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Information on EC 3.4.21.5 - thrombin and Organism(s) Homo sapiens and UniProt Accession P00734

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.5 thrombin
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P00734 not found.
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Word Map
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
hide
selective cleavage of Arg-/-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B
Synonyms
thrombin, alpha-thrombin, factor iia, fibrinogenase, beta-thrombin, activated factor ii, alphath, thrombin-c, thrombase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-thrombin
-
activated factor II
-
-
beta-thrombin
-
-
blood-coagulation factor II, activated
-
-
-
-
blood-coagulation factor IIa
-
-
-
-
clotting factor IIa
-
-
factor IIa
fibrinogenase
thrombase
-
-
-
-
thrombin, E
-
-
-
-
thrombin-C
-
-
-
-
thrombofort
-
-
-
-
topical
-
-
-
-
tropostasin
-
-
-
-
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
CAS REGISTRY NUMBER
COMMENTARY hide
9002-04-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
coagulation factor V + H2O
?
show the reaction diagram
-
-
-
?
coagulation factor VIII + H2O
?
show the reaction diagram
-
-
-
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
show the reaction diagram
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
show the reaction diagram
fibrinopeptide A + H2O
?
show the reaction diagram
-
-
?
PAR1 peptide + H2O
?
show the reaction diagram
protease-activated receptor I peptide fragment, amino acid sequence
-
?
protease-activated receptor 3 residues 44-56 + H2O
?
show the reaction diagram
-
-
-
?
protein C
?
show the reaction diagram
-
-
-
?
protein C + H2O
?
show the reaction diagram
-
-
?
protein G + H2O
?
show the reaction diagram
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
-
-
?
S-2238 + H2O
?
show the reaction diagram
-
-
-
?
S-2366 + H2O
?
show the reaction diagram
-
-
-
?
S-2765 + H2O
?
show the reaction diagram
-
-
-
?
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
-
-
-
-
?
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-nitroaniline
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-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
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
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
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
-
proteolytic activation
-
?
factor XI + H2O
?
show the reaction diagram
-
-
-
?
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 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
-
proteolytic activation
-
?
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 + 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 Aalpha chain + 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
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-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
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
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 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
?
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
-
-
-
-
?
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 ethyl ester + H2O
tosyl-Arg + ethanol
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
-
-
-
?
UpA + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
show the reaction diagram
-
-
-
?
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
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
factor VIIIa + propeptide
show the reaction diagram
-
proteolytic activation
-
?
factor X + H2O
factor Xa + propeptide
show the reaction diagram
-
proteolytic 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 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 + 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 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
-
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
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
?
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
Rb+
-
activates, can partially substitute for Na+, binding to Asp189
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-amidinophenylpyruvate
-
antithrombin
wild-type and mutant DELTAK9, the mutant shows 20fold lower susceptibility than the wild-type
-
benzamidine
-
Bovine pancreatic trypsin inhibitor
-
-
D-Phe-L-Pro-L-Arg-chloromethylketone
-
D-Phe-Pro-Arg-chloromethylketone
-
heparin
from porcine intestinal mucosa, about 16.5 kDa
N-alpha-(2-naphthylsulfonyl-glycyl)-4-amidinophenylalanine-piperidine
i.e. alpha-NAPAP
Nalpha-dansyl-(p-guanidino)-L-phenylalanine piperidide
-
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
(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-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
aeruginosin 298-A
-
isolated from Microcystis aeruginosa strain NIES-298
-
aeruginosin 98-B
-
isolated from Microcystis aeruginosa strain NIES-98
-
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
-
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 695–699 from the C-terminus of the heavy chain of factor Va inhibits prothrombin activation by prothrombinase in a competitive manner with respect to substrate, mechanism, overview
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
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
butyl 4-carbamimidoyl-N-(naphthalen-2-ylsulfonyl)phenylalaninate
-
-
Ca2+
-
slight inhibition at 10 mM
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-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
-
-
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
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
-
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%
-
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
-
heparin
heparin cofactor II
-
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
-
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
-
heparin cofactor II agonist, inhibitory effect on fluid-phase and surface-bound thrombin in vivo in rabbits and in vitro
L-Phe-L-Pro-L-Arg-chloromethylketone
-
-
lepirudin
-
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
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-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
-
binding mode to the enzyme, crystal structure
nexin-1
-
potent endogenous thrombin inhibitor
-
paraoxon
-
-
Phe-Pro-Arg-chloromethyl ketone
propan-2-yl N-(naphthalen-2-ylsulfonyl)glycyl-3-carbamimidoyl-D-phenylalaninate
-
-
RA-1008
-
a synthetic, low-molecular cyanopeptide-analogue inhibitor, binding structure and inhibition mechanism, overview
RA-1014
-
a synthetic, low-molecular cyanopeptide-analogue inhibitor, binding structure and inhibition mechanism, overview
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
-
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-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(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
-
-
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
ximelagatran
-
prodrug of melagatran
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
Na+
-
increase in ratio kcat/KM from 0.0018 per mM and s in absence of Na+ to 0.125 per mM and s in presence of saturating concentration of Na+
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
vitamin K
-
dependent on
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0051 - 0.013
Fibrinopeptide A
0.0084 - 0.028
PAR1 peptide
0.435 - 0.464
S-2366
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
0.0015 - 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
-
0.0355 - 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 - 0.0152
tosyl-Arg methyl ester
0.0085 - 0.0164
tosyl-Gly-Pro-Arg-4-nitroanilide
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.82 - 45.3
Fibrinopeptide A
4.2 - 146
PAR1 peptide
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
-
-
2.53 - 7.88
fibrinogen
-
4.53 - 57
fibrinogen Aalpha chain
-
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
-
0.065 - 0.65
protein C
-
15 - 91
spectrozyme-TH
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
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+
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8800 - 51000
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide
900 - 1900
di-L-Glu-L-Pro-L-Arg-4-nitroanilide
1000
Fc-[RFSRPQL]-PEG
-
-
3 - 7.43
fibrinogen
-
3 - 7.43
protease-activated receptor 1
-
3 - 7.43
Protein kinase C
-
14300 - 22700
tosyl-Gly-Pro-Arg-4-nitroanilide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00062
4-amidinophenylpyruvate
-
0.0003
benzamidine
-
0.00000066 - 0.0000021
N-alpha-(2-naphthylsulfonyl-glycyl)-4-amidinophenylalanine-piperidine
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
-
-
0.1
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
0.0000045
dabigatran
-
-
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
0.000023
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
-
-
0.00001
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
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.089
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
0.0000726 - 0.000102
hirulog-1
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
0.307
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
-
-
0.00000825 - 0.0000104
variegin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
7.5
-
assay at
7.8
-
assay at
8.6
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
15 - 25
-
assay at
22
-
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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
Manually annotated by BRENDA team
-
sections from Alzheimer's disease brains show reactivity to thrombin antibody in blood vessel walls but not in vessels from controls
Manually annotated by BRENDA team
-
brain endothelial cells can synthesize thrombin and thus be a source of this neurotoxin in Alzheimer's disease brains
Manually annotated by BRENDA team
-
high levels of thrombin are detected in cerebrospinal fluid obtained from Alzheimer's disease but not control patients
Manually annotated by BRENDA team
-
vascular, cell surface
Manually annotated by BRENDA team
-
both thrombin and thrombin receptor agonist peptide enhance the permeability barrier of 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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
human capsular bag model
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
thrombin is highly expressed in microvessels from Alzheimer's disease brains but is not detectable in control vessels
Manually annotated by BRENDA team
-
a metastatic melanoma cell line
Manually annotated by BRENDA team
-
a metastatic melanoma cell line
Manually annotated by BRENDA team
additional information
-
craniocerebral trauma patients present a state of hypercoagulability at early stage and thrombin content is very high level at the site of injury
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
malfunction
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
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
THRB_HUMAN
622
0
70037
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31500 - 40600
-
thrombin in 0.21 M NaCl, 0.02 M sodium phosphate, pH 7.2, equilibrium sedimentation
32000
33500
-
x * 33500, high-speed equilibrium sedimentation in guanidine
36000
-
gel filtration
36500
36600
-
equilibrium sedimentation
37000
70000
-
1 * 70000 + 1 * 32000, SDS-PAGE
72000
-
x * 72000, enzyme mutant, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
activation of recombinant wild-type and mutant DELTAK9 prothrombins by Taipan snake venom treatment
proteolytic modification
side-chain modification
additional information
-
Staphylococcus aureus staphylocoagluase activates proenzyme without proteolysis. Staphylocoagulase-enzyme complex forms a dimer that binds substrate fibrinogen with dissociation constant of 8-34 nM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
bound to a heparin fragment of eight monosaccharide units in length
crystal structures of thrombin in complex with chemically modified thrombin DNA aptamers
mutant E217K, shows repositioned E192 and destructed oxyanion hole
mutant W215A/E217A, free and in complex with inhibitor D-Phe-Pro-Arg-chloromethylketone
Na+-free form, Na+-binding site is in a highly ordered position slightly removed from that seen in the Na+-bound state
thrombin-suramin complex refined at 2.4 A resolution,. hanging drop vapor diffusion method, using 400 mM NaCl, 20 mM MES pH 6.0, 25% (v/v) tert-butanol, 100 mM Tris pH 8.5
8 mg/ml purified enzyme in complex with factor XIII(28-37) peptide as a chloromethylketone derivative, hanging drop vapor diffusion method, room temperature, 24% PEG 8000, 200 mM sodium chloride, 50 mM sodium citrate, pH 5.5, 2 weeks for full size crystals, X-ray diffraction structure determination and analysis at 1.6 A
-
about 6 mg/ml alpha-thrombin in ternary complex with hirugen and inhibitor RWJ-51438, in 50 mM phosphate buffer, pH 7.3, room temperature, hanging drop method, equal volume of 0.003 mL of protein complex and reservoir solution, the latter containing 0.1 M sodium cacodylate, pH 6.5, 0.75 M sodium acetate, 0.01% w/v sodium azide, 20% w/v PEG 4000, equilibration against 1 ml reservoir solution, 5 days, X-ray diffraction structure determination and analysis at 1.7 A resolution with 25% glycerol as cryoprotectant
-
alpha-thrombin complexed with synthetic variegin, hanging drop vapor diffusion method, 0.001 ml of protein solution, containing 20 mg/ml protein, 3 mg/ml variegin inhibitor, 50 mM HEPES, pH 7.5, and 375 mM NaCl, is mixed with 0.001 ml of precipitant solution, containing 100 mM HEPES, pH 7.4, and 20-25% PEG 8000, and equilibrated against 1 ml of the precipitant solution, 4°C, X-ray diffraction structure determination and analysis at 2.4 A resolution, modeling
-
alpha-thrombin is crystallized at 4°C in a complex with sulfated hirudin 53-65, sitting drop vapor diffusion method
-
crystal growth of enzyme complexed with acyl (alpha-aminoalkyl)phosphonate inhibitor within 1 week, formation of 2 different complexes, pentacoordinated complex I and tetracoordinated complex II, X-ray diffraction structure determination and analysis at 1.4-1.75 A
-
crystal structure of thrombin complexed to a novel series of synthetic inhibitors containing a 5,5'-trans-lactone template
-
crystallographic studies of thrombin with Ac-D-Phe-Pro-boroArg-OH and its Lys, amidine, homolysine, and Orn analogs
-
D120N mutant thrombin slow enzyme form in a self-inhibited conformation, X-ray diffraction structure determination and analysis at 1.87 A resolution
-
enzyme complexed with hirugen, 5.5 mg/ml in 24-30% PEG 4000, 0.1 M sodium phosphate, pH 7.3, 20°C, vapour diffusion method, single crystals are soaked overnight in 30% PEG 4000, 0.1 M sodium phosphate, pH 7.3, and 0.5 mg/ml inhibitor, X-ray diffraction structure determination and analysis
-
free enzyme mutant R77aA in presence of K+, two molecules in the asymmetric unit, one with the cation site bound to K+ and the other with the site free, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
gamma thrombin
-
hanging drop vapor diffusion method, using 100 mM MES, 30% (w/v) polyethylene glycol 400, pH 6.5
-
hanging drop vapor diffusion method, using 28% (w/v) PEG 8000 and 100 mM sodium phosphate buffer (pH 7.5)
-
mutant D221A/D222K bound with a fragment of hirudin, slight collapse of the 186 and 220 loops into the Na+ bindung site. Crucial role of D221/D187 ion pair in stabilizing the “fast” form of enzyme
-
mutant enzyme N143P is crystallized by the hanging drop vapor diffusion method, using 0.2 M NaNO3 and 20% (w/v) PEG3350
-
prethrombin 2 bound to a fully active fragment of residues 1-325 from Staphylococcus aureus staphylocoagluase. Complex forms dimers
-
purified alpha-thrombin complexed with a modified 15-mer thrombin-binding aptamer, sitting drop vapour diffusion method, 8 mg/ml protein in 50 mM potassium phosphate, pH 7.1, and 0.1 M KCl, is mixed in a 1:1 ratio of 0.001 ml each with crystallization solution, containing 20% v/v PEG 20 000, 0.2 M ammonium sulfate, 3% v/v n-propanol, 100 mM sodium acetate, pH 5.8, 20°C, a few days, X-ray diffraction structure determination and analysis at 2.15 A resolution
-
purified hirudin-alpha-thrombin in complex with inhibitors RA-1008, RA-1014, aeruginosin 98-B, and aeruginosin 298-A, hanging-drop vapour diffusion method, the protein solution contains 4-5 mg/ml protein, 50 mg/ml hirudin, and 2-3 mM inhibitor and is mixed with reservoir solution containing 22-27% polyethylene glycol 8000 and 0.1 M sodium phosphate buffer, pH 7.5, a few days to microcrystals, macroseeding to obtain laregr crystals, X-ray diffraction structure determination and analysis at 1.85 A resolution, modeling
-
thrombin in complex with fibrinogen gamma' peptide, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
thrombin in complex with hirudin, hanging drop vapor diffusion method, using 0.05 M sodium phosphate buffer pH 7.3, 28% (w/v) PEG8000
-
thrombin mutant S195A in complex with a 30-residue long uncleaved extracellular fragment of protease-activated receptor 1, hanging drop vapor diffusion method, using 0.2 M potassium/sodium tartrate, 20%,(w/v) PEG 3350, at 22°C
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
W215A/E217A
drastically impaired catalytic activity, but able to efficiently activate protein C in presence of thrombomodulin
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
D189A
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
E217A
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
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
I174A
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
R77aA
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
S195A
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
W215A/E217A
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
W215P
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
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10.3
-
rapid loss of clotting and esterase activity below pH 5 and above pH 10.3
95528
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
-
stable for up to 3 days at room temperature
35
-
pH 6, loss of activity above
80
-
lyophilized enzyme, 8 h, 90% remaining activity
additional information
-
with increasing salt concentrations, the thermal stability of the enzyme activity is improved by group Ia clorides in decreasing order: Na+, K+, Rb+, Cs+. For ionic strength below 3 M the stability is reduced by group IIa chlorides in increasoing order: Mg2+, Sr2+, Ba2+, Ca2+. If the ionic strenght is about 3 M, the stability changes only slightly in LiCl or NaNO3
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
autolytic degradation during sedimentation in neutral salt solution
-
autolytic degradation of alpha-thrombin to nonclotting beta-thrombins and gamma-thrombins is retarded by increasing concentrations of Li+, Cs+, K+, Rb+ chlorides
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-50°C, 0.75 M NaCl, pH 6, stable for about 1 year
-
-70°C, stable for at least six months
-
4°C, 0.75 M NaCl, pH 6, stable for about 1 week
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzyme from CHO cells
dysprothrombin Perija
-
large-scale preparation from human plasma. Isolation of prothrombin is followed by activation to thrombin and further purification
-
native enzyme from plasma
-
recombinant enzyme mutants from BHK cells by anion and cation exchange chromatography to homogeneity
-
recombinant protein
-
recombinant wild-type and mutant enzymes to homogeneity
-
recombinant wild-type enzyme and mutants from baby hamster kidney cells. Recombinant enzyme mutants W215M and W215T, and wild-type enzyme from Escherichia coli including unfolding and refolding of the pelleted enzymes, dialysis, heparin affinity hcromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in CHO cells
DNA sequence determination of the natural mutant gene
-
engineering of a prothrombin cDNA coding for a secreted form of prethrombin-2, production in a mammalian expression system using DXB11 cells, a mutant strain of CHO cells in which the dihydrofolate reductase gene has been deleted and an expression vector carrying the dihydrofolate reductase cDNA
-
expressed in Mus musculus
-
expression of enzyme mutants in BHK cells
-
expression of wild-type and mutant enzymes in baby hamster kidney cells
-
expression of wild-type and mutant enzymes in EA.hy926 cells, co-expression with activated protein C
-
recombinant expression of wild-type and mutant enzymes in baby hamster kidney cells, only mutants W215M and W215T, and also the wild-type enzyme are expressed in Escherichia coli strain BL21(DE3)
-
wild type and mutant enzymes are expressed as prethrombin-2 zymogens in baby hamster kidney cells using the pNUT-PL2 expression/purification vector system
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
binding of immunoglobulin G to the Fc receptors of the thrombocytes is paralleled by increased synthesis of thrombin
-
enhancement of thrombin-stimulated migration and gene expression by high glucose, which can be abolished by endogenous protease-activated receptor-4, PAR-4, knockdown
-
oxidative stress or cell signaling perturbations lead to increased expression of thrombin mRNA in brain endothelial cells
-
sucrose octasulfate suppresses ex vivo thrombin generation in human plasma both in an heparin cofactor II-dependent and -independent process, the latter possibly involving inhibition of prothrombin activation
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
denaturation by urea, 60% reversible at pH 8.0, completely reversible at pH 6.5. Na+-bound form of enzyme is more stable to urea denaturation than Na+-free form by 2 kcal/mol
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
analysis
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
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lundblad, R.L.; Kingdon, H.S.; Mann, K.G.
Thrombin
Methods Enzymol.
45
156-176
1976
Bos taurus, Equus caballus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Landis, B.H.; Koehler, K.A.; Fenton II, J.W.
Human thrombins. Group IA and IIA salt-dependent properties of alpha-thrombin
J. Biol. Chem.
256
4604-4610
1981
Homo sapiens
Manually annotated by BRENDA team
Fenton, J.W.; Fasco, M.J.; Stackrow, A.B.; Aronson, D.L.; Young, A.M.; Finlayson, J.S
Human thrombins. Production, evaluation, and properties of alpha-thrombin
J. Biol. Chem.
252
3587-3598
1977
Homo sapiens
Manually annotated by BRENDA team
Lanchantin, G.F.; Friedmann, J.A.; Hart, D.W.
Two forms of human thrombin. Isolation and characterization
J. Biol. Chem.
248
5956-5966
1973
Homo sapiens
Manually annotated by BRENDA team
Bezaud, A.; Guillin, M.C.
Enzymic and nonenzymic properties of human beta-thrombin
J. Biol. Chem.
263
3576-3581
1988
Homo sapiens
Manually annotated by BRENDA team
Thompson, A.R.; Enfield, D.L.; Ericsson, L.H.; Legaz, M.E.; Fenton II, J.W.
Human thrombin: partial primary structure
Arch. Biochem. Biophys.
178
356-367
1977
Homo sapiens
Manually annotated by BRENDA team
Fasco, M.J.; Fenton II, J.W.
Specificity of thrombin. I. Esterolytic properties of thrombin, plasma, trypsin, and chymotrypsin with Nbeta-substituted guanidino derivatives of p-nitrophenyl-p'-guanidinobenzoate
Arch. Biochem. Biophys.
159
802-812
1973
Homo sapiens
-
Manually annotated by BRENDA team
Mazzucato, M.; de Marco, L.; Masotti, A.; Pradella, P.; Bahou, W.F.; Ruggeri, Z.M.
Characterization of the initial alpha-thrombin interaction with glycoprotein Ibaalpha in relation to platelet activation
J. Biol. Chem.
273
1880-1887
1998
Homo sapiens
Manually annotated by BRENDA team
Jhoti, H.; Cleasby, A.; Reid, S.; Thomas, P.J.; Weir, M.; Wonacott, A.
Crystal structures of thombin complexed to a novel series of synthetic inhibitors containing a 5,5-trans lactone template
Biochemistry
38
7969-7977
1999
Homo sapiens
Manually annotated by BRENDA team
Brass, L.F.; Woolkalis, M.J.
Dual regulation of cyclic AMP formation by thrombin in HEL cells, a leukaemic cell line with megakaryocytic properties
Biochem. J.
281
73-80
1992
Homo sapiens
Manually annotated by BRENDA team
Gibbs, C.S.; Coutre, S.E.; Tsiang, M.; Li, W.X.; Jain, A.K.; Dunn, K.E.; Law, V.S.; Mao, C.T.; Matsumura, S.Y.; Mejza, S.J.; Paborsky, L.R.; Leung, L.L.K.
Conversion of thrombin into an anticoagulant by protein engineering
Nature
378
413-416
1995
Homo sapiens
Manually annotated by BRENDA team
Weber, P.C.; Lee, S.L.; Lewandowski, F.A.; Schadt, M.C.; Chang, C.H.; Kettner, C.A.
Kinetic and crystallographic studies of thrombin with Ac-(D)Phe-Pro-boroArg-OH and its lysine, amidine, homolysine, and ornithine analogs
Biochemistry
34
3750-3757
1995
Homo sapiens
Manually annotated by BRENDA team
Tsiang, M.; Paborsky, L.R.; Li, W.X.; Jain, A.K.; Mao, C.T.; Dunn, K.E.; Lee, D.W.; Matsumura, S.Y.; Matteucci, M.D.; Coutre, S.E.; Leung, L.L.K.; Gibbs, C.S.
Protein engineering thrombin for optimal specificity and potency of anticoagulant activity in vivo
Biochemistry
35
16449-16457
1996
Homo sapiens
Manually annotated by BRENDA team
Naski, M.C.; Lorand, L.; Shafer, J.A.
Characterization of the kinetic pathway for fibrin promotion of alpha-thrombin-catalyzed activation of plasma factor XIII
Biochemistry
30
934-941
1991
Homo sapiens
Manually annotated by BRENDA team
Rydel, T.J.; Yin, M.; Padmanabhan, K.P.; Blankenship, D.T.; Cardin, A.D.; Correa, P.E.; Fenton 2nd, J.W.; Tulinsky, A.
Crystallographic structure of human gamma-thrombin
J. Biol. Chem.
269
22000-22006
1994
Homo sapiens
Manually annotated by BRENDA team
Engh, R.A.; Brandstetter, H.; Sucher, G.; Eichinger, A.; Baumann, U.; Bode, W.; Huber, R.; Poll, T.; Rudolph, R.; von der Saal, W.
Enzyme flexibility, solvent and weak' interactions characterize thrombin-ligand interactions: implications for drug design
Structure
4
1353-1362
1996
Homo sapiens
Manually annotated by BRENDA team
Russo, G.; Gast, A.; Schlaeger, E.J.; Angiolillo, A.; Pietropaolo, C.
Stable expression and purification of a secreted human recombinant prethrombin-2 and its activation to thrombin
Protein Expr. Purif.
10
214-225
1997
Homo sapiens
Manually annotated by BRENDA team
Recacha, R.; Costanzo, M.J.; Maryanoff, B.E.; Carson, M.; DeLucas, L.; Chattopadhyay, D.
Structure of human alpha-thrombin complexed with RWJ-51438 at 1.7 A: unusual perturbation of the 60A-60I insertion loop
Acta Crystallogr. Sect. D
56
1395-1400
2000
Homo sapiens
-
Manually annotated by BRENDA team
Deinum, J.; Gustavsson, L.; Gyzander, E.; Kullman-Magnusson, M.; Edstroem, A.; Karlsson, R.
A thermodynamic characterization of the binding of thrombin inhibitors to human thrombin, combining biosensor technology, stopped-Flow spectrophotometry, and microcalorimetry
Anal. Biochem.
300
152-162
2002
Homo sapiens
Manually annotated by BRENDA team
De Cristofaro, R.; De Filippis, V.
Interaction of the 268-282 region of glycoprotein Ibalpha with the heparin-binding site of thrombin inhibits the enzyme activation of factor VIII
Biochem. J.
373
593-601
2003
Homo sapiens
Manually annotated by BRENDA team
Hayakawa, Y.; Hayashi, T.; Lee, J.; Srisomporn, P.; Maeda, M.; Ozawa, T.; Sakuragawa, N.
Inhibition of thrombin by sulfated polysaccharides isolated from green algae
Biochim. Biophys. Acta
1543
86-94
2000
Homo sapiens
Manually annotated by BRENDA team
Myles, T.; Yun, T.H.; Leung, L.L.
Structural requirements for the activation of human factor VIII by thrombin
Blood
100
2820-2826
2002
Homo sapiens
Manually annotated by BRENDA team
Lange, U.; Keilholz, W.; Schaub, G.A.; Landmann, H.; Markwardt, F.; Nowak, G.
Biochemical characterization of a thrombin inhibitor from the bloodsucking bug Dipetalogaster maximus
Haemostasis
29
204-211
2000
Homo sapiens
Manually annotated by BRENDA team
Chambers, R.C.; Leoni, P.; Blanc-Brude, O.P.; Wembridge, D.E.; Laurent, G.J.
Thrombin is a potent inducer of connective tissue growth factor production via proteolytic activation of protease-activated receptor-1
J. Biol. Chem.
275
35584-35591
2000
Homo sapiens
Manually annotated by BRENDA team
Sadasivan, C.; Yee, V.C.
Interaction of the factor XIII activation peptide with alpha-thrombin. Crystal structure of its enzyme-substrate analog complex
J. Biol. Chem.
275
36942-36948
2000
Homo sapiens
Manually annotated by BRENDA team
Prasad, S.; Cantwell, A.M.; Bush, L.A.; Shih, P.; Xu, H.; Di Cera, E.
Residue Asp-189 controls both substrate binding and the monovalent cation specificity of thrombin
J. Biol. Chem.
279
10103-10108
2004
Homo sapiens
Manually annotated by BRENDA team
De Cristofaro, R.; Akhavan, S.; Altomare, C.; Carotti, A.; Peyvandi, F.; Mannucci, P.M.
A natural prothrombin mutant reveals an unexpected influence of A-chain structure on the activity of human alpha-thrombin
J. Biol. Chem.
279
13035-13043
2004
Homo sapiens (P00734), Homo sapiens
Manually annotated by BRENDA team
Lopez, M.; Mende, K.; Steinmetzer, T.; Nowak, G.
Cloning, purification and biochemical characterization of dipetarudin, a new chimeric thrombin inhibitor
J. Chromatogr. B
786
73-80
2003
Homo sapiens
Manually annotated by BRENDA team
Guimaraes, C.R.W.; Bicca de Alencastro, R.
Thrombin inhibition by novel benzamidine derivatives: a free-energy perturbation study
J. Med. Chem.
45
4995-5004
2002
Homo sapiens (P00734)
Manually annotated by BRENDA team
Skordalakes, E.; Dodson, G.G.; Green, D.S.; Goodwin, C.A.; Scully, M.F.; Hudson, H.R.; Kakkar, V.V.; Deadman, J.J.
Inhibition of human alpha-thrombin by a phosphonate tripeptide proceeds via a metastable pentacoordinated phosphorus intermediate
J. Mol. Biol.
311
549-555
2001
Homo sapiens
Manually annotated by BRENDA team
Dullweber, F.; Stubbs, M.T.; Musil, D.; Sturzebecher, J.; Klebe, G.
Factorising ligand affinity: a combined thermodynamic and crystallographic study of trypsin and thrombin inhibition
J. Mol. Biol.
313
593-614
2001
Homo sapiens, Bos taurus (P00735)
Manually annotated by BRENDA team
De Cristofaro, R.; De Candia, E.
Thrombin domains: structure, function and interaction with platelet receptors
J. Thromb. Thrombolysis
15
151-163
2003
Homo sapiens
Manually annotated by BRENDA team
Backes, B.J.; Harris, J.L.; Leonetti, F.; Craik, C.S.; Ellman, J.A.
Synthesis of positional-scanning libraries of fluorogenic peptide substrates to define the extended substrate specificity of plasmin and thrombin
Nat. Biotechnol.
18
187-193
2000
Homo sapiens
Manually annotated by BRENDA team
Meh, D.A.; Siebenlist, K.R.; Brennan, S.O.; Holyst, T.; Mosesson, M.W.
The amino acid sequence in fibrin responsible for high affinity thrombin binding
Thromb. Haemost.
85
470-474
2001
Homo sapiens
Manually annotated by BRENDA team
Buchanan, M.R.; Maclean, G.A.; Brister, S.J.
Selective and sustained inhibition of surface-bound thrombin activity by intimatan/heparin cofactor II and its relevance to assessing systemic anticoagulation in vivo, ex vivo and in vitro
Thromb. Haemost.
86
909-913
2001
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Sekine, O.; Sugo, T.; Ebisawa, K.; Umeyama, H.; Iwahana, H.; Ruiz-Saez, A.; de Bosch, N.; Matsudai, M.
Substitution of Gly-548 to Ala in the substrate binding pocket of prothrombin Perija leads to the loss of thrombin proteolytic activity
Thromb. Haemost.
87
282-287
2002
Homo sapiens
Manually annotated by BRENDA team
de Bosch, N.B.; Mosesson, M.W.; Ruiz-Saez, A.; Echenagucia, M.; Rodriguez-Lemoin, A.
Inhibition of thrombin generation in plasma by fibrin formation (antithrombin I)
Thromb. Haemost.
88
253-258
2002
Homo sapiens
Manually annotated by BRENDA team
Maekawa, H.; Sato, H.; Tollefsen, D.M.
Thrombin inhibition by HCII in the presence of elastase-cleaved HCII and thrombin-HCII complex
Thromb. Res.
100
443-451
2000
Homo sapiens
Manually annotated by BRENDA team
Mourao, P.A.; Boisson-Vidal, C.; Tapon-Bretaudiere, J.; Drouet, B.; Bros, A.; Fischer, A.
Inactivation of thrombin by a fucosylated chondroitin sulfate from echinoderm
Thromb. Res.
102
167-176
2001
Homo sapiens
Manually annotated by BRENDA team
Michaud, S.E.; Wang, L.Z.; Korde, N.; Bucki, R.; Randhawa, P.K.; Pastore, J.J.; Falet, H.; Hoffmeister, K.; Kuuse, R.; Uibo, R.; Herod, J.; Sawyer, E.; Janmey, P.A.
Purification of salmon thrombin and its potential as an alternative to mammalian thrombins in fibrin sealants
Thromb. Res.
107
245-254
2002
Homo sapiens, Salmo salar
Manually annotated by BRENDA team
Weitz, J.I.
A novel approach to thrombin inhibition
Thromb. Res.
109 Suppl 1
S17-22
2003
Homo sapiens
Manually annotated by BRENDA team
De Filippis, V.; De Dea, E.; Lucatello, F.; Frasson, R.
Effect of Na+ binding on the conformation, stability and molecular recognition properties of thrombin
Biochem. J.
390
485-492
2005
Homo sapiens (P00734)
Manually annotated by BRENDA team
Johnson, D.J.; Adams, T.E.; Li, W.; Huntington, J.A.
Crystal structure of wild-type human thrombin in the Na+-free state
Biochem. J.
392
21-28
2005
Homo sapiens (P00734), Homo sapiens
Manually annotated by BRENDA team
Croy, C.H.; Koeppe, J.R.; Bergqvist, S.; Komives, E.A.
Allosteric changes in solvent accessibility observed in thrombin upon active site occupation
Biochemistry
43
5246-5255
2004
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Shi, F.; Winzor, D.J.; Jackson, C.M.
Temperature dependence of the thrombin-catalyzed proteolysis of prothrombin
Biophys. Chem.
110
1-13
2004
Homo sapiens
Manually annotated by BRENDA team
Pineda, A.O.; Zhang, E.; Guinto, E.R.; Savvides, S.N.; Tulinsky, A.; Di Cera, E.
Crystal structure of the thrombin mutant D221A/D222K: the Asp222:Arg187 ion-pair stabilizes the fast form
Biophys. Chem.
112
253-256
2004
Homo sapiens
Manually annotated by BRENDA team
Scheffler, J.E.; Berliner, L.J.
Aspartame and aspartame derivatives effect human thrombin catalytic activity
Biophys. Chem.
112
285-291
2004
Homo sapiens
Manually annotated by BRENDA team
Nogami, K.; Zhou, Q.; Wakabayashi, H.; Fay, P.J.
Thrombin-catalyzed activation of factor VIII with His substituted for Arg372 at the P1 site
Blood
105
4362-4368
2005
Homo sapiens
Manually annotated by BRENDA team
James, C.; Collison, D.J.; Duncan, G.
Characterization and functional activity of thrombin receptors in the human lens
Invest. Ophthalmol. Vis. Sci.
46
925-932
2005
Homo sapiens
Manually annotated by BRENDA team
Zhang, D.; Kovach, I.M.
Full and partial deuterium solvent isotope effect studies of alpha-thrombin-catalyzed reactions of natural substrates
J. Am. Chem. Soc.
127
3760-3766
2005
Homo sapiens
Manually annotated by BRENDA team
Yonemura, H.; Imamura, T.; Soejima, K.; Nakahara, Y.; Morikawa, W.; Ushio, Y.; Kamachi, Y.; Nakatake, H.; Sugawara, K.; Nakagaki, T.; Nozaki, C.
Preparation of recombinant alpha-thrombin: high-level expression of recombinant human prethrombin-2 and its activation by recombinant ecarin
J. Biochem.
135
577-582
2004
Homo sapiens
Manually annotated by BRENDA team
Carter, W.J.; Myles, T.; Gibbs, C.S.; Leung, L.L.; Huntington, J.A.
Crystal structure of anticoagulant thrombin variant E217K provides insights into thrombin allostery
J. Biol. Chem.
279
26387-26394
2004
Homo sapiens (P00734), Homo sapiens
Manually annotated by BRENDA team
Pineda, A.O.; Chen, Z.W.; Caccia, S.; Cantwell, A.M.; Savvides, S.N.; Waksman, G.; Mathews, F.S.; Di Cera, E.
The anticoagulant thrombin mutant W215A/E217A has a collapsed primary specificity pocket
J. Biol. Chem.
279
39824-39828
2004
Homo sapiens (P00734)
Manually annotated by BRENDA team
Nogami, K.; Zhou, Q.; Myles, T.; Leung, L.L.; Wakabayashi, H.; Fay, P.J.
Exosite-interactive regions in the A1 and A2 domains of factor VIII facilitate thrombin-catalyzed cleavage of heavy chain
J. Biol. Chem.
280
18476-18487
2005
Homo sapiens
Manually annotated by BRENDA team
Carter, W.J.; Cama, E.; Huntington, J.A.
Crystal structure of thrombin bound to heparin
J. Biol. Chem.
280
2745-2749
2005
Homo sapiens (P00734), Homo sapiens
Manually annotated by BRENDA team
Panizzi, P.; Friedrich, R.; Fuentes-Prior, P.; Richter, K.; Bock, P.E.; Bode, W.
Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes
J. Biol. Chem.
281
1179-1187
2006
Homo sapiens
Manually annotated by BRENDA team
Bush, L.A.; Nelson, R.W.; Di Cera, E.
Murine thrombin lacks Na+ activation but retains high catalytic activity
J. Biol. Chem.
281
7183-7188
2006
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Pajdak, W.; Radwan, J.; Guzik, T.J.
Cleavage of prothrombin bound in immune complexes results in high thrombin enzymatic activity
J. Physiol. Pharmacol.
55
477-484
2004
Homo sapiens
Manually annotated by BRENDA team
Hosokawa, K.; Ohnishi, T.; Kawakami, A.; Wakabayashi, S.; Koide, T.
Chemically modified thrombin and anhydrothrombin that differentiate macromolecular substrates of thrombin
J. Thromb. Haemost.
3
2703-2711
2005
Homo sapiens
Manually annotated by BRENDA team
Lam, J.K.; Chion, C.K.; Zanardelli, S.; Lane, D.A.; Crawley, J.T.
Further characterization of ADAMTS-13 inactivation by thrombin
J. Thromb. Haemost.
5
1010-1018
2007
Homo sapiens
Manually annotated by BRENDA team
Sutherland, J.S.; Bhakta, V.; Filion, M.L.; Sheffield, W.P.
The transferable tail: fusion of the N-terminal acidic extension of heparin cofactor II to alpha1-proteinase inhibitor M358R specifically increases the rate of thrombin inhibition
Biochemistry
45
11444-11452
2006
Homo sapiens
Manually annotated by BRENDA team
Isetti, G.; Maurer, M.C.
Employing mutants to study thrombin residues responsible for factor XIII activation peptide recognition: a kinetic study
Biochemistry
46
2444-2452
2007
Homo sapiens
Manually annotated by BRENDA team
Carrell, C.J.; Bush, L.A.; Mathews, F.S.; Di Cera, E.
High resolution crystal structures of free thrombin in the presence of K(+) reveal the molecular basis of monovalent cation selectivity and an inactive slow form
Biophys. Chem.
121
177-184
2006
Homo sapiens
Manually annotated by BRENDA team
Pineda, A.O.; Chen, Z.W.; Marino, F.; Mathews, F.S.; Mosesson, M.W.; Di Cera, E.
Crystal structure of thrombin in complex with fibrinogen gamma peptide
Biophys. Chem.
125
556-559
2007
Homo sapiens
Manually annotated by BRENDA team
Gianni, S.; Ivarsson, Y.; Bah, A.; Bush-Pelc, L.A.; Di Cera, E.
Mechanism of Na+ binding to thrombin resolved by ultra-rapid kinetics
Biophys. Chem.
131
111-114
2007
Homo sapiens
Manually annotated by BRENDA team
Bae, J.S.; Yang, L.; Manithody, C.; Rezaie, A.R.
The ligand occupancy of endothelial protein C receptor switches the protease-activated receptor 1-dependent signaling specificity of thrombin from a permeability-enhancing to a barrier-protective response in endothelial cells
Blood
110
3909-3916
2007
Homo sapiens
Manually annotated by BRENDA team
Stief, T.W.
Specific determination of plasmatic thrombin activity
Clin. Appl. Thromb. Hemost.
12
324-329
2006
Homo sapiens
Manually annotated by BRENDA team
Nishi, N.; Itoh, A.; Shoji, H.; Miyanaka, H.; Nakamura, T.
Galectin-8 and galectin-9 are novel substrates for thrombin
Glycobiology
16
15C-20C
2006
Homo sapiens
Manually annotated by BRENDA team
Pineda, A.O.; Chen, Z.W.; Bah, A.; Garvey, L.C.; Mathews, F.S.; Di Cera, E.
Crystal structure of thrombin in a self-inhibited conformation
J. Biol. Chem.
281
32922-32928
2006
Homo sapiens
Manually annotated by BRENDA team
Bukys, M.A.; Kim, P.Y.; Nesheim, M.E.; Kalafatis, M.
A control switch for prothrombinase: characterization of a hirudin-like pentapeptide from the COOH terminus of factor Va heavy chain that regulates the rate and pathway for prothrombin activation
J. Biol. Chem.
281
39194-39204
2006
Homo sapiens
Manually annotated by BRENDA team
Bah, A.; Garvey, L.C.; Ge, J.; Di Cera, E.
Rapid kinetics of Na+ binding to thrombin
J. Biol. Chem.
281
40049-40056
2006
Homo sapiens
Manually annotated by BRENDA team
Smadja, D.M.; Basire, A.; Amelot, A.; Conte, A.; Bieche, I.; Le Bonniec, B.F.; Aiach, M.; Gaussem, P.
Thrombin bound to a fibrin clot confers angiogenic and hemostatic properties on endothelial progenitor cells
J. Cell. Mol. Med.
12
975-986
2007
Homo sapiens
Manually annotated by BRENDA team
Radau, G.; Fokkens, J.
Design and X-ray crystal structures of human thrombin with synthetic cyanopeptide-analogues
Pharmazie
62
83-88
2007
Homo sapiens
Manually annotated by BRENDA team
Rock, G.; Neurath, D.; Semple, E.; Harvey, M.; Freedman, M.
Preparation and characterization of human thrombin for use in a fibrin glue
Transfus. Med.
17
187-191
2007
Homo sapiens
Manually annotated by BRENDA team
Hu, J.; Zheng, P.C.; Jiang, J.H.; Shen, G.L.; Yu, R.Q.; Liu, G.K.
Electrostatic interaction based approach to thrombin detection by surface-enhanced Raman spectroscopy
Anal. Chem.
81
87-93
2009
Homo sapiens
Manually annotated by BRENDA team
Rahgozar, S.; Giannakopoulos, B.; Yan, X.; Wei, J.; Cheng Qi, J.; Gemmell, R.; Krilis, S.A.
beta2-Glycoprotein I protects thrombin from inhibition by heparin cofactor II: potentiation of this effect in the presence of anti-beta2-glycoprotein I autoantibodies
Arthritis Rheum.
58
1146-1155
2008
Homo sapiens
Manually annotated by BRENDA team
Kang, Y.; Feng, K.J.; Chen, J.W.; Jiang, J.H.; Shen, G.L.; Yu, R.Q.
Electrochemical detection of thrombin by sandwich approach using antibody and aptamer
Bioelectrochemistry
73
76-81
2008
Homo sapiens
Manually annotated by BRENDA team
Chao, J.; Huang, W.Y.; Wang, J.; Xiao, S.J.; Tang, Y.C.; Liu, J.N.
Click-chemistry-conjugated oligo-angiomax in the two-dimensional DNA lattice and its interaction with thrombin
Biomacromolecules
10
877-883
2009
Homo sapiens
Manually annotated by BRENDA team
Hanessian, S.; Simard, D.; Bayrakdarian, M.; Therrien, E.; Nilsson, I.; Fjellstroem, O.
Design, synthesis, and thrombin-inhibitory activity of pyridin-2-ones as P2/P3 core motifs
Bioorg. Med. Chem. Lett.
18
1972-1976
2008
Homo sapiens
Manually annotated by BRENDA team
Centi, S.; Messina, G.; Tombelli, S.; Palchetti, I.; Mascini, M.
Different approaches for the detection of thrombin by an electrochemical aptamer-based assay coupled to magnetic beads
Biosens. Bioelectron.
23
1602-1609
2008
Homo sapiens
Manually annotated by BRENDA team
Hu, L.; Ibrahim, S.; Liu, C.; Skaar, J.; Pagano, M.; Karpatkin, S.
Thrombin induces tumor cell cycle activation and spontaneous growth by down-regulation of p27Kip1, in association with the up-regulation of Skp2 and MiR-222
Cancer Res.
69
3374-3382
2009
Homo sapiens
Manually annotated by BRENDA team
Schellhammer, F.; Steinhaus, D.; Cohnen, M.; Hoppe, J.; Moedder, U.; Fuerst, G.
Minimally invasive therapy of pseudoaneurysms of the trunk: application of thrombin
Cardiovasc. Intervent. Radiol.
31
535-541
2008
Homo sapiens
Manually annotated by BRENDA team
Alexandru, N.; Constantin, A.; Popov, D.
Carbonylation of platelet proteins occurs as consequence of oxidative stress and thrombin activation, and is stimulated by ageing and type 2 diabetes
Clin. Chem. Lab. Med.
46
528-536
2008
Homo sapiens, Mesocricetus auratus, Rattus norvegicus
Manually annotated by BRENDA team
Eichinger, S.; Hron, G.; Kollars, M.; Kyrle, P.A.
Prediction of recurrent venous thromboembolism by endogenous thrombin potential and D-dimer
Clin. Chem.
54
2042-2048
2008
Homo sapiens
Manually annotated by BRENDA team
Okumura, N.; Haneishi, A.; Terasawa, F.
Citrullinated fibrinogen shows defects in FPA and FPB release and fibrin polymerization catalyzed by thrombin
Clin. Chim. Acta
401
119-123
2009
Homo sapiens
Manually annotated by BRENDA team
Doria, C.; Fischer, C.P.; Wood, C.G.; Li, P.M.; Marra, S.; Hart, J.
Phase 3, randomized, double-blind study of plasma-derived human thrombin versus bovine thrombin in achieving hemostasis in patients undergoing surgery
Curr. Med. Res. Opin.
24
785-794
2008
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Cuccioloni, M.; Mozzicafreddo, M.; Sparapani, L.; Spina, M.; Eleuteri, A.M.; Fioretti, E.; Angeletti, M.
Pomegranate fruit components modulate human thrombin
Fitoterapia
80
301-305
2009
Homo sapiens
Manually annotated by BRENDA team
Kashyap, V.S.; Ginsberg, J.S.; Davidson, B.L.; Comp, P.C.; Francis, C.W.; Friedman, R.J.; Huo, M.H.; Lieberman, J.R.; Muntz, J.E.; Raskob, G.E.; Clements, M.L.; Hantel, S.; Schnee, J.M.; Caprini, J.A.
Oral thrombin inhibitor dabigatran etexilate vs North American enoxaparin regimen for prevention of venous thromboembolism after knee arthroplasty surgery
J. Arthroplasty
24
1-9
2009
Homo sapiens
Manually annotated by BRENDA team
Bae, J.S.; Kim, Y.U.; Park, M.K.; Rezaie, A.R.
Concentration dependent dual effect of thrombin in endothelial cells via Par-1 and Pi3 Kinase
J. Cell. Physiol.
219
744-751
2009
Homo sapiens
Manually annotated by BRENDA team
Song, M.; Zhang, Y.; Li, T.; Wang, Z.; Yin, J.; Wang, H.
Highly sensitive detection of human thrombin in serum by affinity capillary electrophoresis/laser-induced fluorescence polarization using aptamers as probes
J. Chromatogr. A
1216
873-878
2009
Homo sapiens
Manually annotated by BRENDA team
Erez, O.; Romero, R.; Kim, S.S.; Kim, J.S.; Kim, Y.M.; Wildman, D.E.; Than, N.G.; Mazaki-Tovi, S.; Gotsch, F.; Pineles, B.; Kusanovic, J.P.; Espinoza, J.; Mittal, P.; Mazor, M.; Hassan, S.S.; Kim, C.J.
Over-expression of the thrombin receptor (PAR-1) in the placenta in preeclampsia: a mechanism for the intersection of coagulation and inflammation
J. Matern. Fetal. Neonatal. Med.
21
345-355
2008
Homo sapiens
Manually annotated by BRENDA team
Ilas, J.; Tomasic, T.; Kikelj, D.
Novel potent and selective thrombin inhibitors based on a central 1,4-benzoxazin-3(4H)-one scaffold
J. Med. Chem.
51
2863-2867
2008
Homo sapiens
Manually annotated by BRENDA team
Lopez, J.J.; Salido, G.M.; Pariente, J.A.; Rosado, J.A.
Thrombin induces activation and translocation of Bid, Bax and Bak to the mitochondria in human platelets
J. Thromb. Haemost.
6
1780-1788
2008
Homo sapiens
Manually annotated by BRENDA team
Mueller, J.; Freitag, D.; Mayer, G.; Poetzsch, B.
Anticoagulant characteristics of HD1-22, a bivalent aptamer that specifically inhibits thrombin and prothrombinase
J. Thromb. Haemost.
6
2105-2112
2008
Homo sapiens
Manually annotated by BRENDA team
Miah, M.F.; Boffa, M.B.
Functional analysis of mutant variants of thrombin-activatable fibrinolysis inhibitor resistant to activation by thrombin or plasmin
J. Thromb. Haemost.
7
665-672
2009
Homo sapiens
Manually annotated by BRENDA team
Curzio, K.M.; Cheng-Lai, A.; Kheyfets, V.; Sinnet, M.; Billett, H.H.
A comparison of direct thrombin inhibitors in the treatment of heparin-induced thrombocytopenia: a single institution experience
J. Thromb. Thrombolysis
28
117-123
2008
Homo sapiens
Manually annotated by BRENDA team
Cho, H.; Baker, B.R.; Wachsmann-Hogiu, S.; Pagba, C.V.; Laurence, T.A.; Lane, S.M.; Lee, L.P.; Tok, J.B.
Aptamer-based SERRS sensor for thrombin detection
Nano Lett.
8
4386-4390
2008
Homo sapiens
Manually annotated by BRENDA team
Fitzgibbon, J.; Morrison, J.J.; Smith, T.J.; OBrien, M.
Modulation of human uterine smooth muscle cell collagen contractility by thrombin, Y-27632, TNF alpha and indomethacin
Reprod. Biol. Endocrinol.
7
2-2
2009
Homo sapiens
Manually annotated by BRENDA team
Bae, J.S.; Rezaie, A.R.
Protease activated receptor 1 (PAR-1) activation by thrombin is protective in human pulmonary artery endothelial cells if endothelial protein C receptor is occupied by its natural ligand
Thromb. Haemost.
100
101-109
2008
Homo sapiens
Manually annotated by BRENDA team
De Smedt, E.; Wagenvoord, R.; Coen Hemker, H.
The technique of measuring thrombin generation with fluorogenic substrates: 3. The effects of sample dilution
Thromb. Haemost.
101
165-170
2009
Homo sapiens
Manually annotated by BRENDA team
Bae, J.S.; Rezaie, A.R.
Thrombin inhibits nuclear factor kappaB and RhoA pathways in cytokine-stimulated vascular endothelial cells when EPCR is occupied by protein C
Thromb. Haemost.
101
513-520
2009
Homo sapiens
Manually annotated by BRENDA team
Huisse, M.G.; Ajzenberg, N.; Feldman, L.; Guillin, M.C.; Steg, P.G.
Microparticle-linked tissue factor activity and increased thrombin activity play a potential role in fibrinolysis failure in ST-segment elevation myocardial infarction
Thromb. Haemost.
101
734-740
2009
Homo sapiens
Manually annotated by BRENDA team
Aizawa, P.; Winge, S.; Karlsson, G.
Large-scale preparation of thrombin from human plasma
Thromb. Res.
122
560-567
2008
Homo sapiens
Manually annotated by BRENDA team
Ben Mansour, M.; Dhahri, M.; Venisse, L.; Jandrot-Perrus, M.; Chaubet, F.; Maaroufi, R.M.
Mechanism of thrombin inhibition by heparin cofactor II and antithrombin in the presence of the ray (Raja radula) skin dermatan sulfate
Thromb. Res.
123
902-908
2009
Homo sapiens
Manually annotated by BRENDA team
Parrales, A.; Palma-Nicolas, J.P.; Lopez, E.; Lopez-Colome, A.M.
Thrombin stimulates RPE cell proliferation by promoting c-Fos-mediated cyclin D1 expression
J. Cell. Physiol.
222
302-312
2010
Homo sapiens
Manually annotated by BRENDA team
Cooper, T.; Taber, D.; Mazur, J.
Implementation of a collaborative drug therapy management service for inpatients receiving direct thrombin inhibitors
Am. J. Health Syst. Pharm.
66
1297-1303
2009
Homo sapiens
Manually annotated by BRENDA team
Suzuki, T.; Ikewaki, J.; Iwata, H.; Ohashi, Y.; Ichinose, A.
The first two Japanese cases of severe type I congenital plasminogen deficiency with ligneous conjunctivitis: successful treatment with direct thrombin inhibitor and fresh plasma
Am. J. Hematol.
84
363-365
2009
Homo sapiens
Manually annotated by BRENDA team
Yin, X.; Wright, J.; Wall, T.; Grammas, P.
Brain endothelial cells synthesize neurotoxic thrombin in Alzheimers disease
Am. J. Pathol.
176
1600-1606
2010
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Heil, S.
[Heparin-induced thrombocytopenia type II with thrombosis in an intensive care patient: therapy management using the direct thrombin inhibitor argatroban]
Anaesthesist
58
1119-1122
2009
Homo sapiens
Manually annotated by BRENDA team
Chang, H.; Tang, L.; Wang, Y.; Jiang, J.; Li, J.
Graphene fluorescence resonance energy transfer aptasensor for the thrombin detection
Anal. Chem.
82
2341-2346
2010
Homo sapiens
Manually annotated by BRENDA team
Koelbel, T.; Donath, T.; Strandberg, K.; Flondell-Site, D.; Kuehme, T.; Gottsaeter, A.; Lindblad, B.
Is increased thrombin activation in patients with abdominal aortic aneurysms dependent on area or volume of aneurysm thrombus mass?
Angiology
61
113-118
2010
Homo sapiens
Manually annotated by BRENDA team
Bogatkevich, G.S.; Ludwicka-Bradley, A.; Silver, R.M.
Dabigatran, a direct thrombin inhibitor, demonstrates antifibrotic effects on lung fibroblasts
Arthritis Rheum.
60
3455-3464
2009
Homo sapiens
Manually annotated by BRENDA team
Chang, C.J.; Hsu, L.A.; Ko, Y.H.; Chen, P.L.; Chuang, Y.T.; Lin, C.Y.; Liao, C.H.; Pang, J.H.
Thrombin regulates matrix metalloproteinase-9 expression in human monocytes
Biochem. Biophys. Res. Commun.
385
241-246
2009
Homo sapiens
Manually annotated by BRENDA team
Cheng, D.C.; Zhong, G.C.; Su, J.X.; Liu, Y.H.; Li, Y.; Wang, J.Y.; Hattori, T.; Ling, H.; Zhang, F.M.
A sensitive HIV-1 envelope induced fusion assay identifies fusion enhancement of thrombin
Biochem. Biophys. Res. Commun.
391
1780-1784
2010
Homo sapiens
Manually annotated by BRENDA team
Chung, S.W.; Park, J.W.; Lee, S.A.; Eo, S.K.; Kim, K.
Thrombin promotes proinflammatory phenotype in human vascular smooth muscle cell
Biochem. Biophys. Res. Commun.
396
748-754
2010
Homo sapiens
Manually annotated by BRENDA team
Ofosu, F.A.; Dewar, L.; Song, Y.; Cedrone, A.C.; Hortelano, G.; Craven, S.J.
Early intraplatelet signaling enhances the release of human platelet PAR-1 and -4 amino-terminal peptides in response to thrombin
Biochemistry
48
1562-1572
2009
Homo sapiens
Manually annotated by BRENDA team
Kovach, I.M.; Kelley, P.; Eddy, C.; Jordan, F.; Baykal, A.
Proton bridging in the interactions of thrombin with small inhibitors
Biochemistry
48
7296-7304
2009
Homo sapiens
Manually annotated by BRENDA team
Qureshi, S.H.; Yang, L.; Manithody, C.; Iakhiaev, A.V.; Rezaie, A.R.
Mutagenesis studies toward understanding allostery in thrombin
Biochemistry
48
8261-8270
2009
Homo sapiens
Manually annotated by BRENDA team
Lima, L.M.; Becker, C.F.; Giesel, G.M.; Marques, A.F.; Cargnelutti, M.T.; de Oliveira Neto, M.; Monteiro, R.Q.; Verli, H.; Polikarpov, I.
Structural and thermodynamic analysis of thrombin:suramin interaction in solution and crystal phases
Biochim. Biophys. Acta
1794
873-881
2009
Homo sapiens (P00734), Homo sapiens
Manually annotated by BRENDA team
Freitas, S.C.; Barbosa, M.A.; Martins, M.C.
The effect of immobilization of thrombin inhibitors onto self-assembled monolayers on the adsorption and activity of thrombin
Biomaterials
31
3772-3780
2010
Homo sapiens
Manually annotated by BRENDA team
Verghese, J.; Liang, A.; Sidhu, P.P.; Hindle, M.; Zhou, Q.; Desai, U.R.
First steps in the direction of synthetic, allosteric, direct inhibitors of thrombin and factor Xa
Bioorg. Med. Chem. Lett.
19
4126-4129
2009
Homo sapiens
Manually annotated by BRENDA team
Pu, J.; Yang, T.
Thrombin: A potential regulator between head injury and enhanced osteogenesis
Biosci. Hypotheses
2
326-328
2009
Homo sapiens
-
Manually annotated by BRENDA team
Kastl, S.P.; Speidl, W.S.; Katsaros, K.M.; Kaun, C.; Rega, G.; Assadian, A.; Hagmueller, G.W.; Hoeth, M.; de Martin, R.; Ma, Y.; Maurer, G.; Huber, K.; Wojta, J.
Thrombin induces the expression of oncostatin M via AP-1 activation in human macrophages: a link between coagulation and inflammation
Blood
114
2812-2818
2009
Homo sapiens
Manually annotated by BRENDA team
Azizova, O.A.; Piryazev, A.P.; Aseychev, A.V.; Shvachko, A.G.
Oxidative modification of fibrinogen inhibits its transformation into fibrin under the effect of thrombin
Bull. Exp. Biol. Med.
147
201-203
2009
Homo sapiens
Manually annotated by BRENDA team
Dobrovolsky, A.B.; Titaeva, E.V.; Khaspekova, S.G.; Spiridonova, V.A.; Kopylov, A.M.; Mazurov, A.V.
Inhibition of thrombin activity with DNA-aptamers
Bull. Exp. Biol. Med.
148
33-36
2009
Homo sapiens
Manually annotated by BRENDA team
Azizova, O.A.; Shvachko, A.G.; Aseichev, A.V.
Effect of iron ions on functional activity of thrombin
Bull. Exp. Biol. Med.
148
776-779
2009
Homo sapiens
Manually annotated by BRENDA team
Zhang, T.; Ma, Z.; Wang, R.; Wang, Y.; Wang, S.; Cheng, Z.; Xu, H.; Jin, X.; Li, W.; Wang, X.
Thrombin facilitates invasion of ovarian cancer along peritoneum by inducing monocyte differentiation toward tumor-associated macrophage-like cells
Cancer Immunol. Immunother.
59
1097-1108
2010
Homo sapiens
Manually annotated by BRENDA team
Green, D.; Karpatkin, S.
Role of thrombin as a tumor growth factor
Cell Cycle
9
656-661
2010
Homo sapiens
Manually annotated by BRENDA team
Stangier, J.; Clemens, A.
Pharmacology, pharmacokinetics, and pharmacodynamics of dabigatran etexilate, an oral direct thrombin inhibitor
Clin. Appl. Thromb. Hemost.
15
9S-16S
2009
Homo sapiens
Manually annotated by BRENDA team
Walfridsson, H.; Johansson, B.; Englund, A.; Kennebaeck, G.; Schwieler, J.; Kongstad, O.; Wahlander, K.; Malm, A.R.; Edvardsson, N.
Effects of AZD0837, a novel direct thrombin inhibitor, on the electrophysiological properties of the human heart: a randomized, double-blind, parallel-group, placebo-controlled study
Clin. Drug Investig.
30
461-471
2010
Homo sapiens
Manually annotated by BRENDA team
Turpie, A.G.
Direct Factor Xa and direct thrombin inhibitors: a clinical trial update
Curr. Opin. Drug Discov. Devel.
12
497-508
2009
Homo sapiens
Manually annotated by BRENDA team
Yoshikawa, Y.; Hirayasu, H.; Tsuzuki, S.; Fushiki, T.
Granzyme A and thrombin differentially promote the release of interleukin-8 from alveolar epithelial A549 cells
Cytotechnology
62
325-332
2010
Homo sapiens
Manually annotated by BRENDA team
Lip, G.Y.; Rasmussen, L.H.; Olsson, S.B.; Jensen, E.C.; Persson, A.L.; Eriksson, U.; Wahlander, K.F.; Wahlander, K.F.
Oral direct thrombin inhibitor AZD0837 for the prevention of stroke and systemic embolism in patients with non-valvular atrial fibrillation: a randomized dose-guiding, safety, and tolerability study of four doses of AZD0837 vs. vitamin K antagonists
Eur. Heart J.
30
2897-2907
2009
Homo sapiens
Manually annotated by BRENDA team
Schaden, E.; Kozek-Langenecker, S.A.
Direct thrombin inhibitors: pharmacology and application in intensive care medicine
Intensive Care Med.
36
1127-1137
2010
Homo sapiens
Manually annotated by BRENDA team
Squizzato, A.; Dentali, F.; Steidl, L.; Ageno, W.
New direct thrombin inhibitors
Intern. Emerg. Med.
4
479-484
2009
Homo sapiens
Manually annotated by BRENDA team
Gandhi, P.S.; Page, M.J.; Chen, Z.; Bush-Pelc, L.; Di Cera, E.
Mechanism of the anticoagulant activity of thrombin mutant W215A/E217A
J. Biol. Chem.
284
24098-24105
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Petrera, N.S.; Stafford, A.R.; Leslie, B.A.; Kretz, C.A.; Fredenburgh, J.C.; Weitz, J.I.
Long range communication between exosites 1 and 2 modulates thrombin function
J. Biol. Chem.
284
25620-25629
2009
Homo sapiens
Manually annotated by BRENDA team
Niu, W.; Chen, Z.; Bush-Pelc, L.A.; Bah, A.; Gandhi, P.S.; Di Cera, E.
Mutant N143P reveals how Na+ activates thrombin
J. Biol. Chem.
284
36175-36185
2009
Homo sapiens
Manually annotated by BRENDA team
Gandhi, P.S.; Chen, Z.; Di Cera, E.
Crystal structure of thrombin bound to the uncleaved extracellular fragment of PAR1
J. Biol. Chem.
285
15393-15398
2010
Homo sapiens
Manually annotated by BRENDA team
Gambaryan, S.; Kobsar, A.; Rukoyatkina, N.; Herterich, S.; Geiger, J.; Smolenski, A.; Lohmann, S.M.; Walter, U.
Thrombin and collagen induce a feedback inhibitory signaling pathway in platelets involving dissociation of the catalytic subunit of protein kinase A from an NFkappaB-IkappaB complex
J. Biol. Chem.
285
18352-18363
2010
Homo sapiens
Manually annotated by BRENDA team
Sarilla, S.; Habib, S.Y.; Kravtsov, D.V.; Matafonov, A.; Gailani, D.; Verhamme, I.M.
Sucrose octasulfate selectively accelerates thrombin inactivation by heparin cofactor II
J. Biol. Chem.
285
8278-8289
2010
Homo sapiens
Manually annotated by BRENDA team
Chen, H.T.; Tsou, H.K.; Tsai, C.H.; Kuo, C.C.; Chiang, Y.K.; Chang, C.H.; Fong, Y.C.; Tang, C.H.
Thrombin enhanced migration and MMPs expression of human chondrosarcoma cells involves PAR receptor signaling pathway
J. Cell. Physiol.
223
737-745
2010
Homo sapiens
Manually annotated by BRENDA team
Bae, J.S.; Kim, I.S.; Rezaie, A.R.
Thrombin down-regulates the TGF-beta-mediated synthesis of collagen and fibronectin by human proximal tubule epithelial cells through the EPCR-dependent activation of PAR-1
J. Cell. Physiol.
225
233-239
2010
Homo sapiens
Manually annotated by BRENDA team
Nicolotti, O.; Giangreco, I.; Miscioscia, T.F.; Convertino, M.; Leonetti, F.; Pisani, L.; Carotti, A.
Screening of benzamidine-based thrombin inhibitors via a linear interaction energy in continuum electrostatics model
J. Comput. Aided Mol. Des.
24
117-129
2010
Homo sapiens
Manually annotated by BRENDA team
Nilsson, M.; Haemaelaeinen, M.; Ivarsson, M.; Gottfries, J.; Xue, Y.; Hansson, S.; Isaksson, R.; Fex, T.
Compounds binding to the S2-S3 pockets of thrombin
J. Med. Chem.
52
2708-2715
2009
Homo sapiens
Manually annotated by BRENDA team
Lu, T.; Markotan, T.; Ballentine, S.K.; Giardino, E.C.; Spurlino, J.; Crysler, C.S.; Brown, K.; Maryanoff, B.E.; Tomczuk, B.E.; Damiano, B.P.; Shukla, U.; End, D.; Andrade-Gordon, P.; Bone, R.F.; Player, M.R.
Discovery and clinical evaluation of 1-{N-[2-(amidinoaminooxy)ethyl]amino}carbonylmethyl-6-methyl-3-[2,2-difluoro-2-phenylethylamino]pyrazinone (RWJ-671818), a thrombin inhibitor with an oxyguanidine P1 motif
J. Med. Chem.
53
1843-1856
2010
Homo sapiens
Manually annotated by BRENDA team
Muley, L.; Baum, B.; Smolinski, M.; Freindorf, M.; Heine, A.; Klebe, G.; Hangauer, D.G.
Enhancement of hydrophobic interactions and hydrogen bond strength by cooperativity: synthesis, modeling, and molecular dynamics simulations of a congeneric series of thrombin inhibitors
J. Med. Chem.
53
2126-2135
2010
Homo sapiens
Manually annotated by BRENDA team
Baum, B.; Muley, L.; Heine, A.; Smolinski, M.; Hangauer, D.; Klebe, G.
Think twice: understanding the high potency of bis(phenyl)methane inhibitors of thrombin
J. Mol. Biol.
391
552-564
2009
Homo sapiens
Manually annotated by BRENDA team
Cuerrier, C.M.; Gagner, A.; Lebel, R.; Gobeil, F.; Grandbois, M.
Effect of thrombin and bradykinin on endothelial cell mechanical properties monitored through membrane deformation
J. Mol. Recognit.
22
389-396
2009
Homo sapiens
Manually annotated by BRENDA team
Werthmann, R.C.; von Hayn, K.; Nikolaev, V.O.; Lohse, M.J.; Buenemann, M.
Real-time monitoring of cAMP levels in living endothelial cells: thrombin transiently inhibits adenylyl cyclase 6
J. Physiol.
587
4091-4104
2009
Homo sapiens
Manually annotated by BRENDA team
Adjemian, J.; Anne, A.; Cauet, G.; Demaille, C.
Cleavage-sensing redox peptide monolayers for the rapid measurement of the proteolytic activity of trypsin and alpha-thrombin enzymes
Langmuir
26
10347-10356
2010
Homo sapiens
Manually annotated by BRENDA team
Wang, Z.; Kong, L.; Kang, J.; Morgan, J.H.; Shillcutt, S.D.; Robinson, J.S.; Nakayama, D.K.
Thrombin stimulates mitogenesis in pig cerebrovascular smooth muscle cells involving activation of pro-matrix metalloproteinase-2
Neurosci. Lett.
451
199-203
2009
Homo sapiens
Manually annotated by BRENDA team
Argueelles, S.; Herrera, A.J.; Carreno-Mueller, E.; de Pablos, R.M.; Villaran, R.F.; Espinosa-Oliva, A.M.; Machado, A.; Cano, J.
Degeneration of dopaminergic neurons induced by thrombin injection in the substantia nigra of the rat is enhanced by dexamethasone: role of monoamine oxidase enzyme
Neurotoxicology
31
55-66
2010
Homo sapiens
Manually annotated by BRENDA team
Robert, S.; Ghiotto, J.; Pirotte, B.; David, J.L.; Masereel, B.; Pochet, L.; Dogne, J.M.
Is thrombin generation the new rapid, reliable and relevant pharmacological tool for the development of anticoagulant drugs?
Pharmacol. Res.
59
160-166
2009
Homo sapiens
Manually annotated by BRENDA team
Papareddy, P.; Rydengard, V.; Pasupuleti, M.; Walse, B.; Moergelin, M.; Chalupka, A.; Malmsten, M.; Schmidtchen, A.
Proteolysis of human thrombin generates novel host defense peptides
PLoS Pathog.
6
e1000857
2010
Homo sapiens
Manually annotated by BRENDA team
Grade, S.; Agasse, F.; Bernardino, L.; Silva, C.G.; Cortes, L.; Malva, J.O.
Functional identification of neural stem cell-derived oligodendrocytes by means of calcium transients elicited by thrombin
Rejuvenation Res.
13
27-37
2010
Homo sapiens
Manually annotated by BRENDA team
Zheng, J.; Cheng, G.F.; He, P.G.; Fang, Y.Z.
An aptamer-based assay for thrombin via structure switch based on gold nanoparticles and magnetic nanoparticles
Talanta
80
1868-1872
2010
Homo sapiens
Manually annotated by BRENDA team
Leoncini, G.; Signorello, M.G.; Segantin, A.; Giacobbe, E.; Armani, U.; Piana, A.; Camicione, P.
In retinal vein occlusion platelet response to thrombin is increased
Thromb. Res.
124
e48-e55
2009
Homo sapiens
Manually annotated by BRENDA team
Bae, J.S.; Rezaie, A.R.
Thrombin and activated protein C inhibit the expression of secretory group IIA phospholipase A2 in the TNF-alpha-activated endothelial cells by EPCR and PAR-1 dependent mechanisms
Thromb. Res.
125
e9-e15
2010
Homo sapiens
Manually annotated by BRENDA team
Christersson, C.; Johnell, M.; Siegbahn, A.
The influence of direct thrombin inhibitors on the formation of platelet-leukocyte aggregates and tissue factor expression
Thromb. Res.
126
e327-e333
2010
Homo sapiens
Manually annotated by BRENDA team
Osipov, A.V.; Filkin, S.Y.; Makarova, Y.V.; Tsetlin, V.I.; Utkin, Y.N.
A new type of thrombin inhibitor, noncytotoxic phospholipase A2, from the Naja haje cobra venom
Toxicon
55
186-194
2010
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Russo Krauss, I.; Merlino, A.; Randazzo, A.; Mazzarella, L.; Sica, F.
Crystallization and preliminary X-ray analysis of the complex of human alpha-thrombin with a modified thrombin-binding aptamer
Acta Crystallogr. Sect. F
66
961-963
2010
Homo sapiens
Manually annotated by BRENDA team
Zavyalova, E.G.; Protopopova, A.D.; Yaminsky, I.V.; Kopylov, A.M.
Kinetic characterization of inhibition of human thrombin with DNA aptamers by turbidimetric assay
Anal. Biochem.
421
234-239
2012
Homo sapiens
Manually annotated by BRENDA team
Kasetty, G.; Papareddy, P.; Kalle, M.; Rydengard, V.; Moergelin, M.; Albiger, B.; Malmsten, M.; Schmidtchen, A.
Structure-activity studies and therapeutic potential of host defense peptides of human thrombin
Antimicrob. Agents Chemother.
55
2880-2890
2011
Homo sapiens
Manually annotated by BRENDA team
Dangwal, S.; Rauch, B.H.; Gensch, T.; Dai, L.; Bretschneider, E.; Vogelaar, C.F.; Schroer, K.; Rosenkranz, A.C.
High glucose enhances thrombin responses via protease-activated receptor-4 in human vascular smooth muscle cells
Arterioscler. Thromb. Vasc. Biol.
31
624-633
2011
Homo sapiens
Manually annotated by BRENDA team
Kawanami, D.; Matoba, K.; Kanazawa, Y.; Ishizawa, S.; Yokota, T.; Utsunomiya, K.
Thrombin induces MCP-1 expression through Rho-kinase and subsequent p38MAPK/NF-kappaB signaling pathway activation in vascular endothelial cells
Biochem. Biophys. Res. Commun.
411
798-803
2011
Homo sapiens
Manually annotated by BRENDA team
Siles, R.; Kawasaki, Y.; Ross, P.; Freire, E.
Synthesis and biochemical evaluation of triazole/tetrazole-containing sulfonamides against thrombin and related serine proteases
Bioorg. Med. Chem. Lett.
21
5305-5309
2011
Homo sapiens
Manually annotated by BRENDA team
Choi, S.H.; Smith, S.A.; Morrissey, J.H.
Polyphosphate is a cofactor for the activation of factor XI by thrombin
Blood
118
6963-6970
2011
Homo sapiens
Manually annotated by BRENDA team
Hsu, C.L.; Chang, H.T.; Chen, C.T.; Wei, S.C.; Shiang, Y.C.; Huang, C.C.
Highly efficient control of thrombin activity by multivalent nanoparticles
Chemistry
17
10994-11000
2011
Homo sapiens
Manually annotated by BRENDA team
Marino, F.; Pelc, L.A.; Vogt, A.; Gandhi, P.S.; Di Cera, E.
Engineering thrombin for selective specificity toward protein C and PAR1
J. Biol. Chem.
285
19145-19152
2010
Homo sapiens
Manually annotated by BRENDA team
Burch, M.L.; Ballinger, M.L.; Yang, S.N.; Getachew, R.; Itman, C.; Loveland, K.; Osman, N.; Little, P.J.
Thrombin stimulation of proteoglycan synthesis in vascular smooth muscle is mediated by protease-activated receptor-1 transactivation of the transforming growth factor beta type I receptor
J. Biol. Chem.
285
26798-26805
2010
Homo sapiens
Manually annotated by BRENDA team
Lin, C.H.; Cheng, H.W.; Ma, H.P.; Wu, C.H.; Hong, C.Y.; Chen, B.C.
Thrombin induces NF-kappaB activation and IL-8/CXCL8 expression in lung epithelial cells by a Rac1-dependent PI3K/Akt pathway
J. Biol. Chem.
286
10483-10494
2011
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Kerk, N.; Strozyk, E.A.; Poeppelmann, B.; Schneider, S.W.
The mechanism of melanoma-associated thrombin activity and von Willebrand factor release from endothelial cells
J. Invest. Dermatol.
130
2259-2268
2010
Homo sapiens
Manually annotated by BRENDA team
Koh, C.Y.; Kumar, S.; Kazimirova, M.; Nuttall, P.A.; Radhakrishnan, U.P.; Kim, S.; Jagadeeswaran, P.; Imamura, T.; Mizuguchi, J.; Iwanaga, S.; Swaminathan, K.; Kini, R.M.
Crystal structure of thrombin in complex with s-variegin: insights of a novel mechanism of inhibition and design of tunable thrombin inhibitors
PLoS ONE
6
e26367
2011
Homo sapiens
Manually annotated by BRENDA team
Liu, Y.; Liu, N.; Ma, X.; Li, X.; Ma, J.; Li, Y.; Zhou, Z.; Gao, Z.
Highly specific detection of thrombin using an aptamer-based suspension array and the interaction analysis via microscale thermophoresis
Analyst
140
2762
2015
Homo sapiens
Manually annotated by BRENDA team
Newell-Caito, J.L.; Griffiths, A.E.; Fay, P.J.
P3-P3' residues flanking scissile bonds in factor VIII modulate rates of substrate cleavage and procofactor activation by thrombin
Biochemistry
51
3451-3459
2012
Homo sapiens
Manually annotated by BRENDA team
Winquist, J.; Geschwindner, S.; Xue, Y.; Gustavsson, L.; Musil, D.; Deinum, J.; Danielson, U.H.
Identification of structural-kinetic and structural-thermodynamic relationships for thrombin inhibitors
Biochemistry
52
613-626
2013
Homo sapiens
Manually annotated by BRENDA team
Malovichko, M.; Sabo, T.; Maurer, M.
Ligand binding to anion-binding exosites regulates conformational properties of thrombin
J. Biol. Chem.
288
8667-8678
2013
Homo sapiens (P00734)
Manually annotated by BRENDA team
Gallwitz, M.; Enoksson, M.; Thorpe, M.; Hellman, L.
The extended cleavage specificity of human thrombin
PLoS ONE
7
e31756
2012
Homo sapiens
Manually annotated by BRENDA team
Zavyalova, E.; Kopylov, A.
Multiple inhibitory kinetics reveal an allosteric interplay among thrombin functional sites
Thromb. Res.
135
212-216
2015
Homo sapiens
Manually annotated by BRENDA team
Robertson, A.L.; Headey, S.J.; Ng, N.M.; Wijeyewickrema, L.C.; Scanlon, M.J.; Pike, R.N.; Bottomley, S.P.
Protein unfolding is essential for cleavage within the alpha-helix of a model protein substrate by the serine protease, thrombin
Biochimie
122
227-234
2016
Homo sapiens (P00734)
Manually annotated by BRENDA team
Loevgren, A.; Deinum, J.; Rosen, S.; Bryngelhed, P.; Rosen, P.; Hansson, K.M.
Characterization of thrombin derived from human recombinant prothrombin
Blood Coagul. Fibrinolysis
26
545-555
2015
Homo sapiens (P00734), Homo sapiens
Manually annotated by BRENDA team
Dolot, R.; Lam, C.H.; Sierant, M.; Zhao, Q.; Liu, F.W.; Nawrot, B.; Egli, M.; Yang, X.
Crystal structures of thrombin in complex with chemically modified thrombin DNA aptamers reveal the origins of enhanced affinity
Nucleic Acids Res.
46
4819-4830
2018
Homo sapiens (P00734)
Manually annotated by BRENDA team
Chahal, G.; Thorpe, M.; Hellman, L.
The importance of exosite interactions for substrate cleavage by human thrombin
PLoS ONE
10
e0129511
2015
Homo sapiens (P00734), Homo sapiens
Manually annotated by BRENDA team
Arumugam, J.; Bukkapatnam, S.T.; Narayanan, K.R.; Srinivasa, A.R.
Random forests are able to identify differences in clotting dynamics from kinetic models of thrombin generation
PLoS ONE
11
e0153776
2016
Homo sapiens (P00734)
Manually annotated by BRENDA team