Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy

Selective cleavage of Arg!Thr and Arg!Ile in prothrombin to form thrombin and two inactive fragments

From the venom of the Taipan snake (Oxyuranus scutellatus). Converts prothrombin to thrombin. Specificity is similar to that of Factor Xa (EC 3.4.21.6). However, unlike Factor Xa this enzyme can cleave its target in the absence of coagulation Factor Va. Activity is potentiated by phospholipid and Ca2+ which binds via gamma-carboxyglutamic acid residues. Similar enzymes are known from the venom of other Australian elapid snakes, including Pseudonaja textilis textilis, Oxyuranus microlepidotus and Demansia nuchalis affinis.

EC 3.4.21.60 created 1978 as EC 3.4.99.28, transferred 1992 to EC 3.4.21.60, modified 2010, modified 2011

1  [PMID:6986908]

Walker FJ, Owen WG, Esmon CT.

Characterization of the prothrombin activator from the venom of Oxyuranus scutellatus scutellatus (taipan venom).

Biochemistry 19:1020-3 (1980)
DOI:10.1021/bi00546a029

2  [PMID:3531198]

Speijer H, Govers-Riemslag JW, Zwaal RF, Rosing J.

Prothrombin activation by an activator from the venom of Oxyuranus scutellatus (Taipan snake).

J Biol Chem 261:13258-67 (1986)