Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ac-Gly-Gly-Val-Arg-7-amido-4-methylcoumarin + H2O
Ac-Gly-Gly-Val-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
?
Ac-Leu-Gly-Val-Arg-7-amido-4-methylcoumarin + H2O
Ac-Leu-Gly-Val-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
?
Ac-Nle-Thr-Leu-Arg-7-amido-4-methylcoumarin + H2O
Ac-Nle-Thr-Leu-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
?
Ac-Nle-Thr-Pro-Arg-7-amido-4-methylcoumarin + H2O
Ac-Nle-Thr-Pro-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
?
Ac-Val-Thr-Pro-Arg-7-amido-4-methylcoumarin + H2O
Ac-Val-Thr-Pro-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
?
activated protein C + H2O
?
-
Substrates: -
Products: -
?
Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Ala-Ala-Pro-Phe + 4-nitroaniline
-
Substrates: synthetic chromogenic substrate
Products: -
?
benzoyl-Arg ethyl ester + H2O
benzoyl-Arg + ethanol
-
Substrates: -
Products: -
?
benzoyl-Arg methyl ester + H2O
benzoyl-Arg + methanol
-
Substrates: -
Products: -
?
benzoyl-L-Arg-p-nitroanilide + H2O
benzoyl-L-Arg + p-nitroaniline
-
Substrates: -
Products: -
?
beta-Ala-Gly-Arg-4-nitroanilide + H2O
beta-Ala-Gly-Arg + 4-nitroaniline
-
Substrates: -
Products: -
?
chromozym TH + H2O
? + 4-nitroaniline
-
Substrates: -
Products: -
?
coagulation factor V + H2O
?
Substrates: -
Products: -
?
coagulation factor VIII + H2O
?
Substrates: -
Products: -
?
D-Phe-L-pipecolyl-L-Arg-4-nitroanilide + H2O
D-Phe-L-pipecolyl-L-Arg + 4-nitroaniline
-
Substrates: -
Products: -
?
D-Phe-L-Pro-L-Arg-4-nitroanilide + H2O
D-Phe-L-Pro-L-Arg + 4-nitroaniline
D-Phe-L-Pro-L-Phe-4-nitroanilide + H2O
D-Phe-L-Pro-L-Phe + 4-nitroaniline
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
-
Substrates: i.e. S-2238
Products: -
?
D-Phe-Pro-Arg-4-nitroanilide + H2O
D-Phe-Pro-Arg + 4-nitroaniline
D-Phe-Pro-Lys-4-nitroanilide + H2O
D-Phe-Pro-Lys + 4-nitroaniline
D-Phe-Pro-Phe-4-nitroanilide + H2O
D-Phe-Pro-Phe + 4-nitroaniline
-
Substrates: -
Products: -
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
di-L-Glu-L-Pro-L-Arg-4-nitroanilide + H2O
di-L-Glu-L-Pro-L-Arg + 4-nitroaniline
-
Substrates: -
Products: -
?
factor V (1018) + H2O
?
-
Substrates: cleavage site is LSPR
Products: -
?
factor V (1545) + H2O
?
-
Substrates: cleavage site is WYLR
Products: -
?
factor V (709) + H2O
?
-
Substrates: -
Products: -
?
factor V + H2O
activated factor V + ?
-
Substrates: activation
Products: -
?
factor V + H2O
factor Va + propeptide
-
Substrates: proteolytic activation
Products: -
?
factor VII (1689) + H2O
?
-
Substrates: clevage site is QSPR
Products: -
?
factor VII (372) + H2O
?
-
Substrates: cleavage site is IQIR
Products: -
?
factor VII (740) + H2O
?
-
Substrates: -
Products: -
?
factor VIII + H2O
activated factor VIII + ?
-
Substrates: activation
Products: -
?
factor VIII + H2O
factor VIIIa + propeptide
factor VIII mutant D392A/D394A + H2O
?
-
Substrates: reduction in specific activity similar to a severe hemophilia phenotype. No cleavage at R740, while cleavage at R372 is not affected
Products: -
?
factor VIII mutant Q370E/I371P/V374F/A375S + H2O
?
-
Substrates: -
Products: mutation to P3-P3' residues flanking Arg740, 98% of the activtiy with wild-type
?
factor VIII mutant Q370S/I371P/V374F/A375Q + H2O
?
-
Substrates: -
Products: mutation to P3-P3' residues flanking Arg1689, 14% of the activtiy with wild-type
?
factor VIII mutant R372H + H2O
?
-
Substrates: naturally occuring mutation in hemophilia A patients. About 80fold decrease in cleavage rate compared to wild-type substrate, cleavage at H372-S373 bond
Products: -
?
factor VIII(341-376) peptide + H2O
?
-
Substrates: cleavage of Arg372 involving exosite II, the heparin binding site
Products: -
?
factor X + H2O
factor Xa + propeptide
factor XI + H2O
?
-
Substrates: -
Products: -
?
factor XI + H2O
activated factor XI + ?
-
Substrates: activation
Products: -
?
factor XI + H2O
factor XIa + ?
-
Substrates: activation by thrombin
Products: -
?
factor XI + H2O
factor XIa + propeptide
-
Substrates: proteolytic activation
Products: -
?
factor XII + H2O
activated factor XII + ?
factor XIII + H2O
?
-
Substrates: -
Products: -
?
factor XIII + H2O
activated factor XIII + ?
factor XIII + H2O
factor XIIIa + propeptide
factor XIII V34L mutant + H2O
activated factor XIII V34L mutant + ?
-
Substrates: 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
Products: -
?
Fc-[GRPS]-PEG + H2O
?
-
Substrates: ferrocene-labelled tetrapeptide with a polyethylene glycol linker
Products: -
?
Fc-[RFSRPQL]-PEG + H2O
?
-
Substrates: ferrocene-labelled heptapeptide with a polyethylene glycol linker
Products: -
?
fibrin I-plasma factor XIII complex + H2O
activation peptide + fibrinopeptide B
-
Substrates: -
Products: -
?
fibrinogen + H2O
fibrin + ?
fibrinogen + H2O
fibrin + fibrinopeptide A + fibrinopeptide B
fibrinogen 1 + H2O
fibrin 1 + fibrinopeptide A + fibrinopeptide B
fibrinogen 2 + H2O
fibrin 2 + fibrinopeptide A + fibrinopeptide B
fibrinogen A a + H2O
?
-
Substrates: -
Products: -
?
fibrinogen Aalpha chain + H2O
?
-
Substrates: -
Products: -
?
Fibrinogen Aalpha-chain + H2O
?
Substrates: -
Products: -
?
fibrinogen B b + H2O
?
-
Substrates: -
Products: -
?
GLVPRGVNL + H2O
GLVPR + GVNL
-
Substrates: residues 33-41 of factor XIII with mutation V34L
Products: -
?
GVVPRGVNL + H2O
GVVPR + GVNL
-
Substrates: residues 33-41 of factor XIII
Products: -
?
HD-cyclohexylglycyl-Ala-Arg-4-nitroanilide + H2O
HD-cyclohexylglycyl-Ala-Arg + 4-nitroaniline
-
Substrates: assay method optimization with synthetic substrate HD-cyclohexylglycyl-Ala-Arg-4-nitroanilide, overview
Products: -
?
Meizothrombin + H2O
?
-
Substrates: cleavage of R155-S156 and R284-T285 bond
Products: -
?
N-(4-tosyl)-Gly-L-Pro-L-Arg-4-nitroanilide + H2O
N-(4-tosyl)-Gly-L-Pro-L-Arg + 4-nitroaniline
-
Substrates: -
Products: -
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
-
Substrates: -
Products: -
?
Nalpha-benzyloxycarbonyl-L-Arg 4-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Arg + 4-nitrophenol
-
Substrates: -
Products: -
?
Nalpha-benzyloxycarbonyl-L-Lys 4-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Lys + 4-nitrophenol
-
Substrates: -
Products: -
?
p-nitrophenyl-p'-(Nbeta,n-butyl-Nalpha-guanidino)benzoate + H2O
?
-
Substrates: -
Products: -
?
p-nitrophenyl-p'-(Nbeta,n-hexyl-Nalpha-guanidino)benzoate + H2O
?
-
Substrates: -
Products: -
?
p-nitrophenyl-p'-guanidinobenzoate + H2O
?
-
Substrates: -
Products: -
?
PAR1 peptide + H2O
?
Substrates: protease-activated receptor I peptide fragment, amino acid sequence
Products: -
?
PAR3 + H2O
?
-
Substrates: protease-activated receptor 3
Products: -
?
Pefachrom tPa + H2O
?
-
Substrates: -
Products: -
?
platelet thrombin receptor peptide + H2O
?
-
Substrates: -
Products: -
?
prethrombin + H2O
?
-
Substrates: cleavage of R284-T285 bond
Products: -
?
pro-factor XIII + H2O
factor XIII
-
Substrates: activation by cleavage at Arg37 leading to blood coagulation
Products: -
?
profactor V + H2O
factor V
-
Substrates: human, activation, recombinant
Products: -
?
profactor VIII + H2O
factor VIII
-
Substrates: human, activation, recombinant
Products: -
?
protease-activated receptor + H2O
?
-
Substrates: activation
Products: -
?
protease-activated receptor + H2O
activated protease-activated receptor + ?
-
Substrates: activation
Products: -
?
protease-activated receptor 1 + H2O
?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
-
Substrates: activation
Products: -
?
protease-activated receptor 3 residues 44-56 + H2O
?
Substrates: -
Products: -
?
protease-activated receptor 4 + H2O
activated PAR-4 + ?
-
Substrates: the cleaved form of protease-activated receptor 3, PAR-3, acts as a cofactor for thrombin cleavage and activation of PAR-4 on murine platelets, interaction analysis of thrombin with the extracellular part of PAR-4, overview
Products: -
?
protease-activated receptor-1 + H2O
?
protease-activated receptor-1 + H2O
activated PAR-1
protease-activated receptor-3 + H2O
?
-
Substrates: activation
Products: -
?
protease-activated receptor-4 + H2O
?
-
Substrates: activation
Products: -
?
protein C
?
Substrates: -
Products: -
?
protein C + H2O
activated protein C + ?
-
Substrates: solvent isotope effect study
Products: -
?
protein C zymogen + H2O
activated protein C + propeptide
protein G + H2O
?
Substrates: 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
Products: -
?
protein kinase C + H2O
?
-
Substrates: activation
Products: -
?
proteinase-activated receptor 1 + H2O
?
-
Substrates: alpha-thrombin may not effectively catalyze proteinase-activated receptor 1-(1-41) generation
Products: -
?
proteinase-activated receptor 4 + H2O
?
-
Substrates: alpha-thrombin may not effectively catalyze proteinase-activated receptor 4-(1-47) generation
Products: -
?
prothrombin + H2O
?
-
Substrates: cleavage of R155-S156 and R284-T285 bond
Products: -
?
RAP + H2O
?
-
Substrates: -
Products: -
?
S-2238 + H2O
?
Substrates: -
Products: -
?
S-2366 + H2O
?
Substrates: -
Products: -
?
S-2765 + H2O
?
Substrates: -
Products: -
?
S-thanatin + H2O
?
-
Substrates: -
Products: -
?
spectrozyme TH + H2O
?
-
Substrates: -
Products: -
?
succinyl-AAPR-4-nitroanilide + H2O
succinyl-AAPR + 4-nitroaniline
-
Substrates: -
Products: -
?
thrombin-activable finrinolysis inhibitor + H2O
?
-
Substrates: i.e. TAFI
Products: -
?
thrombin-activatable fibrinolysis inhibitor + H2O
?
tosyl-Arg ethyl ester + H2O
tosyl-Arg + ethanol
-
Substrates: -
Products: -
?
Tosyl-Arg methyl ester + H2O
Tosyl-Arg + methanol
tosyl-Gly-L-Pro-L-Arg-4-nitroanilide + H2O
tosyl-Gly-L-Pro-L-Arg + 4-nitroaniline
-
Substrates: -
Products: -
?
tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
tosyl-Gly-Pro-Arg + 4-nitroaniline
transmembrane receptor PAR1 + H2O
?
-
Substrates: -
Products: -
?
TVELQGLVPRGVNL + H2O
TVELQGLVPR + GVNL
-
Substrates: residues 28-41 of factor XIII with mutation V34L
Products: -
?
TVELQGVVPRGVNL + H2O
TVELQGVVPR + GVNL
-
Substrates: residues 28-41 of factor XIII
Products: -
?
UpA + H2O
?
-
Substrates: -
Products: -
?
additional information
?
-
ADAMTS-13 + H2O
?
-
Substrates: 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
Products: -
?
ADAMTS-13 + H2O
?
-
Substrates: inactivation by cleavage at R257 and R1176, substrate is the plasma metalloprotease, a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13, no activity with R257A and R1176H ADAMTS-13 mutants
Products: -
?
D-Phe-L-Pro-L-Arg-4-nitroanilide + H2O
D-Phe-L-Pro-L-Arg + 4-nitroaniline
-
Substrates: -
Products: -
?
D-Phe-L-Pro-L-Arg-4-nitroanilide + H2O
D-Phe-L-Pro-L-Arg + 4-nitroaniline
-
Substrates: -
Products: -
?
D-Phe-L-Pro-L-Phe-4-nitroanilide + H2O
D-Phe-L-Pro-L-Phe + 4-nitroaniline
-
Substrates: -
Products: -
?
D-Phe-L-Pro-L-Phe-4-nitroanilide + H2O
D-Phe-L-Pro-L-Phe + 4-nitroaniline
-
Substrates: -
Products: -
?
D-Phe-Pro-Arg-4-nitroanilide + H2O
D-Phe-Pro-Arg + 4-nitroaniline
-
Substrates: -
Products: -
?
D-Phe-Pro-Arg-4-nitroanilide + H2O
D-Phe-Pro-Arg + 4-nitroaniline
-
Substrates: synthetic chromogenic substrate
Products: -
?
D-Phe-Pro-Lys-4-nitroanilide + H2O
D-Phe-Pro-Lys + 4-nitroaniline
-
Substrates: -
Products: -
?
D-Phe-Pro-Lys-4-nitroanilide + H2O
D-Phe-Pro-Lys + 4-nitroaniline
-
Substrates: synthetic chromogenic substrate
Products: -
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
Substrates: i.e. S2238, synthetic chromogenic substrate
Products: -
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
Substrates: -
Products: -
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
Substrates: -
Products: -
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
Substrates: i.e. S2238, synthetic chromogenic substrate
Products: -
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
Substrates: i.e. S2238, synthetic chromogenic substrate
Products: -
?
D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-pipecolyl-L-arginine + 4-nitroaniline
-
Substrates: D-phenylalanyl-pipecolyl-L-arginine-4-nitroanilide is S2238
Products: -
?
factor VIII + H2O
?
-
Substrates: -
Products: -
?
factor VIII + H2O
?
-
Substrates: -
Products: proteolysis occurs at residues Arg372 and Arg740 in the facto VIII heavy chain and Arg1689 in the factor VIII light chain. The sequences at Arg740 and Arg1689 are more optimal for thrombin cleavage than at Arg372. Rates of thrombin cleavage at Arg372 are increased about 10fold and about 3fold compared with wild-type factor VIII when replaced with P3-P3' residues flanking Arg740 or Arg1689, respectively, and these values parallel increased rates of A2 subunit generation and procofactor activation. Positioning of more optimal residues flanking Arg372 abrogates the need for initial cleavage at Arg740 to facilitate this step
?
factor VIII + H2O
?
-
Substrates: activation by cleavage of Arg372, Arg74, and Arg1689 involving exosite II, the heparin binding site
Products: -
?
factor VIII + H2O
?
-
Substrates: activation by cleavage of Arg372, Arg74, and Arg1689, plays a fundamental role in the amplification of the coagulation cascade
Products: -
?
factor VIII + H2O
factor VIIIa + propeptide
-
Substrates: proteolytic activation
Products: -
?
factor VIII + H2O
factor VIIIa + propeptide
-
Substrates: high affinity site in A1 subunit of substrate, dependent on Na+-bound form of enzyme. Moderate affinity site in A2 subunit, independent of Na+-state of enzyme
Products: -
?
factor X + H2O
factor Xa + propeptide
-
Substrates: -
Products: -
?
factor X + H2O
factor Xa + propeptide
-
Substrates: proteolytic activation
Products: -
?
factor XII + H2O
activated factor XII + ?
-
Substrates: -
Products: -
?
factor XII + H2O
activated factor XII + ?
-
Substrates: activated factor XII cross-links fibrin molecules and stabilizes the fibrin clot
Products: -
?
factor XIII + H2O
activated factor XIII + ?
-
Substrates: the enzyme is involved in the coagulation cascade, overview
Products: -
?
factor XIII + H2O
activated factor XIII + ?
-
Substrates: binding structure and interaction analysis, wild-type substrate, overview
Products: -
?
factor XIII + H2O
factor XIIIa + propeptide
-
Substrates: -
Products: -
?
factor XIII + H2O
factor XIIIa + propeptide
-
Substrates: proteolytic activation
Products: -
?
Fibrinogen + H2O
?
-
Substrates: cleavage of four Arg-Gly peptide bonds
Products: -
?
Fibrinogen + H2O
?
-
Substrates: cleavage of four Arg-Gly peptide bonds, the enzyme is involved in the final step in the coagulation of mammalian blood
Products: -
?
Fibrinogen + H2O
?
-
Substrates: -
Products: -
?
Fibrinogen + H2O
?
-
Substrates: Aalpha chain
Products: -
?
Fibrinogen + H2O
?
-
Substrates: key regulator of blood coagulation
Products: -
?
Fibrinogen + H2O
?
-
Substrates: clotting of fibrinogen
Products: -
?
Fibrinogen + H2O
?
-
Substrates: the fully reversible interaction of alpha-thrombin with glycoprotein Ibalpha supports the association with platelets of a proteolytically active enzyme that may contribute to activation
Products: -
?
Fibrinogen + H2O
?
-
Substrates: in intact human erythrocyte leucemia cells thrombin activates adenylate cyclase
Products: -
?
fibrinogen + H2O
fibrin + ?
-
Substrates: -
Products: -
?
fibrinogen + H2O
fibrin + ?
-
Substrates: the enzyme mediates the conversion of fibrinogen to fibrin
Products: -
?
fibrinogen + H2O
fibrin + ?
-
show
top
