Venombin A

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Venombin A (EC 3.4.21.74, alpha-fibrinogenase, habutobin, zinc metalloproteinase Cbfib1.1, zinc metalloproteinase Cbfib1.2, zinc metalloproteinase Cbfib2, ancrod) is an enzyme.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical 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

This enzyme is a thrombin-like enzyme from venoms of snakes of the viper/rattlesnake group.

References

↑ Nolan, C., Hall, L.S. and Barlow, G.H. (1976). "Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom". Methods Enzymol. 45: 205–213. doi:10.1016/s0076-6879(76)45020-6. PMID 1011992.
↑ Stocker, K. and Barlow, G.H. (1976). "The coagulant enzyme from Bothrops atrox venom (batroxobin)". Methods Enzymol. 45: 214–223. doi:10.1016/s0076-6879(76)45021-8. PMID 1011993.
↑ Markland, F.S., Kettner, C., Schiffmann, S., Shaw, E., Bajwa, S.S., Reddy, K.N.N., Kirakossian, H., Patkos, G.B., Theodor, I. and Pirkle, H. (1982). "Kallikrein-like activity of crotalase, a snake venom enzyme that clots fibrinogen". Proc. Natl. Acad. Sci. USA 79: 1688–1692. doi:10.1073/pnas.79.6.1688. PMID 7043462.
↑ Simmons, G., Bundalian, M., Theodor, I., Martinoli, J. and Pirkle, H. (1985). "Action of crotalase, an enzyme with thrombin-like and kallikrein-like specificities, on tripeptide nitroanilide derivatives". Thromb. Res. 40: 555–561. doi:10.1016/0049-3848(85)90292-0. PMID 2934864.
↑ Itoh, N., Tanaka, N., Funakoshi, I., Kawasaki, T., Mihashi, S. and Yamashina, I. (1988). "Organisation of the gene for batroxobin, a thrombin-like snake venom enzyme. Homology with the trypsin/kallikrein gene family". J. Biol. Chem. 263: 7628–7631. PMID 3163691.

External links

Venombin A at the US National Library of Medicine Medical Subject Headings (MeSH)

Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)

Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic

Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator

Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase

Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin

Venombin	Ancrod Batroxobin

Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin Streptokinase S1P Cathepsin A G

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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