3.4.21.60: Scutelarin
This is an abbreviated version!
For detailed information about Scutelarin, go to the full flat file.
Word Map on EC 3.4.21.60
-
3.4.21.60
-
clot
-
anticoagulant
-
coagulation
-
venom
-
thromboplastin
-
snake
-
chromogenic
-
dabigatran
-
bleeding
-
thrombocytopenia
-
procoagulant
-
carinatus
-
heparin-induced
-
meizothrombin
-
etexilate
-
viper
-
argatroban
-
echis
-
r-hirudin
-
lepirudin
-
prothrombinase
-
rivaroxaban
-
textilis
-
pseudonaja
-
lonomia
-
anti-factor
-
anti-xa
-
doacs
-
apixaban
-
idarucizumab
-
hemoclot
-
bivalirudin
-
elapid
-
prothrombinase-induced
-
obliqua
-
prethrombin-2
-
tropidechis
-
melagatran
-
medicine
-
edoxaban
-
saw-scaled
-
peg-hirudin
- 3.4.21.60
- clot
-
anticoagulant
- coagulation
- venom
- thromboplastin
- snake
-
chromogenic
- dabigatran
-
bleeding
- thrombocytopenia
-
procoagulant
- carinatus
-
heparin-induced
- meizothrombin
-
etexilate
- viper
- argatroban
- echis
-
r-hirudin
- lepirudin
- prothrombinase
- rivaroxaban
- textilis
- pseudonaja
- lonomia
-
anti-factor
-
anti-xa
-
doacs
- apixaban
-
idarucizumab
-
hemoclot
- bivalirudin
-
elapid
-
prothrombinase-induced
- obliqua
- prethrombin-2
-
tropidechis
- melagatran
- medicine
- edoxaban
-
saw-scaled
-
peg-hirudin
Reaction
selective cleavage of Arg-/-Thr and Arg-/-Ile in prothrombin to form thrombin and two inactive fragments =
Synonyms
cotiaractivase, cotiarinase, EC 3.4.99.28, ecarin, Lopap, Proteinase, Oxyuranus scutellatus prothrombin-activating, prothrombin activator, pseutarin C, scuterin, Taipan activator
ECTree
Advanced search results
General Information
General Information on EC 3.4.21.60 - Scutelarin
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
physiological function
apart from the natural activation pathway, human prothrombin can also be activated by prothrombin activators in snake venoms. Ecarin is not dependent on any cofactors, but generates meizothrombin
physiological function
-
thrombin is generated from prothrombin through cleavage at two sites by the prothrombinase complex. Prothrombinase is composed of a protease, factor Xa, and a cofactor, factor Va, which interact on negatively charged phospholipid surfaces and cleave prothrombin into thrombin 300000times faster than factor Xa alone The enzyme is responsible for the balance between bleeding and thrombosis