venombin A

This is an abbreviated version!
For detailed information about venombin A, go to the full flat file.

Word Map on EC


Selective cleavage of Arg-/- bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme =


alpha-Fibrinogenase, Habutobin, Ancrod, Batroxobin, Crotalase, EC, EC, EC, TLE, Bothrops atrox serine proteinase, Protein C activator, Reptilase, Thrombin-like enzyme, bothrombin, VLAF, viper venom serine protease, albofibrase1, alpha fibrinogenase, RVBCMP, Russell's viper basic coagulant metalloprotease, venom gloshedobin, gloshedobin, Bhalternin, TA-2, thrombin-like serine protease, BpirSP-39, RVV protease, VaF1, beta-fibrinogenase, VLBF, metalloproteinase 1, Vaa serine proteinase homolog 1, VaaSPH-1, snake venom serine protease, Lachesis stenophrys venom serine proteinase, Dav-PA, AaV-SP-II, coagulant serine protease, VLCII


     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
       venombin A


Application on EC - venombin A

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the enzyme may be useful for developing potential diagnostic agents for detecting coagulation disorders
drug development
VaaSPH-1 represents a very promising template to design low molecular mass FVIIIa-directed anticoagulant substances, based on structural features of the interaction surface between VaaSPH-1 and FVIIIa. Construction of a three-dimensional model of VaaSPH-1 bound to FVIIIa. The model exposes the 157-loop and the preceding alpha-helix as the most appropriate structural elements of VaaSPH-1 to be considered as a guideline to synthesize small FVIIIa-binding molecules, potential different generation of anticoagulants
Bhaltenin may be of interest as a therapeutic agent in the treatment and prevention of thrombotic disorders