3.4.21.69: Protein C (activated)
This is an abbreviated version!
For detailed information about Protein C (activated), go to the full flat file.
Word Map on EC 3.4.21.69
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3.4.21.69
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thrombosis
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venous
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leiden
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sepsis
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endothelial
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antithrombin
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thromboembolism
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thrombophilia
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clot
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thrombomodulin
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platelet
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procoagulant
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heparin
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arterial
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vein
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bleeding
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plasminogen
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hypercoagulable
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thromboplastin
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lupus
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fibrinogen
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fibrinolysis
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hemostatic
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viiia
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epcr
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intravascular
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contraceptive
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antiphospholipid
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antithrombotic
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prothrombotic
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fibrin
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k-dependent
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anticardiolipin
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d-dimers
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coagulopathy
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embolism
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prothrombinase
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amidolytic
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thrombin-antithrombin
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haemostasis
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par1
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profibrinolytic
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pharmacology
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goal-directed
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diagnostics
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drug development
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gamma-carboxyglutamic
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deep-vein
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time-based
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tafi
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hypofibrinolysis
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thromboprophylaxis
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medicine
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protac
- 3.4.21.69
- thrombosis
- venous
- leiden
- sepsis
- endothelial
- antithrombin
- thromboembolism
- thrombophilia
- clot
- thrombomodulin
- platelet
-
procoagulant
- heparin
- arterial
- vein
-
bleeding
- plasminogen
-
hypercoagulable
- thromboplastin
-
lupus
- fibrinogen
-
fibrinolysis
-
hemostatic
- viiia
- epcr
-
intravascular
-
contraceptive
-
antiphospholipid
-
antithrombotic
-
prothrombotic
- fibrin
-
k-dependent
-
anticardiolipin
-
d-dimers
- coagulopathy
- embolism
- prothrombinase
-
amidolytic
-
thrombin-antithrombin
-
haemostasis
- par1
-
profibrinolytic
- pharmacology
-
goal-directed
- diagnostics
- drug development
-
gamma-carboxyglutamic
-
deep-vein
-
time-based
- tafi
-
hypofibrinolysis
-
thromboprophylaxis
- medicine
- protac
Reaction
degradation of blood coagulation factors Va and VIIIa =
Synonyms
Activated blood coagulation factor XIV, Activated protein C, anticoagulant activated protein C, anticoagulant protein C/protein S system, anticoagulant serine protease-activated protein C, anticoagulant-activated protein C, APC, Autoprothrombin II-A, Autoprothrombin IIA, Blood coagulation factor XIV, Blood-coagulation factor XIV, activated, Blood-coagulation factor XIVa, ghrelin endopeptidase, GSAPC, hAPC, PROC, Protein Ca, rhAPC
ECTree
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Metals Ions
Metals Ions on EC 3.4.21.69 - Protein C (activated)
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Ca2+
Mg2+
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significantly increases recombinant activated protein C binding to the neutrophil surface
Mn2+
Na+
Zn2+
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Zn2+ enhances the binding of protein C/activated protein C to endothelial cell protein C receptor on endothelial cells by increasing the binding affinities. Zn2+ binding induces conformational changes in protein C/APC. Zn2+ binding to APC inhibits the amidolytic activity of APC, but the inhibition is reversed by Ca2+. Zn2+ increases the rate of APC generation on endothelial cells in the presence of physiological concentrations of Ca2+, but does not further enhance increased APC generation obtained in the presence of physiological concentrations of Mg2+ with Ca2+. Zn2+ has no effect on the anticoagulant activity of APC. Zn2+ enhances APC-mediated activation of protease activated receptor 1 and p44/42 MAPK
additional information
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contains gamma-carboxyglutamic acid residues required for Ca2+-dependent membrane binding
Ca2+
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contains gamma-carboxyglutamic acid residues required for Ca2+-dependent membrane binding
Ca2+
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required, calcium enhances the amidolytic activity of APC by 2fold, the Ca2+ and Na+ metal ion-binding sites are linked energetically
Ca2+
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significantly increases recombinant activated protein C binding to the neutrophil surface
Ca2+
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a group of four or five divalent cation binding sites in the Gla-domain show a high specificity for Ca2+. Ca2+ interactions are essential for the anticoagulant functions of APC and are influenced by mutations in different regions of the Gla-domain
Ca2+
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the presence of Ca2+ is essential for Zn2+ to enhance protein C activation because Zn2+ alone fails to support protein C activation
Mn2+
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significantly increases recombinant activated protein C binding to the neutrophil surface
Na+
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the amidolytic activity of APC is strictly dependent on Na+, the Ca2+ and Na+ metal ion-binding sites are linked energetically
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the divalent cation site is separate from the monovalent cation site and the active site of the enzyme
additional information
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the enzyme displays a strict requirement for monovalent cations in its expression of amidolytic activity towards Nalpha-benzoyl-L-arginine 4-nitroanilide