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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
selective cleavage of Arg-/-Thr and Arg-/-Ile in prothrombin to form thrombin and two inactive fragments
From the venom of the Taipan snake (Oxyuranus scutellatus). Converts prothrombin to thrombin. Specificity is similar to that of Factor Xa (EC 3.4.21.6). However, unlike Factor Xa this enzyme can cleave its target in the absence of coagulation Factor Va. Activity is potentiated by phospholipid and Ca2+ which binds via gamma-carboxyglutamic acid residues. Similar enzymes are known from the venom of other Australian elapid snakes, including Pseudonaja textilis textilis, Oxyuranus microlepidotus and Demansia nuchalis affinis.
cotiarinase is a snake venom serine proteinase that generated thrombin upon incubation with prothrombin, limited proteolysis of this protein to release prothrombin 1, fragment 1 and thrombin
the enzyme does not show fibrinogen-clotting, platelet-aggregating, fibrinogenolytic and factor X activating activities. Very low amidolytic activity as detected by the hydrolysis of the chromogenic substrates D-Phe-Pip-Arg-4-naphthyl amide and D-Val-Leu-Lys-4-naphthylamide
enzyme acts on cell survival, regulating the expression of molecules as NO and avoiding cell death. Enzyme triggers release of interleukin 8, inhibits platelet activation and chemotaxis and causes uncoagulable blood by fibrinogen depletion
cotiarinase is a snake venom serine proteinase that generated thrombin upon incubation with prothrombin, limited proteolysis of this protein to release prothrombin 1, fragment 1 and thrombin
the enzyme does not show fibrinogen-clotting, platelet-aggregating, fibrinogenolytic and factor X activating activities. Very low amidolytic activity as detected by the hydrolysis of the chromogenic substrates D-Phe-Pip-Arg-4-naphthyl amide and D-Val-Leu-Lys-4-naphthylamide
enzyme acts on cell survival, regulating the expression of molecules as NO and avoiding cell death. Enzyme triggers release of interleukin 8, inhibits platelet activation and chemotaxis and causes uncoagulable blood by fibrinogen depletion
the enzyme from Bothrops cotiara venom activates prothrombin in the absence of the typical co-factors required for the specific cleavage of prothrombin
hydrolysis of benzoyl-Ile-Glu-Gly-Arg 4nitroanilide is insensitive to: diisopropyl fluorophosphate, antithrombin III, chicken ovomucoid trypsin inhibitor, EDTA, 1,10-phenanthroline, activated protein C
Management of lepirudin therapy for a patient with antiphospholipid antibody syndrome using the whole blood ecarin clot time and activated partial thromboplastin time.
The cardiovascular and haematological effects of purified prothrombin activator from the common brown snake (Pseudonaja textilis) and their antagonism with heparin.
Vibrio vulnificus secretes a broad-specificity metalloprotease capable of interfering with blood homeostasis through prothrombin activation and fibrinolysis.
A quick assay for monitoring recombinant hirudin during cardiopulmonary bypass in patients with heparin-induced thrombocytopenia type II : adaptation of the ecarin clotting time to the act II device.
Successful use of recombinant hirudin and its monitoring by ecarin clotting time in patients with heparin-induced thrombocytopenia undergoing off-pump coronary artery revascularization.
The use of ecarin chromogenic assay and prothrombinase induced clotting time in the monitoring of lepirudin for the treatment of heparin-induced thrombocytopenia.
[Use of ecarin clotting time in whole blood for monitoring recombinant hirudine treatment during cardiopulmonary bypass in patients with heparin-induced thrombocytopenia]
Comparative proteomic analysis of the venom of the taipan snake, Oxyuranus scutellatus, from Papua New Guinea and Australia: Role of neurotoxic and procoagulant effects in venom toxicity.
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
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
x * 110000 + x * 80000 + 2 disulfide-linked polypeptides of MW 30000 (one or both of these contain the active site), Oxyuranus scutellatus, SDS-PAGE after reduction with 2-mercaptoethanol
x * 110000 + x * 80000 + 2 disulfide-linked polypeptides of MW 30000 (one or both of these contain the active site), Oxyuranus scutellatus, SDS-PAGE after reduction with 2-mercaptoethanol
x * 110000 + x * 80000 + 2 disulfide-linked polypeptides of MW 30000 (one or both of these contain the active site), Oxyuranus scutellatus, SDS-PAGE after reduction with 2-mercaptoethanol
A novel small conductance Ca2+-activated K+ channel blocker from Oxyuranus scutellatus taipan venom. Re-evaluation of taicatoxin as a selective Ca2+ channel probe
Lopap, a prothrombin activator from Lonomia obliqua belonging to the lipocalin family: recombinant production, biochemical characterization and structure-function insights
The catalytic subunit of pseutarin C, a group C prothrombin activator from the venom of Pseudonaja textilis, is structurally similar to mammalian blood coagulation factor Xa