3.4.22.26: cancer procoagulant
This is an abbreviated version!
For detailed information about cancer procoagulant, go to the full flat file.
Word Map on EC 3.4.22.26
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3.4.22.26
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coagulation
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proteinase
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thromboembolic
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clot
-
thrombosis
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intravascular
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gordon
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amnion-chorion
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hypercoagulability
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thrombin-antithrombin
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thrombogenic
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three-stage
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prothrombotic
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warfarin
-
benson
-
anti-cp
-
k-dependent
-
haemostatic
-
x-activating
-
medicine
- 3.4.22.26
- coagulation
- proteinase
-
thromboembolic
- clot
- thrombosis
-
intravascular
-
gordon
-
amnion-chorion
- hypercoagulability
-
thrombin-antithrombin
-
thrombogenic
-
three-stage
-
prothrombotic
- warfarin
-
benson
-
anti-cp
-
k-dependent
-
haemostatic
-
x-activating
- medicine
Reaction
specific cleavage of Arg-/-Ile bond in Factor X to form Factor Xa =
Synonyms
cancer procoagulant, CP
ECTree
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Substrates Products
Substrates Products on EC 3.4.22.26 - cancer procoagulant
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REACTION DIAGRAM
7-methoxycoumarin-4-acetyl-GYPGQV + H2O
7-methoxycoumarin-4-acetate + GYPGQV
-
-
-
-
?
7-methoxycoumarin-4-acetyl-IVGGQE + H2O
7-methoxycoumarin-4-acetate + IVGGQE
-
-
-
-
?
7-methoxycoumarin-4-acetyl-SFLLRN + H2O
7-methoxycoumarin-4-acetate + SFLLRN
-
-
-
-
?
7-methoxycoumarin-4-acetyl-VSQKSP + H2O
7-methoxycoumarin-4-acetate + VSQKSP
-
-
-
-
?
7-methoxycoumarin-4-acetyl-VYQPQP + H2O
7-methoxycoumarin-4-acetate + VYQPQP
-
-
-
-
?
AVSQSKP-7-amido-4-methylcoumarin + H2O
AVSQSKP + 7-amino-4-methylcoumarin
-
low activity
-
-
?
AVYQPQP-7-amido-4-methylcoumarin + H2O
AVYQPQP + 7-amino-4-methylcoumarin
-
low activity
-
-
?
benzyloxycarbonyl-Arg-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Arg-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Leu-Pro-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Leu-Pro-Arg + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Val-Pro-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Val-Pro-Arg + 4-nitroaniline
-
-
-
?
Bz-Ile-Glu-Arg-4-nitroanilide + H2O
Bz-Ile-Glu-Arg + 4-nitroaniline
-
chromogenic commercial substrate
-
-
?
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
-
-
-
?
Fibronectin + H2O
?
-
enzyme CP cleaves fibronectin between Ala and Val residues, in regions rich in Pro and Gln residues. The 45 and 60 kDa fragments have the same N-terminal sequence, generated by cleavage of the bond between Ala292 and Val293
-
-
?
GDR-7-amido-4-methylcoumarin + H2O
GDR + 7-amino-4-methylcoumarin
-
low activity
-
-
?
Glu-Glu-Phe-Lys-4-nitroanilide + H2O
Glu-Glu-Phe-Lys + 4-nitroaniline
-
-
-
?
methylsulfonyl-D-cyclohexylalanyl-butyl-Arg-4-nitroanilide + H2O
methylsulfonyl-D-cyclohexylalanyl-butyl-Arg + 4-nitroaniline
-
-
-
?
PKSQSVA-7-amido-4-methylcoumarin + H2O
PKSQSVA + 7-amino-4-methylcoumarin
-
low activity
-
-
?
PQPQYVA-7-amido-4-methylcoumarin + H2O
PQPQYVA + 7-amino-4-methylcoumarin
-
low activity
-
-
?
RGD-7-amido-4-methylcoumarin + H2O
RGD + 7-amino-4-methylcoumarin
-
low activity
-
-
?
sarcosyl-Pro-Arg-4-nitroanilide + H2O
sarcosyl-Pro-Arg + 4-nitroaniline
-
-
-
?
tert-butoxycarbonyl-AVR-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-AVR + 7-amino-4-methylcoumarin
-
high activity
-
-
?
tert-butoxycarbonyl-AVYQPQP-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-AVYQPQP + 7-amino-4-methylcoumarin
-
high activity
-
-
?
tert-butoxycarbonyl-GDR-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-GDR + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-PKSQSVA-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-PKSQSVA + 7-amino-4-methylcoumarin
-
low activity
-
-
?
tert-butoxycarbonyl-PQPQYVA-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-PQPQYVA + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-PQVR-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-PQVR + 7-amino-4-methylcoumarin
-
best substrate, this substrate is also cleaved by collagenase
-
-
?
tert-butoxycarbonyl-QVR-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-QVR + 7-amino-4-methylcoumarin
tert-butoxycarbonyl-RGD-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-RGD + 7-amino-4-methylcoumarin
-
-
-
-
?
D-Ala-Pro-Arg + 4-nitroaniline
-
-
-
?
D-Ala-Pro-Arg-4-nitroanilide + H2O
D-Ala-Pro-Arg + 4-nitroaniline
-
-
-
?
D-Ile-Pro-Arg + 4-nitroaniline
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
-
-
?
factor X + H2O
?
-
that triggers blood coagulation by directly activating factor X in the absence of factor VII
-
-
?
factor X + H2O
?
-
that triggers blood coagulation by directly activating factor X in the absence of factor VII
-
-
?
factor X + H2O
factor Xa
-
cleavage of Arg-Ile bond in factor X heavy chain
-
?
factor X + H2O
factor Xa
-
cleavage of Arg-Ile bond in factor X heavy chain, activation of the coaglutation factor X and thereby activation of the plasma blood clotting cascade
-
?
factor X + H2O
factor Xa
-
cleavage of Arg-Ile bond, activation of the coaglutation factor X
-
?
factor X + H2O
factor Xa
-
cleavage of Arg-Ile bond in factor X heavy chain, activation of the coaglutation factor X and thereby activation of the plasma blood clotting cascade
-
?
Factor X + H2O
Factor Xa + ?
-
primary cleavage site: Tyr21-Asp22, secondary sites: Asp14-Ser15 and Thr18-Glu19
-
?
Factor X + H2O
Factor Xa + ?
-
primary cleavage site: Tyr21-Asp22, secondary sites: Asp14-Ser15 and Thr18-Glu19
-
?
Glu-Glu-Pro-Arg + 4-nitroaniline
-
-
-
?
Glu-Glu-Pro-Arg-4-nitroanilide + H2O
Glu-Glu-Pro-Arg + 4-nitroaniline
-
-
-
?
active factor Xa + ?
-
activation of blood coagulation factor X
-
-
?
inactive factor X + H2O
active factor Xa + ?
-
activation of blood coagulation factor X, degradation of factor X during 24 h
-
-
?
inactive factor X + H2O
active factor Xa + ?
-
activation of blood coagulation factor X (57.3 kDa), cleavage of factor X at the conventional activation site, i.e. between Arg52 and Ile53, in the heavy chain
-
-
?
inactive factor X + H2O
active factor Xa + ?
-
activation of blood coagulation factor X
-
-
?
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Lys + 4-nitroaniline
-
-
-
?
PAR-1 receptor + H2O
?
-
enzyme competes with thrombin for the same protease-activated receptor, i.e. PAR-1, on the blood platelet surface
-
?
PQVR-7-amido-4-methylcoumarin + H2O
PQVR + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-QVR + 7-amino-4-methylcoumarin
-
best synthetic substrate
-
-
?
tert-butoxycarbonyl-QVR-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-QVR + 7-amino-4-methylcoumarin
-
high activity
-
-
?
additional information
?
-
-
substrate recognition depends on the secondary and tertiary configuration of the protein substrate rather than on the primary sequence alone, no activity with substrates containing the sequence Xaa-Lys-ProP2-TyrP1-
-
?
additional information
?
-
-
enzyme seems to be regulated allosterically
-
?
additional information
?
-
-
the activity of cancer procoagulant in cases of uterine leiomyomas, overview
-
-
?
additional information
?
-
-
the enzyme is able to stimulate blood platelet adhesion to fibrinogen and collagen, which can also play a role in metastatic spread of cancer as well as primary tumor growth
-
-
?
additional information
?
-
-
the enzyme plays a role in pathogenesis of cancer-related thrombosis, the enzyme concentration in serum is positively correlated to fibrinogen concentration, but negatively correlated to free protein S plasma content, determination of prothrobotic parameters and correlation to enzyme activity, overview
-
-
?
additional information
?
-
-
the enzyme is a cysteine protease, the enzyme mediates growth and adhesion of MCF-7 cancer cells to vitronectin in vitro
-
-
?
additional information
?
-
-
high level of cancer procoagulant is a risk factor for multiple myeloma
-
-
?
additional information
?
-
-
substrate specificity analysis, mass spectrometric detection of cleavage products. No activity with tert-benzyloxycarbonyl-QSPVR-7-amido-4-methylcoumarin and TLDPR-7-amido-4-methylcoumarin. Enzyme CP shows very little cysteine protease activity, it appears to exhibit mixed protease activity, but acts predominantly as a serine protease
-
-
?
additional information
?
-
-
cancer procoagulant is a cysteine protease acting as an activator of coagulation factor X, the protein activates factor X in the absence of tissue factor and factor VII
-
-
?
additional information
?
-
-
rat and human cancer procoagulant activity bind similarly to antiCP antibodies
-
-
?
additional information
?
-
-
in vitro screening of synthetic fluorogenic substrates for detection of cancer procoagulant activity, substrate design, synthesis, and evaluation, e.g. based on the RGD motif of fibronectin, overview. The most reliable assay for the quantification of cancer procoagulant activity is the three-stage chromogenic assay which utilises the ability of cancer procoagulant to activate factor X. In this assay, the activation of factor X leads to the formation of activated thrombin from prothrombin and the eventual hydrolyses of a thrombin chromogenic substrate which contains a p nitroaniline leaving group. No activity with tert-benzyloxycarbonyl-AVSQSKP-7-amido-4-methylcoumarin
-
-
?