Application | Comment | Organism |
---|---|---|
medicine | the enzyme has potential therapeutic application in pathological conditions where the controlled activation of prothrombin is desirable | Bothrops cotiara |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | from venom | Bothrops cotiara | - |
- |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
29000 | - |
x * 29000, SDS-PAGE | Bothrops cotiara |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Bothrops cotiara | 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 | ? | - |
? | |
prothrombin + H2O | Bothrops cotiara | 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 | active thrombin + thrombin fragment 1 + prothrombin 1 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bothrops cotiara | - |
- |
- |
Purification (Comment) | Organism |
---|---|
native enzyme from venom by gel filtration and cation exchange chromatography to homogeneity | Bothrops cotiara |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
venom | - |
Bothrops cotiara | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | 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 | Bothrops cotiara | ? | - |
? | |
prothrombin + H2O | 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 | Bothrops cotiara | active thrombin + thrombin fragment 1 + prothrombin 1 | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 29000, SDS-PAGE | Bothrops cotiara |
Synonyms | Comment | Organism |
---|---|---|
cotiarinase | - |
Bothrops cotiara |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Bothrops cotiara |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Bothrops cotiara |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | the enzyme from Bothrops cotiara venom activates prothrombin in the absence of the typical co-factors required for the specific cleavage of prothrombin | Bothrops cotiara |