Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.60 extracted from

  • Pomowski, A.; Ustok, F.I.; Huntington, J.A.
    Homology model of human prothrombinase based on the crystal structure of Pseutarin C (2014), Biol. Chem., 395, 1233-1241.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure homology modelling using the crystal structure of Pseutarin C, structure analysis Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

General Information

General Information Comment Organism
physiological function thrombin is generated from prothrombin through cleavage at two sites by the prothrombinase complex. Prothrombinase is composed of a protease, factor Xa, and a cofactor, factor Va, which interact on negatively charged phospholipid surfaces and cleave prothrombin into thrombin 300000times faster than factor Xa alone The enzyme is responsible for the balance between bleeding and thrombosis Homo sapiens