Due to scheduled maintenance work, this service may not be available on Monday January 22nd between 08.00 am and 9.00 am CEST
To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...] View this page in https
ENZYME entry: EC 126.96.36.199
View entry in original ENZYME format
View entry in raw text format (no links)
in this entry
|Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme|
- A somewhat thrombin-like enzyme from venoms of snakes of the
- Species variants of the enzyme include ancrod from Agkistrodon
rhodostoma (Malayan pit viper), batroxobin from Bothrops atrox (South
American pit viper) and crotalase from Crotalus adamanteus (Eastern
- Does not require activation by calcium.
- Belongs to peptidase family S1.
- Formerly EC 188.8.131.52, EC 184.108.40.206 and EC 220.127.116.11.
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
|P05620, VSP1_PROFL; ||P81661, VSPA_BOTJA; ||F8S114, VSPCR_CROAD; |
|P26324, VSPF1_CALRH; ||P47797, VSPF2_CALRH; ||P04971, VSPF_BOTAT; |
|Q9PS28, VSPF_CERCE; ||Q9PRP4, VSPF_LACMR; ||P33589, VSPF_LACMU; |
|P0DJ86, VSPL_BOTLC; |
, with possibility to download in different formats, align etc.
entries corresponding to 3.4.21.-
entries corresponding to 3.4.-.-
entries corresponding to 3.-.-.-