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Literature summary for 3.4.21.60 extracted from

  • Loevgren, A.
    Recombinant snake venom prothrombin activators (2013), Bioengineered, 4, 153-157.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.60

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Echis carinatus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ Zn-metalloprotease Echis carinatus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
prothrombin + H2O Echis carinatus ecarin converts prothrombin to thrombin also if the prothrombin is not gamma-carboxylated ?
-
 ?

Organism

Organism UniProt Comment Textmining
Echis carinatus Q90495
-
-

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
 Echis carinatus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prothrombin + H2O ecarin converts prothrombin to thrombin also if the prothrombin is not gamma-carboxylated Echis carinatus ?
-
 ?

Synonyms

Synonyms Comment Organism
ecarin
-
 Echis carinatus
prothrombin activator
-
 Echis carinatus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Echis carinatus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Echis carinatus

Cofactor

Cofactor Comment Organism Structure
additional information ecarin is not dependent on any cofactors Echis carinatus

General Information

General Information Comment Organism
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 Echis carinatus