
thrombin binding sequence is NGDFEEIPEEYL, competitive
-
hirugen
-
complete inhibition, noncompetitive
-
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
-
hyperin
-
slight inhibition
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
-
isohamnetin 3-O-nehesperridin
-
slight inhibition
isorhamnetin 3-O-(6-O-alpha-L-rhamnopyranosyl)-beta-D-glucopyranoside
-
slight inhibition
kaempferol 3-O-(2'',4''-di-(E)-p-coumaroyl)-rhamnoside
-
-
kaempferol 3-O-(2''-p-coumaroyl)-rhamnoside
-
-
kaempferol 3-O-(2-O-alpha-L-rhamnopyranosyl)-beta-D-glucopyranoside
-
slight inhibition
kaempferol 3-O-beta-D-glucoside
-
slight inhibition
L-Phe-L-Pro-L-Arg-chloromethylketone
-
-
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 3-carbamimidoyl-N-(naphthalen-2-ylsulfonyl)phenylalanyl-L-prolinate
-
-
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
Myricitrin
-
slight inhibition
N-(3-chlorobenzyl)-1-(3-cyclohexylpropanoyl)-L-prolinamide
-
-
N-(3-chlorobenzyl)-1-(3-cyclopentylpropanoyl)-L-prolinamide
-
-
N-(3-chlorobenzyl)-1-(cyclohexylacetyl)-L-prolinamide
-
-
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-[(4-carbamimidoylphenyl)sulfonyl]glycyl-3-carbamimidoyl-L-phenylalanine
-
-
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
-
-
Nalpha-dansyl-(p-guanidino)-L-phenylalanine piperidide
-
naphthalen-2-yl 3-[[(2S)-3-(4-carbamimidoylphenyl)-1-oxo-1-(piperazin-1-yl)propan-2-yl]amino]-3-oxopropane-1-sulfonate
-
-
naringenin
-
slight inhibition
naringin
-
slight inhibition
nexin-1
-
potent endogenous thrombin inhibitor
-
Phe-Pro-Arg-chloromethyl ketone
PMSF
2 mM, complete inhibition
propan-2-yl N-(naphthalen-2-ylsulfonyl)glycyl-3-carbamimidoyl-D-phenylalaninate
-
-
puerarin
-
slight inhibition
quercetin 3-O-rhamnose(1-2)glucose(6-1)rhamnose
-
slight inhibition
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
-
rutin
-
slight inhibition
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 inhibitor from Naja haje
-
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
-
Toggle-25 t
-
partial inhibition, noncompetitive
-
tosyl-Lys chloromethyl ketone
-
-
typhaneoside
-
slight inhibition
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
Y-27632
-
attenuates thrombin-mediated phosphorylation of p38MAPK and p65
[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
-
-
[6-methoxy-2-methyl-5-(sulfonatooxy)-1-benzofuran-3-yl]methyl sulfate
-
-
[amino(4-[[([(2S)-1-[(2R)-2-ammoniopropanoyl]pyrrolidin-2-yl]carbonyl)amino]methyl]phenyl)methylidene]ammonium dichloride
-
-
antithrombin
-
-
-
antithrombin
wild-type and mutant DELTAK9, the mutant shows 20fold lower susceptibility than the wild-type
-
antithrombin
-
enhances the inhibitory effect of thrombin inhibitors
-
antithrombin
-
inactive if complexed with heparin
-
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
-
antithrombin III
-
pseudo-complete inhibition, noncompetitive
-
antithrombin III
-
mutant enzymes E229A and E229K are not inhibited
-
AR-H067637
-
selective direct thrombin inhibitor, AZD0837 is bioconverted to its active form AR-H067637
AR-H067637
-
selective and reversible direct thrombin inhibitor
argatroban
-
small site-directed direct thrombin inhibitor
argatroban
-
direct thrombin inhibitor
argatroban
-
reversible thrombin inhibitor
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
-
competitive thrombin inhibitor
argatroban
-
complete inhibition, noncompetitive
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
-
oral direct thrombin inhibitor, prodrug of AR-H067637
AZD0837
-
AZD0837 is the prodrug of ARH06737, a potent, competitive, reversible inhibitor of free and fibrin-bound thrombin
benzamidine
-
bivalirudin
-
synthetic hirudin derivative
bivalirudin
-
reversible bivalent thrombin inhibitor
bivalirudin
-
complete inhibition, noncompetitive
Ca2+
-
slight inhibition at 10 mM
Ca2+
-
50% inhibition at 10 mM
D-Phe-Pro-Arg-chloromethylketone
-
-
D-Phe-Pro-Arg-chloromethylketone
-
D-Phe-Pro-Arg-chloromethylketone
-
-
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
-
thrombin is inhibited by 300 ng/ml
dabigatran etexilate
-
-
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
-
-
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 intestinal mucosa, about 16.5 kDa
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
-
inactive if complexed with antithrombin
heparin
-
blocks enzyme interaction with A2 subunit of substrate factor VIII
heparin
-
partial inhibition, noncompetitive
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
-
enhances the inhibitory effect of thrombin inhibitors
-
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
-
-
-
Hirudin
-
blocks exosite 1
-
Hirudin
-
irreversible, direct thrombin inhibitor, competitive to fibrin, noncompetitive to fibrin
-
Hirudin
-
blocks interaction of enzyme with A1 subunit of substrate factor VIII
-
Hirudin
-
specific inhibition
-
Hirudin
-
specific inhibitor
-
Hirudin
-
irreversible, bivalent thrombin inhibitor
-
Hirudin
-
hirudin-(54-65) (an analog of the COOH terminus of hirudin), inhibits the exosite 2-mediated interaction of thrombin with immobilized gamma'-peptide
-
Hirudin
-
tight-binding thrombin inhibitor
-
inogatran
-
i.e. carboxymethyl-(R)-cyclohexylalanyl-L-piperidine-2-carboxylic acid noragmatine
inogatran
-
binding mode to the enzyme, crystal structure
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
lepirudin
-
-
-
lepirudin
-
reversible bivalent thrombin inhibitor
-
lepirudin
-
a recombinant form of hirudin
-
melagatran
-
i.e. carboxymethyl-(R)-cyclohexylglycine-L-azetidine-2-carboxylic acid 4-amidinobenzylamine
melagatran
-
binding mode to the enzyme, crystal structure
melagatran
-
reversible, active site directed direct thrombin inhibitor, active form of ximelagatran
melagatran
-
direct thrombin inhibitor, inhibited by 0.001 mM
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
napsagatran
binding mode to the enzyme, crystal structure
napsagatran
-
binding mode to the enzyme, crystal structure
napsagatran ethyl ester
binding mode to the enzyme, crystal structure
napsagatran ethyl ester
-
binding mode to the enzyme, crystal structure
Phe-Pro-Arg-chloromethyl ketone
-
i.e. PPACK
Phe-Pro-Arg-chloromethyl ketone
-
complete inhibition, noncompetitive
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
-
ximelagatran
-
prodrug of melagatran
additional information
-
a series of natural flavonoids as thrombin inhibitors, structure-activity relationships, molecular docking, overview
-
additional information
no inhibition by EDTA
-
additional information
-
inhibitor binding mechanism and kinetics
-
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
-
no inhibition by cycloheximide
-
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
-
inhibition mechanism
-
additional information
-
schematic representation of inhibition mode
-
additional information
-
not inhibitory: acetyl-L-Ala-L-Phe methyl ester
-
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
-
not inhibited by soybean trypsin inhibitor
-
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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0.181
Ac-Gly-Gly-Val-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25°C
0.102
Ac-Leu-Gly-Val-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25°C
0.067
Ac-Nle-Thr-Leu-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25°C
0.011
Ac-Nle-Thr-Pro-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25°C
0.03
Ac-Val-Thr-Pro-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25°C
0.0052 - 0.0079
benzoyl-Arg ethyl ester
0.0075 - 0.0088
benzoyl-Arg methyl ester
0.143 - 0.84
benzoyl-L-Arg-p-nitroanilide
0.0015 - 0.0632
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
0.00033 - 0.013
D-Phe-Pro-Arg-4-nitroanilide
0.004 - 0.072
D-Phe-Pro-Lys-4-nitroanilide
0.017 - 0.11
D-Phe-Pro-Phe-4-nitroanilide
0.0026 - 0.298
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
0.1471 - 0.2829
di-L-Glu-L-Pro-L-Arg-4-nitroanilide
0.112
factor VIII(341-376) peptide
-
pH 7.5, 25°C
0.298
factor XIII
-
pH 7.4, 25°C, wild-type enzyme
-
0.315
factor XIII V34L mutant
-
pH 7.4, 25°C, wild-type enzyme
-
0.00001
Fc-[RFSRPQL]-PEG
-
-
0.00316 - 0.0528
fibrinogen
-
0.00355 - 0.0113
fibrinogen Aalpha chain
-
0.0051 - 0.013
Fibrinopeptide A
0.327
GLVPRGVNL
-
pH 7.4, 25°C
0.386
GVVPRGVNL
-
pH 7.4, 25°C
0.0084 - 0.028
PAR1 peptide
0.0355 - 0.181
platelet thrombin receptor peptide
-
0.002 - 0.0032
protein C
-
0.32
succinyl-AAPR-4-nitroanilide
-
-
0.000178
thrombin-activatable fibrinolysis inhibitor
-
presence of thrombomodulin, Km(app) value
-
0.0063 - 0.3
tosyl-Arg methyl ester
0.0085 - 0.0164
tosyl-Gly-Pro-Arg-4-nitroanilide
0.375
TVELQGLVPRGVNL
-
pH 7.4, 25°C
0.644
TVELQGVVPRGVNL
-
pH 7.4, 25°C
additional information
additional information
-
0.0052
benzoyl-Arg ethyl ester
-
0.15 M KCl
0.0056
benzoyl-Arg ethyl ester
-
0.15 M NaCl
0.0057
benzoyl-Arg ethyl ester
-
0.15 M CsCl
0.007
benzoyl-Arg ethyl ester
-
0.15 M NaNO3
0.0079
benzoyl-Arg ethyl ester
-
0.15 M CsNO3
0.0075
benzoyl-Arg methyl ester
-
0.15 M KCl
0.0088
benzoyl-Arg methyl ester
-
0.15 M NaCl
0.143
benzoyl-L-Arg-p-nitroanilide
-
alpha-thrombin
0.84
benzoyl-L-Arg-p-nitroanilide
-
beta-thrombin
0.0015
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
-
recombinant thrombin
0.0016
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
-
alpha thrombin
0.0021
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
-
alpha-thrombin
0.00232
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
-
beta-thrombin
0.00295
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
-
wild-type enzyme
0.0502
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
-
mutant enzyme E229A
0.0632
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
-
mutant enzyme E229K
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
0.0026
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
-
no additive
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)
0.1554
di-L-Glu-L-Pro-L-Arg-4-nitroanilide
-
in the presence of 0.01 mM HD22
0.195
di-L-Glu-L-Pro-L-Arg-4-nitroanilide
-
in the presence of 0.01 mM HD1
0.2829
di-L-Glu-L-Pro-L-Arg-4-nitroanilide
-
no additive
0.00316
fibrinogen
-
wild-type enzyme
-
0.0236
fibrinogen
-
mutant enzyme E229A
-
0.038
fibrinogen
-
mutant enzyme E229K
-
0.0528
fibrinogen
-
mutant enzyme E229W
-
0.00355
fibrinogen Aalpha chain
-
wild-type enzyme
-
0.0113
fibrinogen Aalpha chain
-
mutant enzyme E229A
-
0.0051
Fibrinopeptide A
pH 8.0, 25°C, wild-type enzyme
0.013
Fibrinopeptide A
pH 8.0, 25°C, mutant DELTAK9
0.0084
PAR1 peptide
pH 8.0, 25°C, wild-type enzyme
0.028
PAR1 peptide
pH 8.0, 25°C, mutant DELTAK9
0.0355
platelet thrombin receptor peptide
-
wild-type enzyme
-
0.181
platelet thrombin receptor peptide
-
mutant enzyme E229A
-
0.002
protein C
-
mutant enzyme E229A
-
0.00215
protein C
-
mutant enzyme E229K
-
0.00312
protein C
-
mutant enzyme E229W
-
0.00319
protein C
-
wild-type enzyme
-
0.0032
protein C
-
wild-type enzyme
-
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
0.0063
tosyl-Arg methyl ester
-
0.15 M NaCl
0.0072
tosyl-Arg methyl ester
-
0.15 M NaNO3
0.0122
tosyl-Arg methyl ester
-
0.15 M KCl
0.0133
tosyl-Arg methyl ester
-
0.15 M CsNO3
0.0137
tosyl-Arg methyl ester
-
0.15 M RbCl
0.0152
tosyl-Arg methyl ester
-
0.15 M CsCl
0.17
tosyl-Arg methyl ester
-
alpha-thrombin
0.3
tosyl-Arg methyl ester
-
beta-thrombin
0.0085
tosyl-Gly-Pro-Arg-4-nitroanilide
-
in the presence of 0.01 mM HD22
0.0117
tosyl-Gly-Pro-Arg-4-nitroanilide
-
in the presence of 0.01 mM hirudin-(54-65)
0.0142
tosyl-Gly-Pro-Arg-4-nitroanilide
-
in the presence of 0.01 mM HD1
0.0164
tosyl-Gly-Pro-Arg-4-nitroanilide
-
no additive
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
thermodynamic analysis of enzyme structure
-
additional information
additional information
thermodynamic analysis of enzyme structure
-
additional information
additional information
-
kinetics of mutant enzymes, overview
-
additional information
additional information
-
ratios of kcat/KM for substrates fibrinogen, PAR1, PAR4, protein C and RAP and comparison with human enzyme
-
additional information
additional information
-
ratios of kcat/KM for substrates fibrinogen, PAR1, PAR4, protein C and RAP and comparison with human enzyme
-
additional information
additional information
-
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
-
additional information
additional information
-
stopped flow kinetics of Na+ binding to thrombin, overview
-
additional information
additional information
-
ultra-rapid kinetics of Na+-binding to wild-type and mutant S195A thrombin
-
additional information
additional information
-
fibrinogen hydrolysis kinetics, kinetic model, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.2
Ac-Gly-Gly-Val-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25°C
15.6
Ac-Leu-Gly-Val-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25°C
5.8
Ac-Nle-Thr-Leu-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25°C
45
Ac-Nle-Thr-Pro-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25°C
30.8
Ac-Val-Thr-Pro-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25°C
13.7 - 17.8
benzoyl-Arg ethyl ester
14 - 15
benzoyl-Arg methyl ester
38 - 77.8
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
3.5 - 29
D-Phe-Pro-Arg-4-nitroanilide
0.018 - 12
D-Phe-Pro-Lys-4-nitroanilide
0.018 - 8.3
D-Phe-Pro-Phe-4-nitroanilide
0.11 - 209.4
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
217.1 - 278.6
di-L-Glu-L-Pro-L-Arg-4-nitroanilide
3 - 6
factor VIII(341-376) peptide
2.57
factor XIII
-
pH 7.4, 25°C, wild-type enzyme
-
22.9
factor XIII V34L mutant
-
pH 7.4, 25°C, wild-type enzyme
-
0.01
Fc-[RFSRPQL]-PEG
-
-
4.53 - 57
fibrinogen Aalpha chain
-
1.82 - 45.3
Fibrinopeptide A
24.3
GLVPRGVNL
-
pH 7.4, 25°C
5.8
GVVPRGVNL
-
pH 7.4, 25°C
0.00102
p-nitrophenyl-p'-(Nbeta,n-butyl-Nalpha-guanidino)benzoate
-
-
0.00197
p-nitrophenyl-p'-(Nbeta,n-hexyl-Nalpha-guanidino)benzoate
-
-
0.0018
p-nitrophenyl-p'-guanidinobenzoate
-
-
25 - 34
platelet thrombin receptor peptide
-
0.315
thrombin-activatable fibrinolysis inhibitor
-
presence of thrombomodulin, kcat(app) value
-
3.27 - 10.3
tosyl-Arg ethyl ester
192.8 - 251.6
tosyl-Gly-Pro-Arg-4-nitroanilide
15.2
TVELQGLVPRGVNL
-
pH 7.4, 25°C
6.2
TVELQGVVPRGVNL
-
pH 7.4, 25°C
additional information
additional information
-
analysis of temperature dependence of pseudo-first order rate constants for enzyme-catalyzed hydrolysis of prothrombin-derived substrates, in presence and absence of Ca2+
-
13.7
benzoyl-Arg ethyl ester
-
0.15 M NaNO3
14.1
benzoyl-Arg ethyl ester
-
0.15 M NaCl
15.2
benzoyl-Arg ethyl ester
-
0.15 M KCl
16.1
benzoyl-Arg ethyl ester
-
0.15 M CsCl
17.8
benzoyl-Arg ethyl ester
-
0.15 M CsNO3
14
benzoyl-Arg methyl ester
-
0.15 M NaCl
15
benzoyl-Arg methyl ester
-
0.15 M KCl
38
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
-
mutant enzyme E229A
51
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
-
wild-type enzyme
53.8
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
-
recombinant thrombin
56.5
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
-
beta-thrombin
63.3
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
-
alpha thrombin
77.8
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide
-
alpha-thrombin
3.5
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
6
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
7.5
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
29
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
0.018
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
0.26
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
2 - 8
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
12
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
0.018
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
0.23
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
1.4
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
8.3
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
0.11
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
0.32
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
15.8
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
21.2
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
41.2
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
46.6
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
47.9
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
55.5
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
75
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
-
wild type enzyme, in Tris-HCl (pH 7.5) with 0.2 M NaCl, at 22°C
84.4
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
101.9
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
-
no additive
106.8
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
-
in the presence of 0.01 mM HD22
156.5
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
-
in the presence of 0.01 mM hirudin-(54-65)
209.4
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
-
in the presence of 0.01 mM HD1
217.1
di-L-Glu-L-Pro-L-Arg-4-nitroanilide
-
in the presence of 0.01 mM HD1
231.1
di-L-Glu-L-Pro-L-Arg-4-nitroanilide
-
in the presence of 0.01 mM HD22
249.5
di-L-Glu-L-Pro-L-Arg-4-nitroanilide
-
no additive
278.6
di-L-Glu-L-Pro-L-Arg-4-nitroanilide
-
in the presence of 0.01 mM hirudin-(54-65)
3 - 6
factor VIII(341-376) peptide
-
pH 7.5, 25°C
3.24
factor VIII(341-376) peptide
-
pH 7.5, 25°C
2.53
fibrinogen
-
mutant enzyme E229K
-
3.12
fibrinogen
-
mutant enzyme E229W
-
5.9
fibrinogen
-
wild-type enzyme
-
7.88
fibrinogen
-
mutant enzyme E229A
-
4.53
fibrinogen Aalpha chain
-
mutant enzyme E229A
-
57
fibrinogen Aalpha chain
-
wild-type enzyme
-
1.82
Fibrinopeptide A
pH 8.0, 25°C, mutant DELTAK9
2.94
Fibrinopeptide A
pH 8.0, 25°C, mutant DELTAK9
45.3
Fibrinopeptide A
pH 8.0, 25°C, wild-type enzyme
4.2
PAR1 peptide
pH 8.0, 25°C, mutant DELTAK9
146
PAR1 peptide
pH 8.0, 25°C, wild-type enzyme
25
platelet thrombin receptor peptide
-
mutant enzyme E229A
-
34
platelet thrombin receptor peptide
-
wild-type enzyme
-
0.065
protein C
-
wild-type enzyme
-
0.148
protein C
-
mutant enzyme E229W
-
0.19
protein C
-
mutant enzyme E229A
-
0.21
protein C
-
mutant enzyme E229K
-
0.65
protein C
-
wild-type enzyme
-
15
spectrozyme-TH
-
pH 8.0, 25°C, absence of Na+
21
spectrozyme-TH
-
mutant K222D, pH 8.0, 25°C, absence of Na+
32
spectrozyme-TH
-
wild-type, pH 8.0, 25°C, absence of Na+
32
spectrozyme-TH
-
wild-type, pH 8.0, 25°C, presence of 0.2 M Na+
80
spectrozyme-TH
-
mutant K222D, pH 8.0, 25°C, presence of 0.2 M Na+
91
spectrozyme-TH
-
pH 8.0, 25°C, presence of 0.2 M Na+
3.27
tosyl-Arg ethyl ester
-
0.15 M NaCl
3.78
tosyl-Arg ethyl ester
-
0.15 M NaNO3
9.33
tosyl-Arg ethyl ester
-
0.15 M RbCl
9.4
tosyl-Arg ethyl ester
-
0.15 M KCl
10
tosyl-Arg ethyl ester
-
0.15 M CsNO3
10.3
tosyl-Arg ethyl ester
-
0.15 M CsCl
192.8
tosyl-Gly-Pro-Arg-4-nitroanilide
-
in the presence of 0.01 mM HD22
234.5
tosyl-Gly-Pro-Arg-4-nitroanilide
-
no additive
240.3
tosyl-Gly-Pro-Arg-4-nitroanilide
-
in the presence of 0.01 mM HD1
251.6
tosyl-Gly-Pro-Arg-4-nitroanilide
-
in the presence of 0.01 mM hirudin-(54-65)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00015
(1R)-2-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-cyclohexyl-2-oxoethanaminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00043
(1R)-2-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-cyclopentyl-2-oxoethanaminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00018
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-oxo-3-phenylpropan-2-aminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00681
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-oxobutan-2-aminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.033
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-oxopropan-2-aminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00092
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-3,3-dimethyl-1-oxobutan-2-aminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.0001
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-3-cyclohexyl-1-oxopropan-2-aminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00254
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-aminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00041
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-4,4-dimethyl-1-oxopentan-2-aminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00054
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-4-methyl-1-oxopentan-2-aminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
1.46
(2S)-1-acetyl-N-(3-chlorobenzyl)pyrrolidine-2-carboxamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.322
(2S)-1-butanoyl-N-(3-chlorobenzyl)pyrrolidine-2-carboxamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.0068
(2S)-1-[(2R)-2-aminobutanoyl]-N-(3-chlorobenzyl)pyrrolidine-2-carboxamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% dimethyl sulfoxide, 0.1% (w/v) PEG 8000, at 25 °C
0.00018
(2S)-1-[(2R)-2-aminobutanoyl]-N-(4-carbamimidoylbenzyl)pyrrolidine-2-carboxamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% dimethyl sulfoxide, 0.1% (w/v) PEG 8000, at 25 °C
0.155 - 0.484
(2S)-N-(3-chlorobenzyl)-1-(3-methylbutanoyl)pyrrolidine-2-carboxamide
0.0943
(2S)-N-(3-chlorobenzyl)-1-(3-phenylpropanoyl)pyrrolidine-2-carboxamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.109
(2S)-N-(3-chlorobenzyl)-1-(4-methylpentanoyl)pyrrolidine-2-carboxamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.0724
(2S)-N-(3-chlorobenzyl)-1-(cyclopentylacetyl)pyrrolidine-2-carboxamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.444
(2S)-N-(3-chlorobenzyl)-1-propanoylpyrrolidine-2-carboxamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00175
(E)-2-(3-aminophenyl)-N-(3-[[1-(1-benzothiophen-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)ethenesulfonamide
-
pH and temperature not specified in the publication
0.0392
(E)-2-(3-chlorophenyl)-N-(3-[[1-(pyridin-3-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)ethenesulfonamide
-
pH and temperature not specified in the publication
0.0625
(E)-2-(3-nitrophenyl)-N-(3-[[1-(pyridin-3-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)ethenesulfonamide
-
pH and temperature not specified in the publication
0.00543
(E)-N-(3-[[1-(1,3-benzothiazol-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-(3-chlorophenyl)ethenesulfonamide
-
pH and temperature not specified in the publication
0.0046
(E)-N-(3-[[1-(1,3-benzothiazol-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-(3-nitrophenyl)ethenesulfonamide
-
pH and temperature not specified in the publication
0.00088
(E)-N-(3-[[1-(1-benzothiophen-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-(3-chlorophenyl)ethenesulfonamide
-
pH and temperature not specified in the publication
0.00227
(E)-N-(3-[[1-(1-benzothiophen-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-(3-fluorophenyl)ethenesulfonamide
-
pH and temperature not specified in the publication
0.00171
(E)-N-(3-[[1-(1-benzothiophen-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-(3-nitrophenyl)ethenesulfonamide
-
pH and temperature not specified in the publication
0.00197
(E)-N-(3-[[1-(1-benzothiophen-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-[3-(trifluoromethyl)phenyl]ethenesulfonamide
-
pH and temperature not specified in the publication
0.00689
(E)-N-(3-[[1-(1H-indol-2-ylmethyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-(3-nitrophenyl)ethenesulfonamide
-
pH and temperature not specified in the publication
0.0137
(E)-N-(3-[[1-(3-chlorobenzyl)-1H-1,2,3-triazol-4-yl]methoxy]phenyl)-2-(3-chlorophenyl)ethenesulfonamide
-
pH and temperature not specified in the publication
0.00891
(E)-N-[3-[(1-benzyl-1H-1,2,3-triazol-4-yl)methoxy]phenyl]-2-(3-chlorophenyl)ethenesulfonamide
-
pH and temperature not specified in the publication
0.0052
(E)-N-[3-[2-(3-chlorobenzyl)-2H-tetrazol-5-yl]phenyl]-2-(3-methylphenyl)ethenesulfonamide
-
pH and temperature not specified in the publication
0.000037
1-[N-[2-(amidino-N'-methylaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(2-[4-methylphenyl]ethylamino)pyrazinone
-
-
0.0000017
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-chloro-3-[2,2-difluoro-2-phenylethylamino]pyrazinone
-
-
0.0000023
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-cyano-3-[2,2-difluoro-2-phenylethylamino]pyrazinone
-
-
0.0000068
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(2,2-diphenylethylamino)pyrazinone
-
-
0.000015
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(2-[2,4-difluorophenyl]ethylamino)pyrazinone
-
-
0.000047
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(2-[3,4-difluorophenyl]ethylamino)pyrazinone
-
-
0.000047
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(2-[4-trifluoromethylphenyl]ethylamino)pyrazinone
-
-
0.000044
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(2-[5-indanyl]ethylamino)pyrazinone
-
-
0.00012
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(3,4-dimethoxyphenylethylamino)pyrazinone
-
-
0.000066
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(4-ethylphenethylamino)pyrazinone
-
-
0.000013
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(4-fluorophenethylamino)pyrazinone
-
-
0.000011
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-(4-methoxyphenethylamino)pyrazinone
-
-
0.0000013
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-[2,2-difluoro-2-phenylethylamino]pyrazinone
-
-
0.000012
1-[N-[2-(amidinoaminooxy)ethyl]amino]carbonylmethyl-6-methyl-3-[2-(1-naphthalene)ethyl]aminopyrazinone
-
-
0.00808
2-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-2-oxoethanaminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.0000026
3-(benzyl(2-(4-carbamimidoylbenzyl)-4-methyl-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-7-yl)amino)-3-oxopropanoic acid
-
-
0.0000065
3-(benzyl(2-(4-carbamimidoylbenzyl)-4-methyl-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-7-yl)amino)-4-oxobutanoic acid
-
-
0.00062
4-amidinophenylpyruvate
-
0.1
4-nitrophenyl 2-propyl methylphosphonate
-
IC50 above 0.1 mM, at pH 7.0 in 0.05 M phosphate buffer and 0.15 M NaCl at 25°C
0.00094
amino[4-([[1-(3,3-dimethylbutanoyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00117
amino[4-([[1-(3-cyclohexylpropanoyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00118
amino[4-([[1-(3-cyclopentylpropanoyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00381
amino[4-([[1-(3-methylbutanoyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00075
amino[4-([[1-(3-phenylpropanoyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00128
amino[4-([[1-(4-methylpentanoyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00361
amino[4-([[1-(cyclohexylacetyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00164
amino[4-([[1-(cyclopentylacetyl)-L-prolyl]amino]methyl)phenyl]methaniminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.0057
amino[4-[([[(2S)-1-butanoylpyrrolidin-2-yl]carbonyl]amino)methyl]phenyl]methaniminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.039
amino[4-[([[(2S)-1-propanoylpyrrolidin-2-yl]carbonyl]amino)methyl]phenyl]methaniminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.0000014
antithrombin III
-
pH 7.4, 37°C
-
0.0000064
argatroban
-
pH 7.4, 37°C
98
Aspartame
-
pH 7.4, 37°C
0.000047
beta-phenyl-D-phenylalanyl-N-(3-chlorobenzyl)-L-prolinamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% dimethyl sulfoxide, 0.1% (w/v) PEG 8000, at 25 °C
0.0000001
beta-phenyl-D-phenylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% dimethyl sulfoxide, 0.1% (w/v) PEG 8000, at 25 °C
0.00000175
bivalirudin
-
pH 7.4, 37°C
0.000003
CH-248
-
pH 7.4, 25°C
0.00018
D-phenylalanyl-N-(3-chlorobenzyl)-L-prolinamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% dimethyl sulfoxide, 0.1% (w/v) PEG 8000, at 25 °C
0.000004
D-phenylalanyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% dimethyl sulfoxide, 0.1% (w/v) PEG 8000, at 25 °C
0.0000000000493
dipetalogastin II
-
pH 8.0, 37°C
-
0.000000000446
dipetarudin
-
pH 8.0, 37°C
-
0.0000022
DV23
-
pH and temperature not specified in the publication, after no preincubation time
0.0000006
DV23K10R
-
pH and temperature not specified in the publication, after no preincubation time
0.00000031
DV24
-
pH and temperature not specified in the publication, after no preincubation time
0.0000032
DV24H12A
-
pH and temperature not specified in the publication, after no preincubation time
0.00000004 - 0.00000026
DV24K10RY
0.00000033
DV24Yphos
-
pH and temperature not specified in the publication, after no preincubation time
0.00000006
DV24Ysulf
-
pH and temperature not specified in the publication, after no preincubation time
0.00000032
EP21
-
pH and temperature not specified in the publication, after no preincubation time
0.00000037
EP25
-
pH and temperature not specified in the publication, after no preincubation time
0.00000031
EP25A22E
-
pH and temperature not specified in the publication, after no preincubation time
0.0000036
ethyl 2-(benzyl(2-(4-carbamimidoylbenzyl)-4-methyl-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-7-yl)amino)-2-oxoacetate
-
-
0.0088
glycoprotein Ibalpha(1-282) peptide
-
pH 8.0, 25°C
-
0.054
glycoprotein Ibalpha(268-282) peptide
-
pH 8.0, 25°C
-
0.027
GPRP
-
pH 7.4, 37°C
0.000025
HD22
-
pH 8.0, 25°C
-
0.00265
heparin
-
pH 7.4, 37°C
0.000000000237
Hirudin
-
pH 8.0, 37°C
-
0.0015
hirugen
-
pH 7.4, 37°C
-
0.0000023
hirulog-1
-
pH and temperature not specified in the publication, after no preincubation time
0.000000000125
inhibitor from Dipetalogaster maximus
-
pH 8.0, 25°C
-
0.0000043
inogatran
-
pH 7.4, 25°C
0.000024
L-Phe-L-Pro-L-Arg-chloromethylketone
-
at pH 7.0 in 0.05 M phosphate buffer and 0.15 M NaCl at 25°C
0.0000013
melagatran
-
pH 7.4, 25°C
0.0000149
MH18
-
pH and temperature not specified in the publication, after no preincubation time
0.000329
MH18H12A
-
pH and temperature not specified in the publication, after no preincubation time
0.00000125
MH18Ysulf
-
pH and temperature not specified in the publication, after no preincubation time
0.0000141
MH22
-
pH and temperature not specified in the publication, after no preincubation time
0.0000151
MH22A22E
-
pH and temperature not specified in the publication, after no preincubation time
0.0297
N-(3-chlorobenzyl)-1-(3-cyclohexylpropanoyl)-L-prolinamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.0929
N-(3-chlorobenzyl)-1-(3-cyclopentylpropanoyl)-L-prolinamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.0345
N-(3-chlorobenzyl)-1-(cyclohexylacetyl)-L-prolinamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00000066 - 0.0000021
N-alpha-(2-naphthylsulfonyl-glycyl)-4-amidinophenylalanine-piperidine
0.000023
N-[4-[amino(iminio)methyl]benzyl]-1-[(2R)-2-ammonio-2-cyclohexylacetyl]-L-prolinamide dichloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00015
N-[4-[amino(iminio)methyl]benzyl]-1-[(2R)-2-ammonio-3,3-dimethylbutanoyl]-L-prolinamide dichloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00007
N-[4-[amino(iminio)methyl]benzyl]-1-[(2R)-2-ammonio-3-methylbutanoyl]-L-prolinamide dichloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.000004
N-[4-[amino(iminio)methyl]benzyl]-1-[(2R)-2-ammonio-3-phenylpropanoyl]-L-prolinamide dichloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.000011
N-[4-[amino(iminio)methyl]benzyl]-1-[(2R)-2-ammonio-4,4-dimethylpentanoyl]-L-prolinamide dichloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00002
N-[4-[amino(iminio)methyl]benzyl]-1-[(2R)-2-ammonio-4-methylpentanoyl]-L-prolinamide dichloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00018
N-[4-[amino(iminio)methyl]benzyl]-1-[(2R)-2-ammoniobutanoyl]-L-prolinamide dichloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.1
paraoxon
-
IC50 above 0.1 mM, at pH 7.0 in 0.05 M phosphate buffer and 0.15 M NaCl at 25°C
0.0000208
Phe-Pro-Arg-chloromethyl ketone
-
pH 7.4, 37°C
0.00000000000014
RWJ-50353
-
-
0.0000000000011
RWJ-51438
-
-
0.0000728
thrombin inhibitor from Naja haje
-
in 10 mM imidazole buffer (pH 7.4), at 37°C
-
0.00001
Toggle-25 t
-
pH 7.4, 37°C
-
0.00000032
variegin
-
synthetic molecule, pH and temperature not specified in the publication, after no preincubation time
0.0561
[4-[([[(2S)-1-acetylpyrrolidin-2-yl]carbonyl]amino)methyl]phenyl](amino)methaniminium chloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00142
[amino(4-[[([(2S)-1-[(2R)-2-ammoniopropanoyl]pyrrolidin-2-yl]carbonyl)amino]methyl]phenyl)methylidene]ammonium dichloride
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
additional information
additional information
-
0.155
(2S)-N-(3-chlorobenzyl)-1-(3-methylbutanoyl)pyrrolidine-2-carboxamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.484
(2S)-N-(3-chlorobenzyl)-1-(3-methylbutanoyl)pyrrolidine-2-carboxamide
-
in 50 mM Tris-HCl, pH 7.4, 154 mM NaCl, 5% (v/v) DMSO, 0.1% (w/v) PEG 8000, at 25°C
0.00000004
DV24K10RY
-
pH and temperature not specified in the publication, after no preincubation time
0.00000015
DV24K10RY
-
pH and temperature not specified in the publication, after no preincubation time
0.00000026
DV24K10RY
-
pH and temperature not specified in the publication, after no preincubation time
0.00000066
N-alpha-(2-naphthylsulfonyl-glycyl)-4-amidinophenylalanine-piperidine
pH 8.0, 25°C, mutant DELTAK9
0.0000021
N-alpha-(2-naphthylsulfonyl-glycyl)-4-amidinophenylalanine-piperidine
pH 8.0, 25°C, wild-type enzyme
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
inhibition kinetics
-
additional information
additional information
-
inhibition kinetics
-
additional information
additional information
inhibition kinetics for napsagatran and napsagatran ethyl ester in presence of NaCl or KCl and at 4 different temperatures
-
additional information
additional information
-
kinetics at 25°C and 37°C, thermodynamic analysis of inhibitor binding and interaction
-
additional information
additional information
-
inhibition kinetics, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.4
(2S)-1-(1,3-benzodioxol-5-ylacetyl)-N-(thiophen-2-ylmethyl)pyrrolidine-2-carboxamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.4
(2S)-1-(cyclohexylacetyl)-N-(thiophen-2-ylmethyl)pyrrolidine-2-carboxamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.4
(2S)-1-[(2R)-2-amino-2-cyclohexylacetyl]-N-methylpyrrolidine-2-carboxamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.12
(2S)-1-[(2R)-2-amino-2-cyclohexylacetyl]-N-propylpyrrolidine-2-carboxamide
Homo sapiens
-
at 37°C
0.4
(2S)-1-[(2R)-2-amino-3-(1,3-benzodioxol-5-yl)propanoyl]-N-methylpyrrolidine-2-carboxamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.4
(2S)-1-[(2R)-2-amino-3-(1,3-benzodioxol-5-yl)propanoyl]-N-propylpyrrolidine-2-carboxamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.013
(2S)-1-[(2R)-2-amino-3-(4-chlorophenyl)propanoyl]-N-(thiophen-2-ylmethyl)pyrrolidine-2-carboxamide
Homo sapiens
-
at 37°C
0.21
(2S)-1-[(2R)-2-amino-3-(4-chlorophenyl)propanoyl]-N-propylpyrrolidine-2-carboxamide
Homo sapiens
-
at 37°C
0.4
(2S)-1-[(2R)-2-amino-3-cyclohexylpropanoyl]-N-methylpyrrolidine-2-carboxamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.4
(2S)-1-[(2R)-2-cyclohexyl-2-hydroxyacetyl]-N-(2-methoxyethyl)pyrrolidine-2-carboxamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.4
(2S)-1-[3-(4-chlorophenyl)propanoyl]-N-(2-methoxyethyl)pyrrolidine-2-carboxamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.4
(2S)-1-[3-(4-chlorophenyl)propanoyl]-N-(thiophen-2-ylmethyl)pyrrolidine-2-carboxamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.4
(2S)-1-[3-(4-chlorophenyl)propanoyl]-N-propylpyrrolidine-2-carboxamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.23
1-(2-amino-2-cyclohexyl-acetyl)-pyrrolidine-2-carboxylic acid isobutyl-amide
Homo sapiens
-
at 37°C
0.17
1-(2-cyclohexyl-2-phenylmethanesulfonylamino-acetyl)-pyrrolidine-2-carboxylic acid methylamide
Homo sapiens
-
at 37°C
0.12
1-(3,3-diphenylpropanoyl)-N-(thiophen-2-ylmethyl)-L-prolinamide
Homo sapiens
-
at 37°C
0.4
1-[(2R)-2-amino-2-cyclohexylacetyl]-N-(2-methoxyethyl)-L-prolinamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.02
1-[(2R)-2-amino-2-cyclohexylacetyl]-N-(cyclohexylmethyl)-L-prolinamide
Homo sapiens
-
at 37°C
0.0042
1-[(2R)-2-amino-2-cyclohexylacetyl]-N-(thiophen-2-ylmethyl)-L-prolinamide
Homo sapiens
-
at 37°C
0.4
1-[(2R)-2-amino-4,4-diphenylbutanoyl]-N-(2-methoxyethyl)-L-prolinamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.4
1-[(2R)-2-amino-4,4-diphenylbutanoyl]-N-propyl-L-prolinamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.049
1-[(9-hydroxy-9H-fluoren-9-yl)acetyl]-N-(thiophen-2-ylmethyl)-L-prolinamide
Homo sapiens
-
at 37°C
0.4
3-(1,3-benzodioxol-5-yl)-D-alanyl-N-(2-methoxyethyl)-L-prolinamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.4
3-(9-hydroxy-9H-fluoren-9-yl)-D-alanyl-N-(2-methoxyethyl)-L-prolinamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.4
3-(9-hydroxy-9H-fluoren-9-yl)-D-alanyl-N-methyl-L-prolinamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.38
3-(9-hydroxy-9H-fluoren-9-yl)-D-alanyl-N-propyl-L-prolinamide
Homo sapiens
-
at 37°C
0.4
3-cyclohexyl-D-alanyl-N-(2-methoxyethyl)-L-prolinamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.4
3-cyclohexyl-D-alanyl-N-propyl-L-prolinamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.4
4-chloro-D-phenylalanyl-N-(2-methoxyethyl)-L-prolinamide
Homo sapiens
-
IC50 above 0.4 mM, at 37°C
0.14
acacetin
Bos taurus
-
pH and temperature not specified in the publication
0.18
apigenin
Bos taurus
-
pH and temperature not specified in the publication
0.06
baicalein
Bos taurus
-
pH and temperature not specified in the publication
0.089
beta-phenyl-D-phenylalanyl-N-(2-methoxyethyl)-L-prolinamide
Homo sapiens
-
at 37°C
0.0016
beta-phenyl-D-phenylalanyl-N-(thiophen-2-ylmethyl)-L-prolinamide
Homo sapiens
-
at 37°C
0.23
beta-phenyl-D-phenylalanyl-N-methyl-L-prolinamide
Homo sapiens
-
at 37°C
0.018
beta-phenyl-D-phenylalanyl-N-propyl-L-prolinamide
Homo sapiens
-
at 37°C
0.0000454 - 0.0000778
DV23
0.0000129 - 0.000102
DV23K10R
0.0000075 - 0.0000101
DV24
0.0000482 - 0.000141
DV24H12A
0.0000014 - 0.0000078
DV24K10RY
0.000007 - 0.000012
DV24K10RYphos
0.0000087 - 0.0000124
DV24Yphos
0.0000017 - 0.000002
DV24Ysulf
0.0000162 - 0.000177
EP21
0.0000131 - 0.000173
EP25
0.0000135 - 0.000124
EP25A22E
0.0007
glycosaminoglycan AD17
Bos taurus
-
-
-
0.00429
glycosaminoglycan AD4, glycosaminoglycan AD9, glycosaminoglycan AE11
Bos taurus
-
IC50 above 0.00429 mM
-
0.0025
glycosaminoglycan AE15
Bos taurus
-
-
-
0.00092
glycosaminoglycan AE29
Bos taurus
-
-
-
0.00429
glycosaminoglycan AE6
Bos taurus
-
IC50 above 0.00429 mM
-
0.00095
glycosaminoglycan CS-D
Bos taurus
-
-
-
0.0001
glycosaminoglycan CS-E
Bos taurus
-
-
-
0.00015
glycosaminoglycan DE17
Bos taurus
-
-
-
0.00055
glycosaminoglycan DE2
Bos taurus
-
-
-
0.00025
glycosaminoglycan DE9
Bos taurus
-
-
-
0.071
hinokiflavone
Bos taurus
-
pH and temperature not specified in the publication
0.0000726 - 0.000102
hirulog-1
0.246
isorhamnetin
Bos taurus
-
pH and temperature not specified in the publication
0.109
kaempferol
Bos taurus
-
pH and temperature not specified in the publication
0.052
kaempferol 3-O-(2'',4''-di-(E)-p-coumaroyl)-rhamnoside
Bos taurus
-
pH and temperature not specified in the publication
0.083
kaempferol 3-O-(2''-p-coumaroyl)-rhamnoside
Bos taurus
-
pH and temperature not specified in the publication
0.052
luteolin
Bos taurus
-
pH and temperature not specified in the publication
0.0000109 - 0.0000117
MH18
0.000328 - 0.000343
MH18H12A
0.0000012 - 0.0000013
MH18Ysulf
0.0000115 - 0.0000123
MH22
0.0000136 - 0.0000156
MH22A22E
0.006
myricetin
Bos taurus
-
pH and temperature not specified in the publication
0.307
N-(4-carbamimidoylbenzyl)-2-(1-[[(4-chloro-2-methoxyphenyl)sulfonyl]amino]-4-methyl-2-oxo-1,2-dihydropyridin-3-yl)acetamide
Homo sapiens
-
-
0.092
N-(4-carbamimidoylbenzyl)-2-(1-[[2-(2,5-dimethylphenyl)ethyl]amino]-4-methyl-2-oxo-1,2-dihydropyridin-3-yl)acetamide
Homo sapiens
-
-
0.023
N-(4-carbamimidoylbenzyl)-2-(4-methyl-1-[[2-(2-methylphenyl)ethyl]amino]-2-oxo-1,2-dihydropyridin-3-yl)acetamide
Homo sapiens
-
-
0.091
N-(4-carbamimidoylbenzyl)-2-[4-methyl-2-oxo-1-[(2-phenylethyl)amino]-1,2-dihydropyridin-3-yl]acetamide
Homo sapiens
-
-
0.035
quercetin
Bos taurus
-
pH and temperature not specified in the publication
0.0000002
thrombin inhibitor from Naja haje
Bos taurus
-
in 10 mM imidazole buffer (pH 7.4), at 37°C
-
0.00000825 - 0.0000104
variegin
0.0000454
DV23
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.0000778
DV23
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.0000129
DV23K10R
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.000102
DV23K10R
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.0000075
DV24
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.0000101
DV24
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.0000482
DV24H12A
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.000141
DV24H12A
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.0000014
DV24K10RY
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.0000017
DV24K10RY
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.0000046
DV24K10RY
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.0000078
DV24K10RY
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.000007
DV24K10RYphos
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.000012
DV24K10RYphos
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.0000087
DV24Yphos
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.0000124
DV24Yphos
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.0000017
DV24Ysulf
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.000002
DV24Ysulf
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.0000162
EP21
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.000177
EP21
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.0000131
EP25
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.000173
EP25
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.0000135
EP25A22E
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.000124
EP25A22E
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.0000726
hirulog-1
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.000102
hirulog-1
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.0000109
MH18
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.0000117
MH18
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.000328
MH18H12A
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.000343
MH18H12A
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.0000012
MH18Ysulf
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.0000013
MH18Ysulf
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.0000115
MH22
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.0000123
MH22
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.0000136
MH22A22E
Homo sapiens
-
pH and temperature not specified in the publication, after no preincubation time
0.0000156
MH22A22E
Homo sapiens
-
pH and temperature not specified in the publication, after 20 min preincubation
0.00000825
variegin
Homo sapiens
-
synthetic molecule, pH and temperature not specified in the publication, after no preincubation time
0.0000104
variegin
Homo sapiens
-
synthetic molecule, pH and temperature not specified in the publication, after 20 min preincubation
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malfunction
-
in the transgenic TRAMP mouse model of prostate cancer inhibition of endogenous thrombin by hirudin retards spontaneous tumor growth. Inhibition of thrombin may lead to tumor dormancy
malfunction
-
high glucose enhances smooth muscle cell responsiveness to thrombin through transcriptional upregulation of PAR-4, which may play an important role in the vascular complications of diabetes
metabolism
-
PAR-1 signaling to NF-kappaB in endothelial cells via protein kinase C signaling, CARMA3/Bcl10/MALT1, CBM, signalosome, and IkappaB kinase, and involving thrombin, pathway regulation, overview. The CBM signalosome controls thrombin-dependent monocyte/endothelial adhesion. The process is different in lymphocytes where CARMA1 is active instead of CARMA3
metabolism
-
thrombin induces NF-kappaB activation and IL-8/CXCL8 expression in human lung epithelial cells by a Rac1-dependent PI3K/Akt pathway. Treatment of cells with thrombin causes activation of Rac and Akt. Thrombin induces NF-kappaB activation and protein expression through multiple signaling pathways such as PKCalpha/c-Src, Rac1, extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, c-Jun N-terminal kinase, IkappaB kinases, and PI3K/Akt, overview
metabolism
-
thrombin induces NF-kappaB activation and IL-8/CXCL8 expression in lung epithelial cells by a Rac1-dependent PI3K/Akt pathway. Treatment of cells with thrombin causes activation of Rac and Akt. Thrombin induces NF-kappaB activation and protein expression through multiple signaling pathways such as PKCalpha/c-Src, Rac1, extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, c-Jun N-terminal kinase, IkappaB kinases, and PI3K/Akt, overview
physiological function
-
after treating JR-FL Env-expressing 293T cells with various concentrations of thrombin and subsequent coculture for 14 h, thrombin effect turns out to be a concentration-dependent fusion enhancement, thrombin can enhance the fusion mediated by R5-tropic HIV-1 gp160
physiological function
-
HUVEC cells stimulated with thrombin (10 nM) exhibit an increased amount of actin filaments (show increased cell stiffness) when compared to unstimulated cells
physiological function
-
in thrombin- and collagen-stimulated platelets, protein kinase A is activated by cAMP-independent mechanisms involving dissociation of the catalytic subunit of protein kinase A from an nuclear factor kappaB-IkappaBalpha-catalytic subunit of protein kinase complex. Thrombin and collagen cause platelet activation and fine-tune this response by initiating downstream nuclear factor kappaB-dependent protein kinase A catalytic subunit activation, as a novel feedback inhibitory signaling mechanism for preventing undesired platelet activation
physiological function
-
in vitro, thrombin and ADP increase the formation of platelet-monocyte aggregates and platelet-granulocyte aggregates as well as tissue factor mRNA expression
physiological function
-
O4+ and proteolipid protein-positive oligodendrocytes display a robust intracellular calcium level rise following thrombin stimulation. Thrombin-induced Ca2+ increase in oligodendrocytes is mediated by protease-activated receptor-1 activation and downstream signaling through G(q/11) and phospholipase C, resulting in Ca2+ recruitment from intracellular compartments
physiological function
-
the degeneration of the dopaminergic neurons of rats is observed after intranigral injection of thrombin
physiological function
-
thrombin activates protease-activated receptor 1 and induces a myofibroblast phenotype in normal lung fibroblasts resembling the phenotype of scleroderma lung myofibroblasts
physiological function
-
thrombin activates protease-activated receptors 1, 3, and 4, but not 2
physiological function
-
thrombin activation of proteinase-activated receptor 1 potentiates the myofilament Ca2+ sensitivity and induces vasoconstriction in porcine pulmonary arteries, the contractile effect of thrombin is abolished by either 4-aminidophenyl methane-sulfonyl fluoride or the proteinase-activated receptor 1 antagonist SCH79797, while it is mimicked by proteinase-activated receptor 1-activating peptide but not proteinase-activated receptor 4-activating peptide
physiological function
-
thrombin does not affect expression of cell-associated pro-matrix metalloproteinase-2 (pro-MMP-2) protein. Thrombin activates pro-MMP-2 in the absence of elevated pro-MMP-2 expression and secretion in CSMCs, and thrombin induces cerebrovascular smooth muscle cells mitogenesis involving its action on MMP-2
physiological function
-
thrombin down-regulates the transforming growth factor-beta-mediated synthesis of collagen and fibronectin by human proximal tubule epithelial cells through the endothelial protein C receptor-dependent activation of protease-activated receptor-1. The activation of protease-activated receptor-1 by thrombin inhibits the tumor necrosis factor -alpha-mediated synthesis of interleukin-6 and interleukin-8 and downregulates the transforming growth factor -beta-mediated expression of extracellular matrix proteins
physiological function
-
thrombin elevates transcripts for interleukin-6, CXCL8, and CCL11 genes and also enhances release of interleukin-6 and CXCL8 protein from human aortic smooth muscle cell, thrombin promotes proinflammatory phenotype in human vascular smooth muscle cell
physiological function
-
thrombin enhances the migration of chondrosarcoma cells by increasing matrix metalloproteinase-2 and matrix metalloproteinase-13 expression through the protease-activated receptor/phospholipase C/protein kinase Calpha/c-Src/nuclear factor-kappaB signal transduction pathway
physiological function
-
thrombin facilitates invasion of ovarian cancer along peritoneum by inducing monocyte differentiation toward tumor-associated macrophage-like cells. Thrombin induces monocytes differentiation into M2-like macrophages with tumor-associated macrophage characteristics. Thrombin does not influence monocytes phagocytosis function significantly
physiological function
-
thrombin induces the activation of p38MAPK in human platelets, thrombin increases tyrosine phosphorylation in a concentration-dependent mannerin, resting or in thrombin stimulated platelets total protein tyrosine phosphorylation, p38MAPK, and cytosolic phospholipase A2 phosphorylation are increased
physiological function
-
thrombin induces the expression of oncostatin M via AP-1 activation in human monocyte-derived macrophages, peripheral blood monocytes, and human plaque macrophages up to 16.8fold after 24 h. Thrombin induces phosphorylation of ERK1/2 and p38 in monocyte-derived macrophages. A functional AP-1 site is required for oncostatin M promoter activation by thrombin
physiological function
-
thrombin is a key enzyme in the coagulation cascade. Proteolysis of prothrombin and thrombin generates antimicrobial activity
physiological function
-
thrombin is involved in blood coagulation and wound healing, thrombin may be a potential regulator of early fracture healing, which results in accelerated bone healing and hypertrophic callus. Activation of PAR-1 by thrombin may be one key regulator of COX-2 expression immediately following injury. Thrombin exerts multiple effects upon osteoblasts including stimulating proliferation, and inhibiting osteoblast differentiation and apoptosis. The pro-inflammatory effects of thrombin are mediated through activation of endothelial cells, smooth muscle cells, and platelets as well as release of cellular mediators. Thrombin also induces brain inflammation by activating microglia
physiological function
-
thrombin is the key terminal enzyme of coagulation, does also promote angiogenesis and stimulates tumor-platelet adhesion, adhesion to endothelium, tumor implantation, tumor cell growth and metastasis. Thrombin also exerts direct effects on cancer cells by activation of the cell cycle through downregulation of p27(Kip1) and induction of Skp2, and cyclins D and A. MicroRNA 222, which inhibits p27(Kip1), is upregulated by thrombin
physiological function
-
thrombin promotes the release of interleukin-8 from alveolar epithelial A549 cells via a mechanism partially involving activation of protease-activated receptor-1, maximal interleukin-8 release is observed in cells incubated with serum-free medium containing 25 nM thrombin (3.6fold increase compared to cells incubated with serum-free medium alone)
physiological function
-
thrombin stimulates arginase I transcription activation and enzyme activity in rat aortic endothelial cells through activating protein-1 activation
physiological function
-
thrombin stimulates retinal pigment epithelium cell proliferation by promoting c-Fos-mediated cyclin D1 expression, thrombin induces the biphasic expression of c-Fos
physiological function
-
thrombin stimulation induces matrix metalloproteinase-9 secretion of monocytes dose- and time-dependently (0-8 units/ml thrombin), inhibition of thrombin-induced matrix metalloproteinase-9 secretion by either MEK inhibitor or p38 kinase inhibitor reveals that the thrombin effect is mediated by both ERK1/2 and p38 pathways
physiological function
-
thrombin transiently inhibits adenylyl cyclase 6, the Ca2+-elevating agent thrombin increases endothelial permeability and decreases cAMP levels
physiological function
-
mechanism of melanoma-associated thrombin activity and von Willebrand factor release from endothelial cell and in vitro mechanisms by which two human metastatic melanoma cell lines, MV3 and WM9, transform the vascular endothelium into a prothrombotic activated state, protective effect of heparins, overview. Low-molecular-weight heparins inhibit melanoma cell-triggered thrombin generation
physiological function
-
pro-atherogenic effects of thrombin, thrombin is a potent modulator of endothelial function and, through stimulation of NF-kappaB, induces endothelial expression of intracellular adhesion molecule-1, ICAM-1, and vascular cell adhesion molecule-1, VCAM-1. These cell surface adhesion molecules recruit inflammatory cells to the vessel wall and thereby participate in the development of atherosclerosis, which is increasingly recognized as an inflammatory condition. The principal receptor for thrombin on endothelial cells is protease-activated receptor-1, PAR-1, a member of the G protein-coupled receptor superfamily. Thrombin induces phosphorylation of Akt and NF-kappaB-responsive gene transcription
physiological function
-
the G-protein receptor-coupled agonist thrombin signal changes the structure of proteoglycans produced by vascular smooth muscle cells. Thrombin induces Akt activation and mediates proteoglycan synthesis, which is inhibited by TGF-beta receptor ALK V inhibition, which is not due to the release and autocrine/paracrine action of TGF-beta. A blockade of PAR-1 and ALK V inhibits thrombin-stimulated phosphorylation of Smad2. Regulations, overview
physiological function
-
thrombin activates the PI3K/PDK1/Akt signaling, stimulating Akt Ser473, not Thr308, phosphorylation, which promotes cyclin D1 upregulation and RPE cell proliferation, overview. Thrombin proteolytic activation of protease-activated G protein coupled receptor-1 (PAR-1) activates PI3K and Akt. Thrombin-induced Akt stimulation promotes cyclin D1 accumulation through the phosphorylation/inhibition of GSK-3beta, thus preventing Thr286 cyclin D1 phosphorylation, nuclear export and degradation
physiological function
-
thrombin evokes Ca2+ signaling in smooth muscle cell and induces smooth muscle cell migration and tumor necrosis factor alpha gene expression
physiological function
-
thrombin induces NF-kappaB activation and IL-8/CXCL8 expression in human lung epithelial cells by a Rac1-dependent PI3K/Akt pathway. Treatment of cells with thrombin causes activation of Rac and Akt, the latter by Ser473 phosphorylation. Thrombin induces NF-kappaB activation and protein expression through multiple signaling pathways such as PKCalpha/c-Src, Rac1, extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, c-Jun N-terminal kinase, IkappaB kinases, and PI3K/Akt, overview
physiological function
-
thrombin induces NF-kappaB activation and IL-8/CXCL8 expression in lung epithelial cells by a Rac1-dependent PI3K/Akt pathway. Treatment of cells with thrombin causes activation of Rac and Akt. Thrombin induces NF-kappaB activation and protein expression through multiple signaling pathways such as PKCalpha/c-Src, Rac1, extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, c-Jun N-terminal kinase, IkappaB kinases, and PI3K/Akt, overview
physiological function
-
Thrombin is a multifunctional serine protease generated by the cleavage of prothrombin at sites of vascular injury, and promotes the conversion of fibrinogen to fibrin. thrombin induces monocyte chemoattractant protein 1, MCP-1, expression through Rho-kinase and subsequent p38MAPK/NF-kappaB signaling pathway activation in vascular endothelial cells leading to the development of atherosclerosis, the Rho/Rho-kinase signaling pathway plays a critical role in thrombin-mediated MCP-1 expression and function, Rho-kinase mediates thrombin-induced MCP-1 expression through p38MAPK and NF-jB activation, mechanism, overview
physiological function
thrombin is regulated via the extended active site region and anion-binding exosites I and II. Protease-activated receptor 3 residues 44-56 and protease-activated receptor 1 residues 49-62 bind to thrombin anion-binding exosite I and exhibit long range effects over to anion-binding exosite II. Hirudin residues 54-65 focus more on anion-binding exosite I and do not transmit influences over to anion-binding exosite II. D-Phe-Pro-Arg-chloromethyl ketone inhibition at the thrombin active site leads to further local and long range consequences to thrombin-anion-binding exosite I ligand complexes with the autolysis loop often most affected
physiological function
the enzyme plays a key role in blood coagulation
physiological function
thrombin is the key enzyme in haemostasis and acts on several substrates involved in clot formation, platelet activation and feed-back regulation of its own formation. During activation of blood coagulation, FIIa is formed by proteolytic cleavage of prothrombin
additional information
-
peptides of the C-terminal region of human thrombin are released upon proteolysis and identified in human wounds displaying length- and sequence-dependent antimicrobial, e.g. against Gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa, the Gram-positive bacterium Staphylococcus aureus, and the fungus Candida albicans, as well as immunomodulating effects. A peptide length of at least 20 amino acids is required for effective anti-inflammatory effects in macrophage models, as well as optimal antimicrobial activity
additional information
-
the thrombin catalytic triad comprises residues His57, Asp102, and Ser195
additional information
-
thrombin and trypsin directly activate vagal C-fibres in C57BL6 mouse lung via protease-activated receptor-1,i.e. PAR1, not via PAR3, PAR2, and PAR4, overview
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C191A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
C220A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
D100A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
D120N
-
site-directed mutagenesis, the mutant shows conformational changes compared to the wild-type enzyme
D14A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
D14lA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
D178A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
D186aA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
D189E
-
site-directed mutagenesis, reduced substrate and monovalent cation specificity and enzyme activity
D189N
-
site-directed mutagenesis, reduced substrate and monovalent cation specificity and enzyme activity
D189S
-
site-directed mutagenesis, reduced substrate and monovalent cation specificity and proteolytic activity, amidolytic activity is slightly reduced
D1aA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
D221A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
D221A/D222K
-
no binding of Na+, crystallization data
D222A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
D60eA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
E14cA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
E14eA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
E14hA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
E186bA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
E192A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
E1cA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
E217C/K224C
-
mutant in which the 225-loop of the Na+-binding site is stabilized by an engineered disulfide bond, the activity of the mutant is dramatically impaired, though thrombomodulin interacts with this mutant with more than 20fold elevated KD to partially restore its activity, the mutant exhibits about 2-3fold higher KD for interaction with Na+ and does not clot fibrinogen or activated protein C in the presence of thrombomodulin
E217K
retains ability to activate the anticoagulant protein C pathway, inable to convert fibrinogen to a fibrin clot. Allosteric inactivation by destabilization of Na+ binding site, thus representing the Na+-free, catalytically slow form
E229A
-
mutation substantially shifts thrombin's specificity in favour of the anticoagulant substrate, protein C
E229K
-
the mutation shifts the substrate specificity of thrombin by 130fold to favor the activation of the anticoagulant substrate protein C over the procoagulant substrate fibrinogen. The mutant enzyme is also less effective in activating platelets, is resistant to inhibition by antithrombin III and displays a prolonged half-life in plasma
E39A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
E77A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
E80A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
E8A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
E97aA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
F227A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
F245A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
F34A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
F60hA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
G193A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
G223a
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
G226A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
G548A
-
naturally occuring mutant, substrate binding pocket mutation, loss of proteolytic activity against native substrates fibrinogen, protein C, and synthetic substrates, reduced ability to bind antithrombin III, causes dysprothrombinemia
H71A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
I24A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
I82A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K109A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K10A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K110A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K169A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K186dA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K224A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K235A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K236A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K240A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K36A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K60fA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K70A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K81A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K9A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
L60A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
L65A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
M84A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
N143P t
-
the mutant features no Na+-dependent enhancement of kcat yet binds Na+ with an affinity comparable to that of wild type
N60gA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
P186A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
P198A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
P37A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
P60bA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
P60cA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
Q38A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R101A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R126A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R14dA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R155A/R271A/R286A
-
site-directed mutagenesis, the mutation of enzyme's proteolytic cleavage sites hinder the activation of the enzyme
R155A/R284A/R271A
-
site-directed mutagenesis, the mutant enzyme can be cleaved only at Arg320, cleavage is completely inhibited by Asp-Tyr-Asp-Tyr-Gln
R155A/R284A/R320A
-
site-directed mutagenesis, the mutant enzyme can be cleaved only at Arg271, no inhibition of cleavage by Asp-Tyr-Asp-Tyr-Gln
R165A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R173A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R175A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R187A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R221aA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R233A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R35A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R4A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R67A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R67C/I82C
-
mutant in which the 70-80 loop of exosite-1 is stabilized by an engineered disulfide bond, mutant does not bind thrombomodulin and exhibits a normal amidolytic activity. The mutant exhibits about 2-3fold higher KD for interaction with Na+ and does not clot fibrinogen or activated protein C in the presence of thrombomodulin
R73A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R75A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R93A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R97A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
S171A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
S214A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
S36aA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
T172A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
T60iA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
T74A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
V163A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
V200A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W215A/E217K
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme, the mutant features a less pronounced anticoagulant/antithrombotic profile compared with the wild-type
W215D
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W215E
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme, mutant W215E is 10fold more specific for protein C than fibrinogen and PAR1
W215F
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W215H
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W215I
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme, mutant W215I features a kcat/Km value for cleavage of fibrinogen that is about 100000fold lower than that of wild-type. The kcat/Km value for PAR1 activation is 10,000fold lower compared with wild-type, but the kcat/Km value for activation of protein C in the presence of thrombomodulin is perturbed
W215L
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W215M
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W215R
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W215T
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W215V
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W215Y
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W237A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W29A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W60dA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W96A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
Y117A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
Y184aA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
Y225A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
Y228A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
Y60aA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
Y76A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
Y89A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
K222D
-
introduction of activation by Na+ similar to human enzyme, wild-type is not activated by Na+
S195A
-
mutation of the catalytic residue, inactive mutant
D189A
-
site-directed mutagenesis, reduced substrate and monovalent cation specificity and enzyme activity
D189A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
E217A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
E217A
-
site-directed mutagenesis, mutation of a residue involved in interaction with substrate factore XIII, the mutant shows reduced activity compared to the wild-type enzyme, the mutation affects hydrolysis of substrates due to interruption of key structural contacts involving the thrombin 220 loop and the S1 specificity pocket
I174A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
I174A
-
site-directed mutagenesis, mutation of a residue involved in interaction with substrate factore XIII, the mutant shows reduced activity compared to the wild-type enzyme
L99A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
L99A
-
site-directed mutagenesis, mutation of a residue involved in interaction with substrate factore XIII, the mutant shows eliminated activity compared to the wild-type enzyme
R77aA
-
site-directed mutagenesis, inactive mutant
R77aA
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
R77aA
-
the mutant of thrombin prevents the autolytic cleavage at R77a in exosite I and enables crystallization of thrombin free of inhibitors
S195A
-
inactive
S195A
-
catalytically inactive mutant enzyme
W215A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W215A
-
site-directed mutagenesis, mutation of a residue involved in interaction with substrate factore XIII, the mutant shows highly reduced activity compared to the wild-type enzyme
W215A
-
site-directed mutagenesis, the mutation significantly compromises cleavage of the anticoagulant protein C but has no effect on the hydrolysis of fibrinogen and PAR1
W215A/E217A
drastically impaired catalytic activity, but able to efficiently activate protein C in presence of thrombomodulin
W215A/E217A
-
strikingly compromised fibrinogen cleavage, severe reduction in cleavage of PAR1, PAR4
W215A/E217A
-
site-directed mutagenesis, mutation of a residue involved in interaction with substrate factore XIII, the mutant shows highly reduced activity compared to the wild-type enzyme
W215A/E217A
-
the thrombin mutant is a potent anticoagulant both in vitro and in vivo
W215A/E217A
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme, the mutant shows significant perturbation of fibrinogen and PAR1 cleavage over protein C activation
W215P
-
site-directed mutagenesis, altered substrate specificity compared to the wild-type enzyme
W215P
-
site-directed mutagenesis, the mutation significantly compromises cleavage of the anticoagulant protein C but has no effect on the hydrolysis of fibrinogen and PAR1
W215A/E217A
-
largely compromised fibrinogen cleavage, severe reduction in cleavage of PAR1, PAR4
W215A/E217A
-
the thrombin mutant is a potent anticoagulant both in vitro and in vivo
additional information
-
immobilization of thrombin, determination of optimal conditions, overview. Application of immobilized thrombin for production of S-thanatin, small antimicrobial peptide with 21 amino acid residue, expressed in Escherichia coli strain BL21(DE3) as a fusion protein containing thrombin cleavage site. The immobilizes thrombin in polyacrylamide gel shows excellent cleavage performance within wider ranges of pH value and temperature for reaction than free enzyme, and the residual activity remain above 75% after ten times of usage
additional information
a natural deletion mutant DELTAK9 of prothrombin from 2 homozygous humans lacks Lys9 and Lys10 residues of the A-chain shows 18fold reduced activity with substrate D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide and 60fold reduced activity with fibrinopeptide A compared to the wild-type enzyme, mutant shows reduced sensitivity to antithrombin, and Na+, and a defective PARI receptor recognition, thus reduced platelet activation, alteration of A-and B-chain conformation, especially insertion loop 60, and the catalytic triad residues
additional information
-
a natural deletion mutant DELTAK9 of prothrombin from 2 homozygous humans lacks Lys9 and Lys10 residues of the A-chain shows 18fold reduced activity with substrate D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide and 60fold reduced activity with fibrinopeptide A compared to the wild-type enzyme, mutant shows reduced sensitivity to antithrombin, and Na+, and a defective PARI receptor recognition, thus reduced platelet activation, alteration of A-and B-chain conformation, especially insertion loop 60, and the catalytic triad residues
additional information
-
construction of diverse mutants by site-directed mutagenesis, reduced activity or no remaining activity in activation of factor V and factor VIII, overview
additional information
-
defective mutant enzymes of 2 humans with congenital afibrinogenemia, termed MC and KU, show impaired binding of thrombin to the thrombin binding sites of fibrin and fibrin gamma' peptides, respectively
additional information
-
chemical modification of carboxyl groups by glycine ethyl ester. Modified enzyme induces platelet aggregation through the activation of PAR1, and modified anhydrothrombin inhibits this process completely. Neither modified anhydrothrombin nor modified thrombin inhibit thrombin-induced platelet aggregation
additional information
-
fusion of the N-terminal acidic extension, residues 1-75, of heparin cofactor II to alpha1-proteinase inhibitor M358R to the enzyme specifically increases the rate of thrombin inhibition by 6fold, the mutant is termed HAPI M358R, maximal enhancement of alpha1-PI M358R activity requires the acidic residues between HCII residues 55 and 75, because no enhancement is observed either by fusion of residues 1-54 alone or by fusion of a mutated HCII acidic extension in which all Glu and Asp residues between positions 55 and 75 are neutralized by mutation, overview
additional information
-
lack of thrombin generation in factor II-deficient plasma
additional information
-
engineering thrombin for selective specificity toward protein C and PAR1 by site-directed mutagenesis, overview
additional information
-
when the W215E mutation is combined with deletion of nine residues in the autolysis loop, which by itself shifts the specificity of the enzyme from fibrinogen and PAR1 to protein C, the resulting construct features significant activity only toward PAR1
additional information
-
in mice homozygously lacking the thrombin inhibitor protease nexin, the PI3K-Akt pathway is constitutively activated and expression of myofibroblastic marker smooth-muscle actin is enhanced in vivo in hair follicle dermal cells
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diagnostics
concentrations of active alpha-thrombin, tissue factor-factor VIIa-factor Xa ternary complex, and intrinsic tenase complex with factor X, at specific time windows, can be used to classify acute coronary syndromes to an accuracy of about 87.2%. Such a combination can be used to efficiently assay the coagulation system
nutrition
-
comparison of anticoagulation response to thrombin inhibitors ximelagatran and warfarin in rats on a normal diet to those on a vitamin K deficient diet. Ximelagatran and warfarin increase prothrombin time, activated partial thromboplastin time and ecarin clotting time in rats on normal diet. Vitamin K deficient diet alone causes modest increases in prothrombin time, activated partial thromboplastin time and ecarin clotting time. The anticoagulant activity of both ximelagatran and warfarin is significantly greater in rats on vitamin K deficient diet compared to those on normal diet. Thrombin activity is reduced by both ximelagatran and warfarin to 58% and 44%, respectively, in rats on normal diet. Thrombin activity is virtually abolished by both drugs in rats on vitamin K deficient diet
additional information
a modified in situ proteolysis approach is applied to specifically remove the His tag by thrombin cleavage during crystallization screening trials. This improves the morphology and diffraction quality of the crystals and allowes the acquisition of high-resolution diffraction data and structure solution
analysis
-
detection of enzyme complexed with polyclonal anti-prothrombin antiserum. Enzyme retains enzymatic activity, and binding to antibody may enhance the efficiency of proenzyme activation
analysis
-
affinity probe capillary electrophoresis/laser-induced fluorescence polarization assay for detection of human thrombin using a specific aptamer as probe. Monovalent and bivalent cations promoting the formation of a stable G quadruplex conformation in the aptamer may enhance the binding of the aptamer and thrombin, while cations like K+ and Mg2+ cannot stabilize the affinity complex. Without the use of typical cations, a highly sensitive assay of human thrombin was developed with the corresponding detection limits of 4.38×10?19 and 2.94×10?19 mol in mass for standard solution and human serum, respectively
analysis
-
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
analysis
-
development of a biosensor for thrombin detection using surface-enhanced Raman spectroscopy. The method utilizes the electrostatic interaction between capture thrombin aptamer and probe crystal violet molecules. Procedure shows a highly specific selectivity and a linear detection of thrombin in the range from 0.1 nM to 10 nM with a detection limit of about 20 pM and realizes the thrombin detection in human blood serum solution directly
analysis
-
development of a direct and an indirect competitive assay for thrombin by an electrochemical aptamer-based assay coupled to magnetic beads. With the direct competitive assay, when the aptamer is immobilised onto the magnetic beads, a detection limit of 430 nM for thrombin is achieved. A detection limit of 175 nM is obtained by detecting the product of the enzymatic reaction catalysed by thrombin. A sandwich assay reaches a detection limit of 0.45 nM of thrombin
analysis
-
development of a modified electrochemical sandwich model for target protein detection using differential pulse voltammetry. With model target analyte thrombin, the sensor shows a linear response for thrombin in the range 1-60 nM with a detection limit of 0.5 nM
analysis
-
development of an aptamer-based surface enhanced resonance Raman scattering sensor with high sensitivity, specificity, and stability for the detection of human alpha-thrombin. The sensor displays a limit of detection of 100 pM by monitoring the signal change upon the single-step of thrombin binding to immobilized thrombin binding aptamer and specifically discriminates thrombin from other proteins. The sensor can detect 1 nM thrombin in the presence of complex biofluids, such as 10% fetal calf serum, and is sufficiently robust for clinical diagnostic applications
analysis
-
study on the effects of dilution on the thrombin generation process in assessing the clotting function. Anticoagulant pathways are far more affected by dilution than the procoagulant pathways. Plasma dilution causes a loss of sensitivity towards thrombomodulin and activated protein C. At dilutions above 1:12 a second wave of prothrombinase-activity is observed
analysis
-
design of an aptamer-based suspension array detection platform for the sensitive, specific and rapid detection of human alpha-thrombin as a model. Thrombin is first recognized by a 29-mer biotinylated thrombin-binding aptamer in solution. Then 15-mer TBA modified magnetic beads capture the former aptamer-thrombin to form an aptamer-thrombin-aptamer sandwich complex. The median fluorescence intensity obtained via suspension array technology is positively correlated with the thrombin concentration. The dynamic quantitative working range of the aptamer-based suspension array is 18.37-554.31 nM, and the coefficients of determination R2 are greater than 0.9975. The lowest detection limit of thrombin is 5.4 nM. The method is highly specific for thrombin without being affected by other analogs and interfering proteins. The recoveries of thrombin spiked in diluted human serum are in the range 82.6-114.2%
biotechnology
-
fibrin is a biopolymer that has been used in a variety of biomaterial, cell delivery and tissue engineering applications, the enzyme thrombin catalyzes the formation of fibrin microfibrils, which form a three-dimensional mesh in which cells can be directly embedded at the time of gel formation, method development, overview
biotechnology
-
usage of human thrombin in a fibrin glue, method development, thrombin initiates clotting and cross-linking of fibrin from cryoprecipitate to produce an entirely autologous fibrin glue, overview
medicine
-
the enzyme can be engineered to function in vivo as a potent anticoagulant that may possess a superior therapeutic profile with reduced potential for bleeding complications
medicine
-
enzyme inhibitors are used in therapy and prevention of venous and arterial thrombosis, inhibition mode, efficiency and safety, overview
medicine
-
enzyme is a target for development of inhibitors in antithrombotic therapy
medicine
-
enzyme activation of factor VIII mutant R372H, occuring in patients with hemophilia A, is about 80fold decreased, resulting in generation of about 6.1 nM factor X4 per min compared to 13 nM for wild-type
medicine
-
exposure to thrombin induces an increase in cytosolic calcium in both anterior and equatorial lens cells. Repeated exposure produces a significant increase in cell coverage in the capsular bag model and increased thymidine incorporation into FHL124 cells. In FHL124 cells, exposure to thrombin induces biphasic increases in the phosphorylation of p42/p44
medicine
-
mechanism of high affinity fibrinogen binding and cleavage in Staphylococcus aureus mediated endocarditis
medicine
-
affinity probe capillary electrophoresis/laser-induced fluorescence polarization assay for detection of human thrombin using a specific aptamer as probe. Monovalent and bivalent cations promoting the formation of a stable G quadruplex conformation in the aptamer may enhance the binding of the aptamer and thrombin, while cations like K+ and Mg2+ cannot stabilize the affinity complex. Without the use of typical cations, a highly sensitive assay of human thrombin was developed with the corresponding detection limits of 4.38×10?19 and 2.94×10?19 mol in mass for standard solution and human serum, respectively
medicine
-
beta2-glycoprotein I may regulate thrombin inactivation by heparin cofactor II. The presence of anti-beta2-glycoprotein I antibodies potentiates the protective effect of beta2-glycoprotein I on thrombin and may explain the prothrombic tendency in patients with antiphospholipid syndrome
medicine
-
comparison of anticoagulation response to thrombin inhibitors ximelagatran and warfarin in rats on a normal diet to those on a vitamin K deficient diet. Ximelagatran and warfarin increase prothrombin time, activated partial thromboplastin time and ecarin clotting time in rats on normal diet. Vitamin K deficient diet alone causes modest increases in prothrombin time, activated partial thromboplastin time and ecarin clotting time. The anticoagulant activity of both ximelagatran and warfarin is significantly greater in rats on vitamin K deficient diet compared to those on normal diet. Thrombin activity is reduced by both ximelagatran and warfarin to 58% and 44%, respectively, in rats on normal diet. Thrombin activity is virtually abolished by both drugs in rats on vitamin K deficient diet
medicine
-
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
medicine
-
comparison of thrombin inhibitors lepirudin and argatroban for treatment of heparin-induced thrombocytopenia. Adult subjects with a positive anti-heparin platelet factor 4 antibody test and more than 50% decrease in platelet count during the first 30 days of admission over a period of 2 years were included in the study. Subjects treated with a thrombin inhibitor are more likely to experience platelet count recovery, with 87.5% for the lepirudin group and 82.4% for the argatroban group, compared to those who do not receive antithrombin therapy. The thrombosis rate for subjects who do not receive antithrombin therapy after the diagnosis of heparin-induced thrombocytopenia is 26.8%, compared to 8.3% for the lepirudin group and 5.9% for the argatroban group
medicine
-
development of a biosensor for thrombin detection using surface-enhanced Raman spectroscopy. The method utilizes the electrostatic interaction between capture thrombin aptamer and probe crystal violet molecules. Procedure shows a highly specific selectivity and a linear detection of thrombin in the range from 0.1 nM to 10 nM with a detection limit of about 20 pM and realizes the thrombin detection in human blood serum solution directly
medicine
-
development of a modified electrochemical sandwich model for target protein detection using differential pulse voltammetry. With model target analyte thrombin, the sensor shows a linear response for thrombin in the range 1-60 nM with a detection limit of 0.5 nM
medicine
-
development of an aptamer-based surface enhanced resonance Raman scattering sensor with high sensitivity, specificity, and stability for the detection of human alpha-thrombin. The sensor displays a limit of detection of 100 pM by monitoring the signal change upon the single-step of thrombin binding to immobilized thrombin binding aptamer and specifically discriminates thrombin from other proteins. The sensor can detect 1 nM thrombin in the presence of complex biofluids, such as 10% fetal calf serum, and is sufficiently robust for clinical diagnostic applications
medicine
-
examination of the effect of thrombin on tumor cell cycle activation and spontaneous growth in synchronized serum-starved tumor cell lines and a model of spontaneous prostate cancer development in TRAMP mice expressing the SV40 Large T Antigen under the control of the prostate-specific probasin promoter, leading to the spontaneous development of prostate cancer and metastasis. Prostate LNCaP cells arrested in G0 and treated with thrombin or serum reveal a 48- and 29-fold increase in S phase cells, respectively, at 8 hours. Addition of thrombin, PAR-1 agonist TFLLRN, or serum down-regulates the inhibitory cell cycle regulator p27Kip1 with concomitant induction of Skp2, cyclin D1, and cyclin A with similar kinetics. LNCaP p27Kip1-transfected cells or Skp2 knockdown cells are refractory to thrombin-induced cell cycle activation. Repetitive thrombin injection enhances prostate tumor volume 6- to 8-fold. Repetitive hirudin injection, a specific potent antithrombin, decreases tumor volume 13- to 24fold
medicine
-
exogenous oxidative stress, thrombin activation, progression of ageing and type 2 diabetes lead to protein carbonyls formation in platelets, and this modification can be attenuated by antioxidant enzymes
medicine
-
exogenous oxidative stress, thrombin activation, progression of ageing and type 2 diabetes lead to protein carbonyls formation in platelets, and this modification can be attenuated by antioxidant enzymes
medicine
-
exogenous oxidative stress, thrombin activation, progression of ageing and type 2 diabetes lead to protein carbonyls formation in platelets, and this modification can be attenuated by antioxidant enzymes
medicine
-
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
medicine
-
in patients with acute ST-segment elevation myocardial infarction who have received tenecteplase together with aspirin and heparin, thrombin-antithrombin complexes correlate with tissue factor activity associated with microparticles, and correlates with soluble platelet glycoprotein. Fibrinolysis failure in acute ST-segment elevation myocardial infarction is characterized by a higher procoagulant state associated with tissue factor activity associated with microparticles and lower plasmin generation
medicine
-
in patients with first spontaneous venous thromboembolism, high endogenous thrombin potential confers an 1.6fold increased risk of recurrence, and risk of recurrence is 2.8fold higher among patients with both high endogenous thrombin potential and high fibrin D-dimer
medicine
-
in patients with rheumatoid arthritis, citrullinated fibrin and fibrinogen are present in the synovium. Citrullinated fibrinogen is not a substrate for thrombin and may be associated with the pathophysiology of rheumatoid arthritis
medicine
-
placentas from pregnancies complicated by preterm preeclampsia have a significantly higher frequency of strong receptor PAR-1 expression than placentas from women with spontaneous pre-term labour. Role for PAR-1 as a mediator of the effect of thrombin on coagulation and inflammation in preeclampsia. The effects of thrombin in preeclampsia are due to increased thrombin generation and higher expression of PAR-1
medicine
-
rabbits receiving infusions with recombinant hirudin containing the RGD motif, which competitively inhibits the binding of fibrinogen to GP IIb/IIIa on platelets, have prolonged thrombin time, prothrombin time. and activated partial thromboplastin time which are similar to that of wild-type hirudin. In addition, recombinant RGD-hirudin is capable of inhibiting platelet aggregation and is two to three times more effective than wild-type hirudin in preventing thrombosis
medicine
-
thrombin augments the contractility of uterine smooth muscle cell and immortalized myometrial smooth muscle cell collagen gels. The effect is inhibited by thrombin inhibitor hirudin. Thrombin-induced collagen contractility results in activation of thrombin receptor F2R
medicine
-
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
medicine
-
treatment of adults with one or more mild or moderate bleeding sites not manageable by conventional modalities during elective cardiovascular, neurologic, or general surgey procedures with human or bovine thrombin, applied topically with an absorbable gelatin sponge. The proportions of patients achieving hemostasis within 10 min, 6 min or 3 min were equivalent for human and bovine thrombin.12.7% of patients who received bovine thrombin demonstrated seroconversion compared with 3.3% of the patients who received human thrombin
medicine
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treatment of adults with one or more mild or moderate bleeding sites not manageable by conventional modalities during elective cardiovascular, neurologic, or general surgey procedures with human or bovine thrombin, applied topically with an absorbable gelatin sponge. The proportions of patients achieving hemostasis within 10 min, 6 min or 3 min were equivalent for human and bovine thrombin.12.7% of patients who received bovine thrombin demonstrated seroconversion compared with 3.3% of the patients who received human thrombin. None of the patients in the human thrombin group developed seroconversion for anti-human thrombin or anti-human factor V/Va antibodies
medicine
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treatment of iatrogenic pseudoaneurisms of the trunk by injection of 765 IU thrombin. Both percutaneous and endoluminal techniques are technically feasible and safe but the questioning of dosage and long-term results need further experiences
medicine
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treatment of pigs that underwent mid-left anterior descending coronary artery occlusion followed by reperfusion with saline vehicle or thrombin fragment TP508, i.e. chrysalin as a bolus into the ischemic period followed by continuous intravenous infusion. Endothelium-dependent coronary microvascular relaxation is greater in the TP508 group and associated with higher endothelial nitric oxide synthase phosphorylation. Both infarct size and TUNEL staining is decreased in the TP508 group compared with the saline control group. ession of cell survival proteins B-cell lymphoma and heat shock protein-73 is higher in the TB508 group. Expression of cell death-signaling proteins polyadenosine-diphosphate-ribose polymerase, cleaved polyadenosine-diphosphate-ribose polymerase, and B-cell lymphoma2/adenovirus E1B 19 kDa-interacting protein is significantly higher in the TB508 group in the ischemic territory
medicine
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when endothelial protein C receptor is ligated by protein C, the cleavage of receptor PAR-1 by thrombin initiates antiinflammatory responses, thus leading to activation of Rac I and inhibition of RhoA and nuclear factor kappaB signaling cascades
medicine
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thrombin activation is not related to the measured thrombus surface area or thrombus volume in patients with abdominal aortic aneurysms
medicine
because of the essential role of thrombin in the coagulation cascade, achieving the ability to specifically modulate thrombin activity represents a major goal in the development of anticoagulant strategies. Thrombin-binding aptamer (TBA), is a single-stranded 15-mer DNA with the sequence (5'-GGT TGG TGT GGT TGG-3') that binds thrombin with high specificity and affinity. TBA specifically inhibits clot-bound thrombin and reduces arterial thrombus formation. Native TBA consisting of only natural bases is susceptible to nuclease digestion and has a very short half-life in vivo of 108/s. Its binding affinity and selectivity need to be optimized. These optimization efforts are of critical importance in both diagnostic and therapeutic applications. Chemical modification of the DNA aptamer can be used to significantly improve its binding affinity
medicine
fibrinogenolytic properties make the enzyme applicable for biochemical research and drug development on thrombolytic therapy
synthesis
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production of recombinant human prethrombin-2 in mouse myeloma cells, activation by recombinant ecarin and purification by affinity chromatography. Yield is about 70%, product is indistinguishable from plasma-derived enzyme
synthesis
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preparation of thrombin from human plasma. Isolation of prothrombin is followed by activation to thrombin and further purification, process is suitable for large-scale production with a high degree of virus safety
synthesis
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use of thrombin as enhancer in polymerase chain reaction. Presence of bovine thrombin is exceptionally effective at preventing the formation of primer dimers and enhancing the formation of the desired polymerase chain reaction products. The PCR enhancement effects of thrombin apply to low-copy synthetic single-stranded DNAs, synthetic ssDNA pools, human genomic DNA, or hepatitis B virus genomic DNA. Thrombin is also able to effectively relieve PCR inhibition by nanomaterial inhibitors such as gold nanoparticles and graphene oxide. Compared with bovine serum albumin, thrombin is more effective and requires concentrations 18-178 times less than that of serum albumin to achieve a similar level of PCR enhancement