Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.60 extracted from

  • Kitano, E.S.; Garcia, T.C.; Menezes, M.C.; Tashima, A.K.; Zelanis, A.; Serrano, S.M.
    Cotiarinase is a novel prothrombin activator from the venom of Bothrops cotiara (2013), Biochimie, 95, 1655-1659.
    View publication on PubMed
Search for more literature for 3.4.21.60

Application

Application Comment Organism
medicine the enzyme has potential therapeutic application in pathological conditions where the controlled activation of prothrombin is desirable Bothrops cotiara

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular from venom Bothrops cotiara
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
 x * 29000, SDS-PAGE Bothrops cotiara

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Bothrops cotiara
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from venom by gel filtration and cation exchange chromatography to homogeneity Bothrops cotiara

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Bothrops cotiara
-

Substrates and Products (Substrate)

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

Subunits Comment Organism
? x * 29000, SDS-PAGE Bothrops cotiara

Synonyms

Synonyms Comment Organism
cotiarinase
-
 Bothrops cotiara

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bothrops cotiara

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Bothrops cotiara

Cofactor

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