ENZYME entry: EC 3.4.21.74
Accepted Name |
Venombin A.
|
Reaction catalysed |
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 |
Comment(s) |
- A somewhat thrombin-like enzyme from venoms of snakes of the
viper/rattlesnake group.
- 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
diamondback rattlesnake).
- Does not require activation by calcium.
- Belongs to peptidase family S1.
- Formerly EC 3.4.21.28, EC 3.4.21.29 and EC 3.4.21.30.
|
Cross-references |
PROSITE | PDOC00124 |
BRENDA | 3.4.21.74 |
EC2PDB | 3.4.21.74 |
ExplorEnz | 3.4.21.74 |
PRIAM enzyme-specific profiles | 3.4.21.74 |
KEGG Ligand Database for Enzyme Nomenclature | 3.4.21.74 |
IUBMB Enzyme Nomenclature | 3.4.21.74 |
IntEnz | 3.4.21.74 |
MEDLINE | Find literature relating to 3.4.21.74 |
MetaCyc | 3.4.21.74 |
UniProtKB/Swiss-Prot |
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; |
|
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