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3.4.21.74: venombin A

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

Word Map on EC 3.4.21.74

Reaction

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 =

Synonyms

AaV-SP-II, albofibrase1, alpha fibrinogenase, alpha-Fibrinogenase, Ancrod, Batroxobin, beta-fibrinogenase, Bhalternin, bothrombin, Bothrops atrox serine proteinase, BpirSP-39, coagulant serine protease, Crotalase, Dav-PA, EC 3.4.21.28, EC 3.4.21.29, EC 3.4.21.30, gloshedobin, Habutobin, Lachesis stenophrys venom serine proteinase, metalloproteinase 1, Mutase, acetolactate, Protein C activator, Reptilase, Russell's viper basic coagulant metalloprotease, RVBCMP, RVV protease, snake venom serine protease, TA-2, Thrombin-like enzyme, thrombin-like serine protease, TLE, Vaa serine proteinase homolog 1, VaaSPH-1, VaF1, venom gloshedobin, viper venom serine protease, VLAF, VLBF, VLCII

ECTree

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

Temperature Stability

Temperature Stability on EC 3.4.21.74 - venombin A

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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
heating the RVBCMP at 40°C for 60 min at pH 7.4 does not influence the coagulant activity of the protein, whereas heating RVBCMP at 55°C for 20 min over a pH range from 7.0 to 8.0 results in only 42% of the original clotting activity remaining. Heating the RVBCP at 60°C results in a complete loss of coagulant activity
75
-
30 min, stable, isozyme A3
85
-
30 min, stable, isozymes A1 and 2