Prothrombin

Thrombin (EC 3.4.21.5, fibrinogenase, thrombase, thrombofort, topical, thrombin-C, tropostasin, activated blood-coagulation prothrombin , blood-coagulation factor IIa, factor IIa, E thrombin, beta-thrombin, gamma-thrombin) may be a serine protease, an enzyme that, in humans, is encoded by the F2 gene. Prothrombin (coagulation factor II) is proteolytically cleaved to make thrombin within the clotting process. Thrombin successively acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, also as catalyzing many other coagulation-related reactions. Thrombin is produced by the enzymatic cleavage of two sites on prothrombin by activated prothrombinase (Xa). The activity of factor Xa is greatly enhanced by binding to activated proaccelerin (Va), termed the prothrombinase complex. Prothrombin is produced within the liver and is co-translationally modified during a vitamin K-dependent reaction that converts 10-12 glutamic acids within the N terminus of the molecule to gamma-carboxyglutamic acid (Gla). Within the presence of calcium, the Gla residues promote the binding of prothrombin to phospholipid bilayers. Deficiency of vitamin K or administration of the anticoagulant warfarin inhibits the assembly of gamma-carboxyglutamic acid residues, slowing the activation of the coagulation cascade. Prothrombin G20210A isn't usually amid other factor mutations (i.e., the foremost common is proaccelerin Leiden). The gene could also be inherited heterozygous (1 pair), or far more rarely, homozygous (2 pairs), and isn't associated with gender or blood group . Homozygous mutations increase the danger of thrombosis quite heterozygous mutations, but the relative increased risk isn't well documented.