Ecarin
From Wikipedia, the free encyclopedia
| Ecarin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.- | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Ecarin is an metalloprotease enzyme[1] that is derived from the venom of the Indian saw-scaled viper, Echis carinatus,[2] It is the primary reagent in the Ecarin clotting time test.
Ecarin is known to activate prothrombin, another protein that is a critical component of the blood clotting cascade.[3]

The venom of the saw-scaled viper, Echis carinatus, causes bleeding and eventually death.[4] The venom contains ecarin, which converts prothrombin to meizothrombin, a thrombin analog with increased esterase activity, and not to normal thrombin.[5]