Venombin A
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.21 Serine endopeptidases > 3.4.21.74 venombin A
Venombin A (ancrod/batroxobin/crotalase) is a thrombin-like serine protease in family S1 from viper/rattlesnake venoms, not requiring Ca2+ activation; species variants include ancrod from Calloselasma rhodostoma (Malayan pit viper, formerly EC 3.4.21.28), batroxobin from Bothrops atrox (formerly EC 3.4.21.29) and crotalase from Crotalus adamanteus (formerly EC 3.4.21.30); it selectively cleaves the Arg bond in fibrinogen to form fibrin and release fibrinopeptide A, with further fibrinogen degradation varying by species. By clotting fibrinogen it disturbs prey haemostasis. It appears in viruses and cellular organisms.
Venombin A (ancrod/batroxobin/crotalase) is a thrombin-like serine protease in family S1 from viper/rattlesnake venoms, not requiring Ca2+ activation; species variants include ancrod from Calloselasma rhodostoma (Malayan pit viper, formerly EC 3.4.21.28), batroxobin from Bothrops atrox (formerly EC 3.4.21.29) and crotalase from Crotalus adamanteus (formerly EC 3.4.21.30); it selectively cleaves the Arg bond in fibrinogen to form fibrin and release fibrinopeptide A, with further fibrinogen degradation varying by species. By clotting fibrinogen it disturbs prey haemostasis. It appears in viruses and cellular organisms.
References:
Biomedical Dictionary
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