Information on EC 3.4.21.5 - thrombin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.5
-
RECOMMENDED NAME
GeneOntology No.
thrombin
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9002-04-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
salmon
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ac-Gly-Gly-Val-Arg-7-amido-4-methylcoumarin + H2O
Ac-Gly-Gly-Val-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Ac-Leu-Gly-Val-Arg-7-amido-4-methylcoumarin + H2O
Ac-Leu-Gly-Val-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Ac-Nle-Thr-Leu-Arg-7-amido-4-methylcoumarin + H2O
Ac-Nle-Thr-Leu-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Ac-Nle-Thr-Pro-Arg-7-amido-4-methylcoumarin + H2O
Ac-Nle-Thr-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Ac-Val-Thr-Pro-Arg-7-amido-4-methylcoumarin + H2O
Ac-Val-Thr-Pro-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
activated protein C + H2O
?
show the reaction diagram
-
-
-
-
?
ADAMTS-13 + H2O
?
show the reaction diagram
Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
-
synthetic chromogenic substrate
-
?
benzoyl-Arg ethyl ester + H2O
benzoyl-Arg + ethanol
show the reaction diagram
-
-
-
-
?
benzoyl-Arg methyl ester + H2O
benzoyl-Arg + methanol
show the reaction diagram
-
-
-
-
?
benzoyl-L-Arg-p-nitroanilide + H2O
benzoyl-L-Arg + p-nitroaniline
show the reaction diagram
-
-
-
-
?
beta-Ala-Gly-Arg-4-nitroanilide + H2O
beta-Ala-Gly-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
chromozym TH + H2O
? + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide + H2O
D-Phe-L-pipecolyl-L-Arg + 4-nitroanilide
show the reaction diagram
-
-
-
-
?
D-Phe-L-Pro-L-Arg-4-nitroanilide + H2O
D-Phe-L-Pro-L-Arg + 4-nitroaniline
show the reaction diagram
D-Phe-L-Pro-L-Phe-4-nitroanilide + H2O
D-Phe-L-Pro-L-Phe + 4-nitroaniline
show the reaction diagram
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
show the reaction diagram
-
i.e. S-2238
-
-
?
D-Phe-Pro-Arg-4-nitroanilide + H2O
D-Phe-Pro-Arg + 4-nitroaniline
show the reaction diagram
D-Phe-Pro-Lys-4-nitroanilide + H2O
D-Phe-Pro-Lys + 4-nitroaniline
show the reaction diagram
D-Phe-Pro-Phe-4-nitroanilide + H2O
D-Phe-Pro-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
show the reaction diagram
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine-4-nitroaniline
show the reaction diagram
-
-
-
-
?
di-L-Glu-L-Pro-L-Arg-4-nitroanilide + H2O
di-L-Glu-L-Pro-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
factor V (1018) + H2O
?
show the reaction diagram
-
cleavage site is LSPR
-
?
factor V (1545) + H2O
?
show the reaction diagram
-
cleavage site is WYLR
-
?
factor V (709) + H2O
?
show the reaction diagram
-
-
-
?
factor V + H2O
activated factor V + ?
show the reaction diagram
-
activation
-
-
?
factor V + H2O
factor Va + propeptide
show the reaction diagram
-
proteolytic activation
-
?
factor VII (1689) + H2O
?
show the reaction diagram
-
clevage site is QSPR
-
?
factor VII (372) + H2O
?
show the reaction diagram
-
cleavage site is IQIR
-
?
factor VII (740) + H2O
?
show the reaction diagram
-
-
-
?
factor VIII + H2O
?
show the reaction diagram
factor VIII + H2O
activated factor VIII + ?
show the reaction diagram
-
activation
-
-
?
factor VIII + H2O
factor VIIIa + propeptide
show the reaction diagram
factor VIII mutant D392A/D394A + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
mutation to P3-P3' residues flanking Arg740, 98% of the activtiy with wild-type
-
?
factor VIII mutant Q370S/I371P/V374F/A375Q + H2O
?
show the reaction diagram
-
-
mutation to P3-P3' residues flanking Arg1689, 14% of the activtiy with wild-type
-
?
factor VIII mutant R372H + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
cleavage of Arg372 involving exosite II, the heparin binding site
-
?
factor X + H2O
factor Xa + propeptide
show the reaction diagram
factor XI + H2O
?
show the reaction diagram
-
-
-
?
factor XI + H2O
activated factor XI + ?
show the reaction diagram
-
activation
-
-
?
factor XI + H2O
factor XIa
show the reaction diagram
-
activation by thrombin
-
-
?
factor XI + H2O
factor XIa + propeptide
show the reaction diagram
-
proteolytic activation
-
?
factor XII + H2O
activated factor XII + ?
show the reaction diagram
factor XIII + H2O
?
show the reaction diagram
-
-
-
?
factor XIII + H2O
activated factor XIII + ?
show the reaction diagram
factor XIII + H2O
factor XIIIa + propeptide
show the reaction diagram
factor XIII V34L mutant + H2O
activated factor XIII V34L mutant + ?
show the reaction diagram
-
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
?
show the reaction diagram
-
ferrocene-labelled tetrapeptide with a polyethylene glycol linker
-
-
?
Fc-[RFSRPQL]-PEG + H2O
?
show the reaction diagram
-
ferrocene-labelled heptapeptide with a polyethylene glycol linker
-
-
?
fibrin I-plasma factor XIII complex + H2O
activation peptide + fibrinopeptide B
show the reaction diagram
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
fibrinogen + H2O
fibrin
show the reaction diagram
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
show the reaction diagram
fibrinogen + H2O
fibrin + fibrinoepeptide A + fibrinopeptide B
show the reaction diagram
-
-
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
show the reaction diagram
fibrinogen 1 + H2O
fibrin 1 + fibrinopeptide A + fibrinopeptide B
show the reaction diagram
fibrinogen 2 + H2O
fibrin 2 + fibrinopeptide A + fibrinopeptide B
show the reaction diagram
fibrinogen A a + H2O
?
show the reaction diagram
-
-
-
?
fibrinogen B b + H2O
?
show the reaction diagram
-
-
-
?
fibrinopeptide A + H2O
?
show the reaction diagram
galectin-8 + H2O
?
show the reaction diagram
galectin-9 + H2O
?
show the reaction diagram
GLVPRGVNL + H2O
GLVPR + GVNL
show the reaction diagram
-
residues 33-41 of factor XIII with mutation V34L
-
-
?
GVVPRGVNL + H2O
GVVPR + GVNL
show the reaction diagram
-
residues 33-41 of factor XIII
-
-
?
HD-cyclohexylglycyl-Ala-Arg-4-nitroanilide + H2O
HD-cyclohexylglycyl-Ala-Arg + 4-nitroaniline
show the reaction diagram
-
assay method optimization with synthetic substrate HD-cyclohexylglycyl-Ala-Arg-4-nitroanilide, overview
-
-
?
Meizothrombin + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Arg 4-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Arg + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Lys 4-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Lys + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-p'-(Nbeta,n-butyl-Nalpha-guanidino)benzoate + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-p'-(Nbeta,n-hexyl-Nalpha-guanidino)benzoate + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-p'-guanidinobenzoate + H2O
?
show the reaction diagram
-
-
-
-
?
PAR1 + H2O
?
show the reaction diagram
PAR1 peptide + H2O
?
show the reaction diagram
protease-activated receptor I peptide fragment, amino acid sequence
-
?
PAR3 + H2O
?
show the reaction diagram
-
protease-activated receptor 3
-
?
PAR4 + H2O
?
show the reaction diagram
Pefachrom tPa + H2O
?
show the reaction diagram
-
-
-
-
?
platelet thrombin receptor peptide + H2O
?
show the reaction diagram
-
-
-
-
?
prethrombin + H2O
?
show the reaction diagram
-
cleavage of R284-T285 bond
-
-
?
pro-factor XIII + H2O
factor XIII
show the reaction diagram
-
activation by cleavage at Arg37 leading to blood coagulation
-
?
profactor V + H2O
factor V
show the reaction diagram
-
human, activation, recombinant
-
?
profactor VIII + H2O
factor VIII
show the reaction diagram
-
human, activation, recombinant
-
?
protease-activated receptor + H2O
?
show the reaction diagram
-
activation
-
-
?
protease-activated receptor + H2O
activated protease-activated receptor + ?
show the reaction diagram
-
activation
-
-
?
protease-activated receptor 1 + H2O
?
show the reaction diagram
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
show the reaction diagram
-
activation
-
-
?
protease-activated receptor 3 residues 44-56 + H2O
-
show the reaction diagram
-
-
-
-
?
protease-activated receptor 4 + H2O
activated PAR-4 + ?
show the reaction diagram
-
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
?
show the reaction diagram
protease-activated receptor-1 + H2O
activated PAR-1
show the reaction diagram
-
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
?
show the reaction diagram
-
activation
-
-
?
protease-activated receptor-4 + H2O
?
show the reaction diagram
-
activation
-
-
?
protein C + H2O
?
show the reaction diagram
protein C + H2O
activated protein C + ?
show the reaction diagram
-
solvent isotope effect study
-
-
?
protein C zymogen + H2O
activated protein C + propeptide
show the reaction diagram
protein kinase C + H2O
?
show the reaction diagram
-
activation
-
-
?
proteinase-activated receptor 1 + H2O
?
show the reaction diagram
-
alpha-thrombin may not effectively catalyze proteinase-activated receptor 1-(1-41) generation
-
-
?
proteinase-activated receptor 4 + H2O
?
show the reaction diagram
-
alpha-thrombin may not effectively catalyze proteinase-activated receptor 4-(1-47) generation
-
-
?
prothrombin + H2O
?
show the reaction diagram
-
cleavage of R155-S156 and R284-T285 bond
-
-
?
RAP + H2O
?
show the reaction diagram
-
-
-
-
?
S-thanatin + H2O
?
show the reaction diagram
-
-
-
-
?
S2238 + H2O
?
show the reaction diagram
spectrozyme TH + H2O
?
show the reaction diagram
-
-
-
-
?
spectrozyme-TH + H2O
?
show the reaction diagram
succinyl-AAPR-4-nitroanilide + H2O
succinyl-AAPR + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
thrombin-activable finrinolysis inhibitor + H2O
?
show the reaction diagram
-
i.e. TAFI
-
?
thrombin-activatable fibrinolysis inhibitor + H2O
?
show the reaction diagram
Tosyl-Arg methyl ester + H2O
Tosyl-Arg + methanol
show the reaction diagram
tosyl-Gly-L-Pro-L-Arg-4-nitroanilide + H2O
tosyl-Gly-L-Pro-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
tosyl-Gly-Pro-Arg + 4-nitroaniline
show the reaction diagram
transmembrane receptor PAR1 + H2O
?
show the reaction diagram
-
-
-
?
TVELQGLVPRGVNL + H2O
TVELQGLVPR + GVNL
show the reaction diagram
-
residues 28-41 of factor XIII with mutation V34L
-
-
?
TVELQGVVPRGVNL + H2O
TVELQGVVPR + GVNL
show the reaction diagram
-
residues 28-41 of factor XIII
-
-
?
UpA + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
activated protein C + H2O
?
show the reaction diagram
-
-
-
-
?
ADAMTS-13 + H2O
?
show the reaction diagram
-
proteolysis of ADAMTS-13 by thrombin causes an 8fold reduction in its affinity for von Willebrand factor VWF that contributes to its loss of VWF-cleaving function, physiologic function, overview
-
-
?
factor V + H2O
activated factor V + ?
show the reaction diagram
-
activation
-
-
?
factor V + H2O
factor Va + propeptide
show the reaction diagram
-
proteolytic activation
-
?
factor VIII + H2O
?
show the reaction diagram
-
activation by cleavage of Arg372, Arg74, and Arg1689, plays a fundamental role in the amplification of the coagulation cascade
-
?
factor VIII + H2O
activated factor VIII + ?
show the reaction diagram
-
activation
-
-
?
factor VIII + H2O
factor VIIIa + propeptide
show the reaction diagram
-
proteolytic activation
-
?
factor X + H2O
factor Xa + propeptide
show the reaction diagram
factor XI + H2O
activated factor XI + ?
show the reaction diagram
-
activation
-
-
?
factor XI + H2O
factor XIa
show the reaction diagram
-
activation by thrombin
-
-
?
factor XI + H2O
factor XIa + propeptide
show the reaction diagram
-
proteolytic activation
-
?
factor XII + H2O
activated factor XII + ?
show the reaction diagram
-
activated factor XII cross-links fibrin molecules and stabilizes the fibrin clot
-
-
?
factor XIII + H2O
activated factor XIII + ?
show the reaction diagram
-
the enzyme is involved in the coagulation cascade, overview
-
-
?
factor XIII + H2O
factor XIIIa + propeptide
show the reaction diagram
-
proteolytic activation
-
?
Fibrinogen + H2O
?
show the reaction diagram
fibrinogen + H2O
fibrin
show the reaction diagram
-
-
-
-
?
fibrinogen + H2O
fibrin + ?
show the reaction diagram
fibrinogen + H2O
fibrin + fibrinoepeptide A + fibrinopeptide B
show the reaction diagram
-
-
-
-
?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
show the reaction diagram
fibrinogen 1 + H2O
fibrin 1 + fibrinopeptide A + fibrinopeptide B
show the reaction diagram
fibrinogen 2 + H2O
fibrin 2 + fibrinopeptide A + fibrinopeptide B
show the reaction diagram
fibrinopeptide A + H2O
?
show the reaction diagram
-
-
-
-
?
galectin-8 + H2O
?
show the reaction diagram
-
although intact isoform G8L stimulates neutrophil adhesion to substrate more efficiently than isoform G8M, the activity of isoform G8L but not that of isoform G8M decreases on thrombin digestion, overview
-
-
?
galectin-9 + H2O
?
show the reaction diagram
-
thrombin treatment almost completely abolishes eosinophil chemoattractant activity of isoform G9L, overview
-
-
?
pro-factor XIII + H2O
factor XIII
show the reaction diagram
-
activation by cleavage at Arg37 leading to blood coagulation
-
?
protease-activated receptor + H2O
?
show the reaction diagram
-
activation
-
-
?
protease-activated receptor 1 + H2O
?
show the reaction diagram
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
show the reaction diagram
-
activation
-
-
?
protease-activated receptor-1 + H2O
?
show the reaction diagram
protease-activated receptor-1 + H2O
activated PAR-1
show the reaction diagram
-
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
?
show the reaction diagram
-
activation
-
-
?
protease-activated receptor-4 + H2O
?
show the reaction diagram
-
activation
-
-
?
protein C zymogen + H2O
activated protein C + propeptide
show the reaction diagram
protein kinase C + H2O
?
show the reaction diagram
-
activation
-
-
?
proteinase-activated receptor 1 + H2O
?
show the reaction diagram
-
alpha-thrombin may not effectively catalyze proteinase-activated receptor 1-(1-41) generation
-
-
?
proteinase-activated receptor 4 + H2O
?
show the reaction diagram
-
alpha-thrombin may not effectively catalyze proteinase-activated receptor 4-(1-47) generation
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Thrombomodulin
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Li+
-
activates, can partially substitute for Na+, binding to Asp189
NaCl
-
50% activation at 600 mM
Rb+
-
activates, can partially substitute for Na+, binding to Asp189
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R)-2-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-cyclohexyl-2-oxoethanaminium chloride
-
-
(1R)-2-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-cyclopentyl-2-oxoethanaminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-oxo-3-phenylpropan-2-aminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-oxobutan-2-aminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-1-oxopropan-2-aminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-3,3-dimethyl-1-oxobutan-2-aminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-3-cyclohexyl-1-oxopropan-2-aminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-3-methyl-1-oxobutan-2-aminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-4,4-dimethyl-1-oxopentan-2-aminium chloride
-
-
(2R)-1-[(2S)-2-[(3-chlorobenzyl)carbamoyl]pyrrolidin-1-yl]-4-methyl-1-oxopentan-2-aminium chloride
-
-
(2S)-1-(1,3-benzodioxol-5-ylacetyl)-N-(thiophen-2-ylmethyl)pyrrolidine-2-carboxamide
-
-
(2S)-1-(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
acacetin
-
-
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
-
antithrombin
-
antithrombin III
-
apigenin
-
-
AR-H067637
argatroban
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
AZD0837
baicalein
-
-
Baicalin
-
slight inhibition
benzamidine
-
-
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
-
-
bivalirudin
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
-
-
dabigatran
dabigatran etexilate
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
DV24K10RY
-
-
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
enoxaparin
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
-
heparin
heparin cofactor II
-
hesperetin
-
slight inhibition
hesperidin
-
slight inhibition
hinokiflavone
-
-
Hirudin
-
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
-
inogatran
Intimatan
isohamnetin 3-O-nehesperridin
-
slight inhibition
isorhamnetin
-
-
isorhamnetin 3-O-(6-O-alpha-L-rhamnopyranosyl)-beta-D-glucopyranoside
-
slight inhibition
kaempferol
-
-
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
-
-
lepirudin
-
luteolin
-
-
melagatran
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
myricetin
-
-
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
-
-
naphthalen-2-yl 3-[[(2S)-3-(4-carbamimidoylphenyl)-1-oxo-1-(piperazin-1-yl)propan-2-yl]amino]-3-oxopropane-1-sulfonate
-
-
napsagatran
napsagatran ethyl ester
naringenin
-
slight inhibition
naringin
-
slight inhibition
nexin-1
-
potent endogenous thrombin inhibitor
-
Paraoxon
-
-
Phe-Pro-Arg-chloromethyl ketone
propan-2-yl N-(naphthalen-2-ylsulfonyl)glycyl-3-carbamimidoyl-D-phenylalaninate
-
-
Protease nexin-1
-
-
-
puerarin
-
slight inhibition
quercetin
-
-
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
warfarin
-
-
ximelagatran
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
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
analysis of temperature dependence of pseudo-first order rate constants for enzyme-catalyzed hydrolysis of prothrombin-derived substrates, in presence and absence of Ca2+
D-glucose
-
high glucose enhances thrombin responses through transcriptional upregulation of protease-activated receptor-4, PAR-4, mediated via PKC-beta, -delta, and NFkappaB, in human vascular smooth muscle cells
factor Xa
-
gamma' peptide
-
extensive interactions between thrombin and the gamma' peptide mediated by electrostatic contacts with residues of exosite II and hydrophobic interactions with a pocket in close proximity to the Na+ binding site, complex structure and binding mode, the gamma' peptide completely overlaps with heparin bound to exosite II, overview
-
glycerol
-
increases deacylation rate with p-nitrophenyl-p'-guanidinobenzoate
heparin
-
extensive interactions between thrombin and the gamma' peptide mediated by electrostatic contacts with residues of exosite II and hydrophobic interactions with a pocket in close proximity to the Na+ binding site, complex structure and binding mode, the gamma' peptide completely overlaps with heparin bound to exosite II, overview
lung thromboplastin activator
-
the activation of bovine prothrombin occurs by bovine lung thromboplastin activator
-
Polyphosphate
-
PolyP, secreted by activated platelets, a highly anionic polymer, polyphosphate plus beta-thrombin accelerates plasma clotting and enhances thrombin generation, kinetics, overview. Thrombin binds with high affinity to immobilized polyphosphate. Polyphosphate accelerates factor XI autoactivation and factor XIa autolysis
protease-activated receptor 3
-
the cleaved form of protease-activated receptor 3, PAR-3, acts as a cofactor for thrombin cleavage and activation of PAR-4 on murine platelets, interaction analysis of thrombin with the extracellular part of PAR-3, overview
-
vitamin K
-
dependent on
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.181
Ac-Gly-Gly-Val-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25C
0.102
Ac-Leu-Gly-Val-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25C
0.067
Ac-Nle-Thr-Leu-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25C
0.011
Ac-Nle-Thr-Pro-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25C
0.03
Ac-Val-Thr-Pro-Arg-7-amido-4-methylcoumarin
-
pH 8.0, 25C
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-p-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, 25C
0.298
factor XIII
-
pH 7.4, 25C, wild-type enzyme
-
0.315
factor XIII V34L mutant
-
pH 7.4, 25C, 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, 25C
0.386
GVVPRGVNL
-
pH 7.4, 25C
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, 25C
0.644
TVELQGVVPRGVNL
-
pH 7.4, 25C
additional information
additional information
-