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.
2-aminobenzoyl-VQFRILGDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-VQFR + ILGDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-VQFRSAGDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-VQFR + SAGDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-VQFRSLEDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-VQFR + SLEDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-VQFRSLTDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-VQFR + SLTDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-VQFRSVGDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-VQFR + SCGDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-VQFRTLGDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-VQFR + TLGDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
Abz-VMIAALPRTMFIQ-ED-dinitrophenyl + H2O
?
-
-
-
?
activated factor VIII + H2O
factor VIII
apomyoglobin + H2O
?
-
maleylated sperm whale apomyoglobin. Hydrolysed at the Arg31-Leu32 bond
-
-
?
Arg-Gly-Arg-4-nitroanilide + H2O
Arg-Gly-Arg + 4-nitroaniline
benzoyl-Ile-Glu(gamma-O-methyl)-Gly-Arg-4-nitroanilide + N-benzoyl-Ile-Glu-Gly-Arg-4-nitroanilide + H2O
benzoyl-Ile-Glu(gamma-O-methyl)-Gly-Arg + N-benzoyl-Ile-Glu-Gly-Arg + 4-nitroaniline
benzoyl-Ile-Glu(gamma-OR)-Gly-Arg-4-nitroanilide + H2O
benzoyl-Ile-Glu(gamma-OR)-Gly-Arg + 4-nitroaniline
-
-
-
?
benzoyl-Ile-Glu(piperidineamide)-Gly-Arg-p-nitroanilide + H2O
?
-
-
-
-
?
benzoyl-Ile-Glu-(-H/OMe)-Gly-Arg-p-nitroanilide + H2O
?
-
-
-
-
?
Boc-L-Asp(OBzl)-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
Boc-L-Asp(OBzl)-L-Pro-L-Arg + 7-amino-4-methylcoumarin
chymotrypsin + H2O
?
-
poor substrate
-
-
?
chymotrypsinogen + H2O
?
-
maleylated and performate-oxidized bovine chymotrypsinogen A is hydrolyzed at the Arg230-Val231 bond and at the Arg15-Ile16 bond
-
-
?
D-cyclohexyl-Gly-L-Pro-L-Arg-4-nitroanilide + H2O
D-cyclohexyl-Gly-L-Pro-L-Arg + 4-nitroaniline
-
-
-
-
?
D-hexahydrotyrosol-L-Ala-L-Arg-4-nitroanilide + H2O
D-hexahydrotyrosol-L-Ala-L-Arg + 4-nitroaniline
-
-
-
-
?
D-hexahydrotyrosyl-L-alanyl-L-arginine-4-nitroanilide + H2O
D-hexahydrotyrosyl-L-alanyl-L-arginine + 4-nitroaniline
-
synthetic chromogenic substrate
-
?
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
-
synthetic substrate S2238
-
-
?
D-phenylalanyl-L-pipecolyl-L-arginine-4-nitroanilide + H2O
D-phenylalanyl-L-pipecolyl-L-arginine + 4-nitroaniline
-
-
-
-
?
dimethylsulfonyl-D-norleucine-Gly-Arg-4-nitroanilide + H2O
dimethylsulfonyl-D-norleucine-Gly-Arg + 4-nitroaniline
-
-
-
?
factor VII + H2O
?
-
cleavage of two bonds, rapid cleavage of an Arg-Ile bond and slower cleavage of an Y-Gly bond
-
-
?
factor VIII + H2O
?
-
factor Xa proteolytically activates Factor VIII by cleaving P1 residues Arg372, Arg740, and Arg1689. Factor Xa also catalyzes inactivating cleavages that occur on a slower time scale than the activating ones
-
-
?
factor VIII + H2O
activated factor VIII + B domain
factor X + H2O
?
-
cleavage of three bonds
-
-
?
FPR-prothrombin + H2O
meizothrombin
-
i.e. prothrombin specifically active site-labeled with D-Phe-Pro-Arg-CH2Cl is cleaved by prothrombinase to intermediate meizothrombin, but the reaction is then directed to formation of a different FPR-prothrombin 2 intermediate product
-
-
?
FPR-prothrombin + H2O
meizothrombin + ?
-
i.e. prothrombin specifically active site-labeled with D-Phe-Pro-Arg-CH2Cl and AF660-labeled, is cleaved by prothrombinase to intermediate meizothrombin, but the reaction is then directed to formation of a different FPR-prothrombin 2 intermediate product
-
-
?
fragment 1.2:prethrombin-2 + H2O
thrombin
-
intermediate of prothrombin processing to thrombin, cleavage site is Arg320
-
?
GPRFFL + H2O
GPR + FFL
-
best substrate
-
?
L-Arg-Gly-Arg-4-nitroanilide + H2O
L-Arg-Gly-Arg + 4-nitroaniline
L-Arg-Gly-L-Arg-4-nitroanilide + H2O
L-Arg-Gly-L-Arg + 4-nitroaniline
meizothrombin + H2O
thrombin
-
intermediate of prothrombin processing to thrombin, cleavage site is Arg271
-
?
methoxycarbonyl-D-cyclohexylglycyl-Gly-L-Arg-4-nitroanilide + H2O
methoxycarbonyl-D-cyclohexylglycyl-Gly-L-Arg + 4-nitroaniline
-
-
-
-
?
methoxycarbonyl-D-cyclohexylglycyl-glycyl-L-ariginine-4-nitroanilide + H2O
methoxycarbonyl-D-cyclohexylglycyl-glycyl-L-ariginine + 4-nitroaniline
-
i.e. Spectrozyme fXa, SpfXa
-
?
methoxycarbonylcyclohexyl-Gly-Gly-L-Arg-4-nitroanilide + H2O
methoxycarbonylcyclohexyl-Gly-Gly-L-Arg + 4-nitroaniline
-
-
-
-
?
N-2-benzyloxycarbonyl-D-arginyl-L-arginine-4-nitroanilide + H2O
N-2-benzyloxycarbonyl-D-arginyl-L-arginine + 4-nitroaniline
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine + 4-nitroaniline
N-alpha-benzyloxycarbonyl-Ile-Glu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-Ile-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
N-benzoyl-Arg-4-nitroanilide + H2O
N-benzoyl-Arg + 4-nitroaniline
-
-
-
?
N-benzoyl-Ile-Glu-Gly-Arg-4-nitroanilide + H2O
N-benzoyl-Ile-Glu-Gly-Arg + 4-nitroaniline
-
-
-
?
N6-CBZ-D-Lys-L-Pro-L-Arg-4-nitroanilide + H2O
N6-CBZ-D-Lys-L-Pro-L-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Lys-4-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-L-Lys + 4-nitrophenol
-
-
-
-
?
prethrombin 1 + H2O
thrombin + ?
-
activation of prethrombin 1 is slow with cleavages at residues R320 and R271 occuring with similar rates
-
-
?
prethrombin-1 + H2O
thrombin + ?
-
-
-
-
?
prethrombin-2 + H2O
thrombin-2
-
smallest zymogen form of thrombin containing only the factor Xa cleavage site 2
-
?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
protease-activated receptor 2 + H2O
activated protease-activated receptor 2 + ?
prothrombin + H2O
thrombin + ?
prothrombin + H2O
thrombin + activation peptide
-
-
-
?
prothrombin + H2O
thrombin + propeptide of thrombin
prothrombin + H2O
thrombin + thrombin N-terminal fragment F12
-
at the physiological concentration of prothrombin, thrombin formation results in rapid release of the product into solution due to weak interaction between thrombin and the cleaved N-terminal F12 domain, of which fragment F1 plays an essential role in membrane binding. Thrombin itself interacts with poor affinity with the F12 domain
-
-
?
prothrombin + H2O
thrombin + thrombin propeptide
-
-
-
-
?
prothrombin + H2O
trhombin + ?
ProTS195A + H2O
?
-
the mutant protein also acts as competitive inhibitor of prothrombin activation
-
-
?
recombinant prothrombin R155A/R284A/R271A mutant rMZ-II + H2O
meizothrombin
-
cleavage site is Arg320
reaction intermediate in the reaction with wild-type prothrombin
?
recombinant prothrombin R155A/R284A/R271A/S525C mutant rMZ-II-F + H2O
meizothrombin
-
labeled with fluorescein at Cys525, cleavage site is Arg320
reaction intermediate in the reaction with wild-type prothrombin
?
recombinant prothrombin R155A/R284A/R320A mutant rP2-II + H2O
fragment 1.2:prethrombin-2
-
cleavage site is Arg271
reaction intermediate in the reaction with wild-type prothrombin
?
recombinant prothrombin S525C mutant + H2O
thrombin
-
labeled with fluorescein at Cys525, cleavage sites are Arg271 and Arg320
-
?
S-2765 + H2O
Z-D-Arg-Gly-L-Arg + 4-nitroaniline
-
-
-
-
?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tosyl-glycyl-prolyl-D-arginine-4-nitroanilide + H2O
tosyl-glycyl-prolyl-D-arginine + 4-nitroaniline
-
i.e. Chz-TH, synthetic chromogenic substrate
-
?
Trypsinogen + H2O
?
-
maleylated performate-oxidized trypsinogen, slowly hydrolyzed at the Arg117-Val118 bond
-
-
?
Z-D-Arg-Gly-Arg-4-nitroanilide + H2O
Z-D-Arg-Gly-Arg + 4-nitroaniline
Z-D-Arg-Gly-L-Arg-4-nitroanilide + H2O
Z-D-Arg-Gly-L-Arg + 4-nitroaniline
additional information
?
-
activated factor VIII + H2O
factor VIII
-
proteolytic inactivation
-
-
?
activated factor VIII + H2O
factor VIII
-
inactivation by cleavage at Arg336 and Lys36 of domain A1, low activity
-
-
?
Arg-Gly-Arg-4-nitroanilide + H2O
Arg-Gly-Arg + 4-nitroaniline
-
-
-
-
?
Arg-Gly-Arg-4-nitroanilide + H2O
Arg-Gly-Arg + 4-nitroaniline
-
synthetic substrate S2765
-
-
?
Arg-Gly-Arg-4-nitroanilide + H2O
Arg-Gly-Arg + 4-nitroaniline
-
-
-
-
?
Arg-Gly-Arg-4-nitroanilide + H2O
Arg-Gly-Arg + 4-nitroaniline
-
-
-
-
?
benzoyl-Ile-Glu(gamma-O-methyl)-Gly-Arg-4-nitroanilide + N-benzoyl-Ile-Glu-Gly-Arg-4-nitroanilide + H2O
benzoyl-Ile-Glu(gamma-O-methyl)-Gly-Arg + N-benzoyl-Ile-Glu-Gly-Arg + 4-nitroaniline
-
i.e. S2222, substrate is a 1:1 mixture of the 2 components
-
?
benzoyl-Ile-Glu(gamma-O-methyl)-Gly-Arg-4-nitroanilide + N-benzoyl-Ile-Glu-Gly-Arg-4-nitroanilide + H2O
benzoyl-Ile-Glu(gamma-O-methyl)-Gly-Arg + N-benzoyl-Ile-Glu-Gly-Arg + 4-nitroaniline
-
mixed substrate
-
-
?
benzoyl-Ile-Glu(gamma-O-methyl)-Gly-Arg-4-nitroanilide + N-benzoyl-Ile-Glu-Gly-Arg-4-nitroanilide + H2O
benzoyl-Ile-Glu(gamma-O-methyl)-Gly-Arg + N-benzoyl-Ile-Glu-Gly-Arg + 4-nitroaniline
-
mixed substrate S2222
-
-
?
benzoyl-Ile-Glu(gamma-O-methyl)-Gly-Arg-4-nitroanilide + N-benzoyl-Ile-Glu-Gly-Arg-4-nitroanilide + H2O
benzoyl-Ile-Glu(gamma-O-methyl)-Gly-Arg + N-benzoyl-Ile-Glu-Gly-Arg + 4-nitroaniline
-
mixed substrate
-
-
?
benzoyl-Ile-Glu(gamma-O-methyl)-Gly-Arg-4-nitroanilide + N-benzoyl-Ile-Glu-Gly-Arg-4-nitroanilide + H2O
benzoyl-Ile-Glu(gamma-O-methyl)-Gly-Arg + N-benzoyl-Ile-Glu-Gly-Arg + 4-nitroaniline
-
mixed substrate
-
-
?
Boc-L-Asp(OBzl)-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
Boc-L-Asp(OBzl)-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
I-1560
-
-
?
Boc-L-Asp(OBzl)-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
Boc-L-Asp(OBzl)-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
I-1560
-
-
?
factor VIII + H2O
activated factor VIII + B domain
-
proteolytic activation by removal of the B domain
-
-
?
factor VIII + H2O
activated factor VIII + B domain
-
activation by cleavage at Arg1689 and Arg1721 of domain A3
-
-
?
FS-2765 + H2O
?
-
FS-2765 is a fluorescent peptidyl substrate, factor Xa
-
-
?
FS-2765 + H2O
?
-
FS-2765 is a fluorescent peptidyl substrate, prothrombinase
-
-
?
L-Arg-Gly-Arg-4-nitroanilide + H2O
L-Arg-Gly-Arg + 4-nitroaniline
-
chromogenic substrate
-
?
L-Arg-Gly-Arg-4-nitroanilide + H2O
L-Arg-Gly-Arg + 4-nitroaniline
-
chromogenic synthetic substrate S2765
-
?
L-Arg-Gly-Arg-4-nitroanilide + H2O
L-Arg-Gly-Arg + 4-nitroaniline
-
chromogenic synthetic substrate S2765
-
?
L-Arg-Gly-L-Arg-4-nitroanilide + H2O
L-Arg-Gly-L-Arg + 4-nitroaniline
-
-
-
-
?
L-Arg-Gly-L-Arg-4-nitroanilide + H2O
L-Arg-Gly-L-Arg + 4-nitroaniline
-
-
-
-
?
L-Arg-Gly-L-Arg-4-nitroanilide + H2O
L-Arg-Gly-L-Arg + 4-nitroaniline
-
-
-
-
?
L-Arg-Gly-L-Arg-4-nitroanilide + H2O
L-Arg-Gly-L-Arg + 4-nitroaniline
-
-
-
-
?
N-2-benzyloxycarbonyl-D-arginyl-L-arginine-4-nitroanilide + H2O
N-2-benzyloxycarbonyl-D-arginyl-L-arginine + 4-nitroaniline
-
-
-
-
?
N-2-benzyloxycarbonyl-D-arginyl-L-arginine-4-nitroanilide + H2O
N-2-benzyloxycarbonyl-D-arginyl-L-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine + 4-nitroaniline
-
i.e. S-2765, synthetic chromogenic substrate
-
?
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine + 4-nitroaniline
-
i.e. S2765
-
?
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine + 4-nitroaniline
-
i.e. S-2765, synthetic chromogenic substrate
-
?
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine + 4-nitroaniline
-
i.e. S-2765, synthetic fluorogenic substrate
-
?
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine + 4-nitroaniline
-
i.e. S2765
-
?
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine + 4-nitroaniline
-
i.e. S2765
-
?
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzyloxycarbonyl-D-arginyl-glycyl-L-arginine + 4-nitroaniline
-
i.e. Spectrozyme FXa, synthetic chromogenic substrate
-
?
Prethrombin 2 + H2O
?
-
-
-
?
Prethrombin 2 + H2O
?
-
-
-
-
?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
-
-
-
-
?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
-
PAR-1 activation mediates activation of phospholipase C in endothelial cells
-
-
?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
-
-
-
-
?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
-
PAR-1 activation mediates activation of phospholipase C in endothelial cells
-
-
?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
-
-
-
-
?
protease-activated receptor 2 + H2O
activated protease-activated receptor 2 + ?
-
-
-
-
?
protease-activated receptor 2 + H2O
activated protease-activated receptor 2 + ?
-
PAR-2 activation mediates activation of phospholipase C in endothelial cells
-
-
?
protease-activated receptor 2 + H2O
activated protease-activated receptor 2 + ?
-
-
-
-
?
protease-activated receptor 2 + H2O
activated protease-activated receptor 2 + ?
-
PAR-2 activation mediates activation of phospholipase C in endothelial cells
-
-
?
protease-activated receptor 2 + H2O
activated protease-activated receptor 2 + ?
-
-
-
-
?
prothrombin + H2O
?
-
major role is the activation of prothrombin
-
-
?
prothrombin + H2O
?
-
factor Xaalpha is predominantly responsible for thrombin generation. Slow conversion to factor Xabeta coordinates coagulation and the initiation of fibrinolysis at sites of thrombinase assembly
-
-
?
prothrombin + H2O
?
gamma-carboxylation of prothrombin is required for cleavage
-
-
?
prothrombin + H2O
?
gamma-carboxylation of prothrombin is required for cleavage
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
three major fragments are produced, one of these fragments is the 39000 Da alpha-thrombin
?
prothrombin + H2O
thrombin + ?
-
-
thrombin and two activation fragments
?
prothrombin + H2O
thrombin + ?
-
cleaves first an Arg-Thr bond and then an Arg-Ile bond to form the two-chain enzyme
-
?
prothrombin + H2O
thrombin + ?
-
crucial step in blood coagulation process
-
?
prothrombin + H2O
thrombin + ?
-
a single type of exosite binding interaction drives affinity and binding specificity through the stepwise reactions necessary for the two cleavage reactions of prothrombin activation and product release
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
procoagulant activity
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
665556, 696780, 698769, 699091, 709147, 709211, 710601, 717253, 717829, 752707, 753480, 754844, 754909 -
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
?
prothrombin + H2O
thrombin + ?
-
-
?
prothrombin + H2O
thrombin + ?
-
-
?
prothrombin + H2O
thrombin + ?
-
-
?
prothrombin + H2O
thrombin + ?
-
coupled assay method with measurement of thrombin activity against sythetic chromogenic substrate S2238
-
?
prothrombin + H2O
thrombin + ?
-
hydrolysis of Arg322-Ile323 produces meizothrombin as an intermediate, while hydrolysis of Arg273-Thr274 produces prethrombin 2-fragment 1.2
-
?
prothrombin + H2O
thrombin + ?
-
limited preference for the cleavage site, hydrolyzes two petide bonds in prothrombin having (Glu/Asp)-Gly-Arg-(Thr/Ile) as P3-P2-P1-P1' residues, glycine is not the best P2-residue, phenylalanine shows even higher activity at this position
-
?
prothrombin + H2O
thrombin + ?
-
the cleavage site 2 is preferred to cleavage site 1
-
?
prothrombin + H2O
thrombin + ?
-
wild-type II, cleavage sites are Arg271 and Arg320
-
?
prothrombin + H2O
thrombin + ?
-
acts within the prothrombinase complex
-
?
prothrombin + H2O
thrombin + ?
-
enzyme is involved in thrombotic complications of artherosclerosis and following diseases, overview
-
?
prothrombin + H2O
thrombin + ?
-
enzyme is responsible for the proteolysis of prothrombin to catalytically active thrombin
-
?
prothrombin + H2O
thrombin + ?
-
enzyme plays a key role in thrombosis and hemostasis by cleaving prothrombin to thrombin and thereby regulating the generation of this vital procoagulant enzyme, thrombus formation causes diseases like arterial restenosis, induces mitogenic signaling via binding to effector cell protease receptor-1, i.e. EPR-1, on cell surfaces, and via release of platelet-derived growth factor PDGF in aortic smooth-muscle cells
-
?
prothrombin + H2O
thrombin + ?
-
initial step in thrombus formation
-
?
prothrombin + H2O
thrombin + ?
-
key enzyme in coagulation cascade responsible for the generation of thrombin by limited proteolysis of its zymogen prothrombin
-
?
prothrombin + H2O
thrombin + ?
-
procoagulant activity
-
?
prothrombin + H2O
thrombin + ?
-
prothrombin activation requires proteolysis of 2 bonds and thus involves 2 possible activation pathways, parallel-sequential activation model
-
?
prothrombin + H2O
thrombin + ?
-
activation
-
-
?
prothrombin + H2O
thrombin + ?
-
binding of substrate in two conformations to human prothrombinase drives consecutive cleavage at two sites in prothrombin
-
-
?
prothrombin + H2O
thrombin + ?
-
prothrombinase
-
-
?
prothrombin + H2O
thrombin + ?
-
cleavage at Arg320 followed by cleavage at Arg271
-
-
?
prothrombin + H2O
thrombin + ?
-
the interaction of factor Xa with factor Va on membranes to form prothrombinase profoundly increases the rate of the proteolytic conversion of prothrombin to thrombin
-
-
?
prothrombin + H2O
thrombin + ?
-
cleavage at Arg320 followed by cleavage at Arg271. Enzyme activity and active site docking with wild-type prothrombin and cleavage site variants, in which the cleavage sequence Asp-Gly-Arg is replaced e.g. by Arg-Gly-Arg or Arg-Arg, overview. Product identification, overview
-
-
?
prothrombin + H2O
thrombin + ?
-
activation, a first cleavage of prothrombin by prothrombinase at Arg320 produces the active intermediate meizothrombin, while the second cleavage at Arg271 produces thrombin
-
-
?
prothrombin + H2O
thrombin + ?
-
activation, interaction of factor Xa with factor Va promotes prothrombin activation
-
-
?
prothrombin + H2O
thrombin + ?
-
prothrombinase cleaves prothrombin at two cleavage positions Arg-271-Thr-272 and Arg-320-Ile-321
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
-
?
prothrombin + H2O
thrombin + ?
-
the recombinantly expressed enzyme is inactive in Sf9 cells, activity can be restored by addition of phosphatidyl-L-serine, and further enhanced by addition of factor Va and Ca2+
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
enzyme plays a key role in thrombosis and hemostasis by cleaving prothrombin to thrombin and thereby regulating the generation of this vital procoagulant enzyme, thrombus formation causes diseases like arterial restenosis, induces mitogenic signaling via binding to effector cell protease receptor-1, i.e. EPR-1, on cell surfaces
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
enzyme plays a key role in thrombosis and hemostasis by cleaving prothrombin to thrombin and thereby regulating the generation of this vital procoagulant enzyme, thrombus formation causes diseases like arterial restenosis, induces mitogenic signaling via binding to effector cell protease receptor-1, i.e. EPR-1, on cell surfaces, and via release of platelet-derived growth factor PDGF in aortic smooth-muscle cells
-
?
prothrombin + H2O
thrombin + ?
-
initial step in thrombus formation
-
?
prothrombin + H2O
thrombin + ?
-
-
-
?
prothrombin + H2O
thrombin + ?
-
enzyme plays a key role in thrombosis and hemostasis by cleaving prothrombin to thrombin and thereby regulating the generation of this vital procoagulant enzyme, thrombus formation causes diseases like arterial restenosis, induces mitogenic signaling via binding to effector cell protease receptor-1, i.e. EPR-1, on cell surfaces
-
?
prothrombin + H2O
thrombin + propeptide of thrombin
-
-
-
-
?
prothrombin + H2O
thrombin + propeptide of thrombin
-
proteolytic activation
-
-
?
prothrombin + H2O
thrombin + propeptide of thrombin
-
-
-
-
?
prothrombin + H2O
thrombin + propeptide of thrombin
-
factor V is a cofactor for the prothrombin activation by factor Xa
-
-
?
prothrombin + H2O
trhombin + ?
-
-
-
-
?
prothrombin + H2O
trhombin + ?
-
-
-
-
?
prothrombin + H2O
trhombin + ?
-
-
-
-
?
S2222 + H2O
?
-
-
-
-
?
S2222 + H2O
?
-
chromogenic synthetic peptide substrate
-
?
S2222 + H2O
?
-
chromogenic synthetic peptide substrate
-
?
S2222 + H2O
?
-
a chromogenic substrate
-
-
?
S2238 + H2O
?
-
-
-
-
?
S2238 + H2O
?
-
chromogenic synthetic peptide substrate
-
?
Z-D-Arg-Gly-Arg-4-nitroanilide + H2O
Z-D-Arg-Gly-Arg + 4-nitroaniline
-
-
-
-
?
Z-D-Arg-Gly-Arg-4-nitroanilide + H2O
Z-D-Arg-Gly-Arg + 4-nitroaniline
i.e S2765
-
-
?
Z-D-Arg-Gly-L-Arg-4-nitroanilide + H2O
Z-D-Arg-Gly-L-Arg + 4-nitroaniline
-
-
-
-
?
Z-D-Arg-Gly-L-Arg-4-nitroanilide + H2O
Z-D-Arg-Gly-L-Arg + 4-nitroaniline
-
i.e. S-2765
-
-
?
additional information
?
-
-
substrate specificity study for the positions P'1, P'2, and P'3 with 57 substrates possesssing Gly-Pro-Arg at positions P1-P3, the P'2 position shows the highest selectivity, while the P'3 position is not selective at all, overview
-
?
additional information
?
-
-
factor Xa and thrombin evoke additive calcium and proinflammatory responses in endothelial cells subjected to coagulation, overview
-
-
?
additional information
?
-
-
selection of cleavage substrates by substrate phage display and construction of computational molecular models for enzyme-substrate complexes. Binding modes of substrates vary according to the substrate peptide sequence with at least three different substrate-enzyme recognition modes. Three binding modes corresponding to the aryl-binding site accommodating the P4, P3, and P2 side chains, respectively, are likely to account for the specificity of factor Xa toward substrate peptide sequences
-
-
?
additional information
?
-
-
the enzyme is responsible for clot-associated procoagulant activity
-
?
additional information
?
-
-
enzyme possesses a macromolecular substrate binding site, exosite
-
?
additional information
?
-
-
substrate specificity and catalytic efficiency, catalytic groove structure, activity with peptide substrate is virtually the same in presence or absence of complexed factor Va, indicating that the factor Va does not allosterically control the catalytic groove, catalytic efficacy of prothrombinase complex originates from exosite interactions with factor Va and/or prothrombin
-
?
additional information
?
-
-
substrate specificity, no activity with a substrate containing the active site sequence of the Bauhinia variegata trypsin inhibitor BvTI
-
?
additional information
?
-
enzyme is involved in the coagulation cascade
-
?
additional information
?
-
-
enzyme is involved in the coagulation cascade
-
?
additional information
?
-
-
enzyme link between cancer and thrombosis appears to be a bidirectional relationship, physiological role of factor Xa, involvement in inflammation and diseases, physiological interactions, regulation, overview
-
?
additional information
?
-
-
properties of and indications for different enzyme inhibitors, overview, the enzyme is responsible for clot-associated procoagulant activity, enzyme inhibition lead to reduced platelet deposition and aggregation at thrombic sites
-
?
additional information
?
-
-
the enzyme is regulated by sequential occupancy of a pair of linked lipid binding sites, each of which have different minimum ligand structural requirements to induce structural changes
-
?
additional information
?
-
-
factor Xa can induce mesangial cell proliferation through the activation of extracellular regulated kinase via protease-activated receptor 2 in mesangial cells. Protease-activated receptor 2 may play a crucial role in the cell proliferation induced by factor Xa
-
-
?
additional information
?
-
-
blood clot elongation is regulated by factor Xa formation by intrinsic tenase, i.e. factor VIIa and tissue factor complex, coagulation factors from plasma bind to tissue factor TF-expressing cells, become activated, dissociate, and diffuse into plasma to form enzymatic complexes on the membranes of activated platelets, overview
-
-
?
additional information
?
-
-
coagulation factor Xa is a serine protease that plays a crucial role during blood coagulation by converting prothrombin into thrombin, it drives tumor cells of epithelial, but not endothelial, origin into apoptosis through BH3-only protein Bim up-regulation, and enhances fibroblast survival, overview, signaling through protease-activated receptor 1, PAR-1, with rapid and transient desensitization of PAR-1 signaling, signaling pathway, overview
-
-
?
additional information
?
-
different anticoagulant mechanisms, overview
-
-
?
additional information
?
-
-
different anticoagulant mechanisms, overview
-
-
?
additional information
?
-
-
factor Xa and thrombin evoke additive calcium and proinflammatory responses in endothelial cells subjected to coagulation, overview
-
-
?
additional information
?
-
-
factor Xa inhibits the inhibition of the procoagulant function of activated factor V by activated protein C through proteolytic cleavages at Arg506, with a half-maximum inhibition of 2 nM, while the cleavage at Arg306, and Arg679 is not protected, protein S counteracted the inhibition by FXa of the Arg506 cleavage, whereas protein S and FXa yielded additive stimulatory effect of the cleavage at Arg306, activity with recombinant FVa Q306/Q679 and FVa Q506/Q679 variants, interaction analysis with 1.5-dansyl-Glu-Gly-Arg-inhibited factor Xa, overview
-
-
?
additional information
?
-
-
PD0313052 and argatroban, inhibitors of blood coagulation factors Xa and IIa, synergize to reduce thrombus weight and thrombin generation in vivo and in vitro
-
-
?
additional information
?
-
-
structural basis for Na+ specificity of enzymes involved in the coagulation cascade, overview
-
-
?
additional information
?
-
-
annexin 2 acts as a receptor for factor Xa on the cell surface. It facilitates factor Xa activation of receptor PAR-1 but does not enhance coagulant function of factor Xa. Overexpression of tissue factor abolishes annexin 2 dependence on factor Xa signaling and diminishes binding to cell surface annexin 2, whereas selectively abolishing tissue factor promotes the annexin 2/factor Xa interaction
-
-
?
additional information
?
-
-
treatment with factor Xa markedly diminishes the migration of different cancer cell lines from breast, lung and colon. Factor Xa mediates inhibition of cancer cell migration specifically and dose dependently. It acts via protease-activated receptor-1 dependent signaling. The G protein alpha 1 pathway is not involved in signaling
-
-
?
additional information
?
-
-
construction of computational molecular models for enzyme-substrate complexes. Binding modes of substrates vary according to the substrate peptide sequence with at least three different substrate-enzyme recognition modes. Three binding modes corresponding to the aryl-binding site accommodating the P4, P3, and P2 side chains, respectively, are likely to account for the specificity of factor Xa toward substrate peptide sequences
-
-
?
additional information
?
-
-
coagulation factor Xa inhibits cancer cell migration via LIMK1-mediated cofilin inactivation through induction of myosin light chain phosphorylation and LIMK1 activation, overview
-
-
?
additional information
?
-
-
effects of factor X on the respiratory function and asthmatic response in mice, factor X transcript levels and factor Xa activity are increased in lungs of asthmatic mice leading to a significant decrease in the thickness of the mucosal layer and in lung collagen deposition, factor Xa modulates airway remodeling, overview
-
-
?
additional information
?
-
-
enzyme elicits a signaling response in C2C12 and NIH-3T3 fibroblast cells. ERK1/2 phosphorylation by factor Xa is dependent on protease-activated receptor PAR-2 cleavage and leads to fibroblast proliferation, migration, and differentiation into myofibroblasts
-
-
?
additional information
?
-
-
enzyme link between cancer and thrombosis appears to be a bidirectional relationship, physiological role of factor Xa, involvement in inflammation and diseases, physiological interactions, regulation, overview
-
?
additional information
?
-
recombinant oscutarin cannot efficiently generate thrombin without additional protein cofactors
-
-
?
additional information
?
-
-
recombinant oscutarin cannot efficiently generate thrombin without additional protein cofactors
-
-
?
additional information
?
-
-
enzyme link between cancer and thrombosis appears to be a bidirectional relationship, physiological role of factor Xa, involvement in inflammation and diseases, physiological interactions, regulation, overview
-
?
additional information
?
-
-
roles of coagulation pathway and factor Xa in rat mesangioproliferative glomerulonephritis, initiation of the extrinsic coagulation pathway by activating coagulation factor X to factor Xa, factor Xa promote the proliferation of mesangial cells in culture, enzyme inhibitor DX-9065a treatment significantly ameliorated proteinuria in vivo in rats with a a significant reduction in the size of glomeruli, the total number of glomerular cells, and crescent formation, as well as abolishing phosphorylation of p44/42 MAP kinase on day 8, overview
-
-
?
additional information
?
-
-
enzyme link between cancer and thrombosis appears to be a bidirectional relationship, physiological role of factor Xa, involvement in inflammation and diseases, physiological interactions, regulation, overview
-
?
additional information
?
-
recombinant trocarin cannot efficiently generate thrombin without additional protein cofactors
-
-
?
additional information
?
-
-
recombinant trocarin cannot efficiently generate thrombin without additional protein cofactors
-
-
?