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Information on EC 3.4.17.20 - Carboxypeptidase U
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3.4.17.20 Carboxypeptidase USpecify your search results
Word Map
- 3.4.17.20
- plasminogen
- coagulation
- clot
-
fibrinolytic
- thrombosis
- thrombomodulin
- plasmin
- fibrinogen
- pai-1
-
bleeding
- inhibitor-1
-
antifibrinolytic
-
hemostatic
- prothrombin
- zymogen
- venous
-
anticoagulant
- thromboembolism
-
tissue-type
-
d-dimers
-
hypofibrinolysis
-
profibrinolytic
-
thrombolytic
- thrombin-thrombomodulin
-
hypercoagulable
-
procoagulant
- c5a
- antithrombin
- thrombus
-
prothrombotic
-
thrombin-antithrombin
-
thrombin-mediated
- coagulopathy
-
plasmin-antiplasmin
-
haemostasis
- thromboplastin
- medicine
- antiplasmin
- alpha2-antiplasmin
-
fxiii
- metallocarboxypeptidase
- anaphylatoxins
- molecular biology
- pharmacology
-
plasmin-mediated
- thrombophilia
-
thrombelastography
-
activator-induced
-
thrombin-dependent
- rfviia
-
t-pa-induced
-
thrombin-cleaved
-
euglobulin
- diagnostics
The enzyme appears in viruses and cellular organisms
Synonyms
tafia, thrombin-activatable fibrinolysis inhibitor, thrombin activatable fibrinolysis inhibitor, procpu, procarboxypeptidase b, carboxypeptidase u, thrombin-activable fibrinolysis inhibitor, procarboxypeptidase u, carboxypeptidase b2, plasma carboxypeptidase b, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Arginine carboxypeptidase
-
-
-
-
Carboxypeptidase B, pro-
-
-
-
-
Carboxypeptidase R
carboxypeptidase U
Carboxypeptidase-U
-
-
-
-
CPR
CPU
Plasma carboxypeptidase B
plasma CPB
plasma procarboxypeptidase U
pro-pCPB
-
-
-
-
Procarboxypeptidase B
procarboxypeptidase R
procarboxypeptidase U
proCPU
pTAFI
-
-
-
-
rTAFI
-
-
-
-
TAFI
TAFIa
thrombin activatable fibrinolysis inhibitor
Thrombin-activable fibrinolysis inhibitor
-
-
-
-
thrombin-activatable fibrinolysis inhibitor
Carboxypeptidase R
-
-
-
-
CPU
-
-
-
-
Plasma carboxypeptidase B
-
-
-
-
Procarboxypeptidase B
-
-
-
-
TAFI
-
-
-
-
TAFI
-
-
TAFIa
-
-
-
-
TAFIa
-
-
thrombin activatable fibrinolysis inhibitor
-
-
thrombin-activatable fibrinolysis inhibitor
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of C-terminal Arg and Lys from a polypeptide
peptidyl-L-lysine (or L-arginine) + H2O = peptide + L-lysine (or L-arginine)
-
-
-
release of C-terminal Arg and Lys from a polypeptide
catalytic mechanism and substrate specificity
-
release of C-terminal Arg and Lys from a polypeptide
catalytically important residues are G207, I243, I247, S254, and I255, catalytic mechanism and substrate binding
-
release of C-terminal Arg and Lys from a polypeptide
substrate binding involves residues ARg235, Tyr341, and Asn234, while catalysis involves residues Glu363 and ARg217, mechanism of action of TAFI, overview
-
release of C-terminal Arg and Lys from a polypeptide
substrate binding involves residues ARg235, Tyr341, and Asn234, while catalysis involves residues Glu363 and ARg217, mechanism of action of TAFI, overview, Zn2+ is important in the catalytic mechanism
-
release of C-terminal Arg and Lys from a polypeptide
the enzyme prefers C-terminal arginine over lysine
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
156621-18-0
-
37329-68-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ala-Ser-His-Leu-Gly-Leu-Ala-Arg + H2O
Ala-Ser-His-Leu-Gly-Leu-Ala + Arg
-
reaction is much more efficient than reaction with EC 3.4.17.3
-
?
Arg6-Leu5-enkephalin + H2O
Tyr-Gly-Gly-Phe-Leu + Arg
-
i.e. Tyr-Gly-Gly-Phe-Leu-Arg
-
-
?
Arg6-Met5-enkephalin + H2O
Tyr-Gly-Gly-Phe-Met + Arg
-
i.e. Tyr-Gly-Gly-Phe-Met-Arg
-
-
?
biotinyl-(epsilon-aminocaproic acid)-(epsilon-aminocaproic acid)-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Arg-OH + H2O
biotinyl-(epsilon-aminocaproic acid)-(epsilon-aminocaproic acid)-Gly-Leu-Met-Val-Gly-Gly-Val-Val-OH + Arg
-
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
-
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
?
complement component C3a octapeptide + H2O
?
-
removal of terminal arginine, low activity
-
-
?
complement component C5a octapeptide + H2O
?
-
removal of terminal arginine
-
-
?
hippuryl-arginine + H2O
hippuric acid + L-arginine
-
substrate is used to measure the TAFI activation by plasmin
-
-
?
hippuryl-L-arginine + H2O
hippuric acid + L-arginine
-
-
-
-
?
Lys6-Leu5-enkephalin + H2O
Tyr-Gly-Gly-Phe-Leu + Lys
-
i.e. Tyr-Gly-Gly-Phe-Leu-Lys
-
-
?
Lys6-Met5-enkephalin + H2O
Tyr-Gly-Gly-Phe-Met + Lys
-
i.e. Tyr-Gly-Gly-Phe-Met-Lys
-
-
?
N-benzoyl-2'-cyano-L-Phe-L-Arg + H2O
N-benzoyl-2'-cyano-L-Phe + L-Arg
-
selective CPU substrate
-
-
?
N-[3-(2-Furylacryloyl)]-L-Ala-L-Arg + H2O
N-[3-(2-Furylacryloyl)]-L-Ala + L-Arg
-
-
-
-
?
p-anisylazoformyl-L-arginine + H2O
p-anisylazoformic acid + L-arginine
-
substrate is used to measure the TAFI activation by thrombin and thrombin-thrombomodulin
-
-
?
[3-(2-furylacryloyl)]-L-alanyl-L-arginine + H2O
[3-(2-furylacryloyl)]-L-alanine + L-arginine
-
-
-
-
?
[3-(2-furylacryloyl)]-L-phenylalanyl-L-phenylalanine + H2O
[3-(2-furylacryloyl)]-L-phenylalanine + L-phenylalanine
-
-
-
-
?
fibrin + H2O
fibrin + Lys
-
cleavage of C-terminal Lys, regulation, overview
the cleaved fibrin cannot be bound by plasminogen and the plasminogen activator in contrast to the uncleaved fibrin, fibrinolysis and plasmin regulation cycle involving the enzyme, overview
-
?
fibrin + H2O
fibrin + Lys
-
partially degraded fibrin in fibrin clots, cleavage of C-terminal Lys
-
-
?
fibrin + H2O
fibrin + Lys
-
cleavage of C-terminal Lys, regulation, overview
the cleaved fibrin cannot be bound by plasminogen and the plasminogen activator in contrast to the uncleaved fibrin, fibrinolysis and plasmin regulation cycle involving the enzyme, overview
-
?
fibrin + H2O
Lys + ?
-
attenuates clot lysis by removing lysine residues from a fibrin clot
-
?
Fibrin, partially degraded + H2O
?
-
the enzyme suppresses the ability of fibrin to catalyze plasminogen activation and thus delays clot lysis
-
-
?
Fibrin, partially degraded + H2O
?
-
molecular connection between coagulation and fibrinolysis
-
-
?
Fibrin, partially degraded + H2O
Fibrin, partially degraded + L-Lys + L-Arg
-
-
-
?
Fibrin, partially degraded + H2O
Fibrin, partially degraded + L-Lys + L-Arg
-
-
-
?
Fibrin, partially degraded + H2O
Fibrin, partially degraded + L-Lys + L-Arg
-
-
-
?
Fibrin, partially degraded + H2O
Fibrin, partially degraded + L-Lys + L-Arg
-
-
-
-
?
His-Lys-Asp-Met-Gln-Leu-Gly-Arg + H2O
His-Lys-Asp-Met-Gln-Leu-Gly + Arg
-
i.e. C5a, reaction is much more efficient than reaction with EC 3.4.17.3
-
?
His-Lys-Asp-Met-Gln-Leu-Gly-Arg + H2O
His-Lys-Asp-Met-Gln-Leu-Gly + Arg
-
i.e. C5a, the enzyme significantly contributes to the inactivation of C5a, the most potent of the complement derived anaphylatoxins
-
?
N-[3-(2-Furylacryloyl)]-L-Ala-L-Lys + H2O
N-[3-(2-Furylacryloyl)]-L-Ala + L-Lys
-
-
-
?
N-[3-(2-Furylacryloyl)]-L-Ala-L-Lys + H2O
N-[3-(2-Furylacryloyl)]-L-Ala + L-Lys
-
-
-
-
?
additional information
?
-
-
inhibition of the enzyme leads to facilitated induction of coronary artery thrombolysis involving the plasminogen activator
-
-
?
additional information
?
-
-
no substrates are hippuryl-L-Phe, hippurylphenyllactic acid, hippuryl-Gly-Phe
-
-
?
additional information
?
-
-
removal of Lys or Arg from carboxy-terminus of peptides, specific for basic amino acids at carboxy-terminus
-
-
?
additional information
?
-
-
the activated enzyme shows anti-fibrinolytic and fibrin clot lysis activity
-
-
?
additional information
?
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-
the enzyme circulates as inactive zymogen in the blood stream becoming activated upon blood clotting, the enzyme inhibits fibrinolysis by cleaving C-terminal lysine from the surface of partially degraded fibrin, which stimulates the tissue-type plasminogen activator-mediated conversion of plasminogen to plasmin, the enzyme might also be involved in regulation of inflammation and tissue repair, enzyme regulation overview
-
-
?
additional information
?
-
-
the enzyme down-regulates fibrinolysis by removing carboxy-terminal lysine residues, which are ligands for plasminogen and tissue-type plasminogen activator, from partially degraded fibrin, pharmacological profile and pathphysiological role of the enzyme in rat thrombolysis
-
-
?
additional information
?
-
-
the enzyme inhibits fibrinolysis and has a distinct role in haemostasis and a possible risk factor for thrombotic disease involving the polymorphism at position 325, overview, the plasminogen activation system plays a role in enzyme regulation
-
-
?
additional information
?
-
-
the enzyme is involved and important in control of clot stability determined by clot formation and fibrinolysis, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the regulation of the coagulation and fibrinolytic systems preventing blood loss at sites of vessel wall damage and maintainthe fluidity of the blood in the body
-
-
?
additional information
?
-
-
the enzyme is partially accountable for the antifibrinolytic activity in amniotic fluid
-
-
?
additional information
?
-
-
the enzyme might be the primary in vivo regulator of complement component C5a-mediated inflammation in the circulation, the enzyme cleaves terminal lysine from the surface of fibrin clots preventing the binding and activation of plasminogen and inhibiting whole blood clot lysis
-
-
?
additional information
?
-
-
the enzyme, activated by thrombin, protects the fibrin clot against lysis, altered enzyme activity is involved in bleeding and thrombotic disorders, the enzyme is involved in wound healing and inflammation, overview
-
-
?
additional information
?
-
-
thrombin activatable fibrinolysis inhibitor and its fibrinolytic effect in normal pregnancy
-
-
?
additional information
?
-
-
thrombin activatable fibrinolysis inhibitor, TAFI, plays a role in the delicate balance between coagulation and fibrinolysis, the stability of the fibrin clot, inflammation, thrombosis, and in Behcets disease, vascular involvement pattern in patients, overview
-
-
?
additional information
?
-
-
enzyme assay using a specific chromogenic dipeptide substrate
-
-
?
additional information
?
-
-
the enzyme binds alpha2-macroglobulin and pregnancy zone protein, which does not inhibit the enzyme
-
-
?
additional information
?
-
-
the enzyme binds to plasminogen and fibrinogen
-
-
?
additional information
?
-
the effects of the carboxypeptidase U system on the regulation of fibrinolysis is investigated and compared in four different in vitro models of fibrinolysis
-
-
?
additional information
?
-
pro-carboxypeptidase R is an acute phase protein under inflammatory conditions
-
?
additional information
?
-
-
pro-carboxypeptidase R is an acute phase protein under inflammatory conditions
-
?
additional information
?
-
-
the enzyme circulates as inactive zymogen in the blood stream becoming activated upon blood clotting, the enzyme inhibits fibrinolysis by cleaving C-terminal lysine from the surface of partially degraded fibrin, which stimulates the tissue-type plasminogen activator-mediated conversion of plasminogen to plasmin, the enzyme might also be involved in regulation of inflammation and tissue repair, enzyme regulation overview
-
-
?
additional information
?
-
-
the enzyme, activated by thrombin, protects the fibrin clot against lysis, altered enzyme activity is involved in bleeding and thrombotic disorders, the enzyme is involved in wound healing and inflammation, overview
-
-
?
additional information
?
-
-
pro-carboxypeptidase R production is increased under inflammatory conditions
-
?
additional information
?
-
-
the enzyme down-regulates fibrinolysis by removing carboxy-terminal lysine residues, which are ligands for plasminogen and tissue-type plasminogen activator, from partially degraded fibrin, pharmacological profile and pathphysiological role of the enzyme in rat thrombolysis
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
His-Lys-Asp-Met-Gln-Leu-Gly-Arg + H2O
His-Lys-Asp-Met-Gln-Leu-Gly + Arg
-
i.e. C5a, the enzyme significantly contributes to the inactivation of C5a, the most potent of the complement derived anaphylatoxins
-
?
fibrin + H2O
fibrin + Lys
-
cleavage of C-terminal Lys, regulation, overview
the cleaved fibrin cannot be bound by plasminogen and the plasminogen activator in contrast to the uncleaved fibrin, fibrinolysis and plasmin regulation cycle involving the enzyme, overview
-
?
fibrin + H2O
fibrin + Lys
-
partially degraded fibrin in fibrin clots, cleavage of C-terminal Lys
-
-
?
fibrin + H2O
fibrin + Lys
-
cleavage of C-terminal Lys, regulation, overview
the cleaved fibrin cannot be bound by plasminogen and the plasminogen activator in contrast to the uncleaved fibrin, fibrinolysis and plasmin regulation cycle involving the enzyme, overview
-
?