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Literature summary for 3.4.21.6 extracted from

  • Lee, C.J.; Wu, S.; Eun, C.; Pedersen, L.G.
    A revisit to the one form kinetic model of prothrombinase (2010), Biophys. Chem., 149, 28-33.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Factor Va
-
Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of prothrombinase, methematical analysis, overview Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
prothrombin + H2O Homo sapiens prothrombinase cleaves prothrombin at two cleavage positions Arg-271-Thr-272 and Arg-320-Ile-321 thrombin + ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prothrombin + H2O prothrombinase cleaves prothrombin at two cleavage positions Arg-271-Thr-272 and Arg-320-Ile-321 Homo sapiens thrombin + ?
-
?

Subunits

Subunits Comment Organism
More three-dimensional model structure of the prothrombinase/prothrombin complex obtained from solvent equilibration molecular dynamics simulations for factor Xa/factor Va, docking, structure, and mechanism analysis, model comparisons, overview Homo sapiens

Synonyms

Synonyms Comment Organism
factor Xa
-
Homo sapiens
FXa
-
Homo sapiens
prothrombinase
-
Homo sapiens

General Information

General Information Comment Organism
additional information the mechanism for the activation of prothrombin to thrombin by prothrombinase is achieved through two distinct intermediate pathways, overview Homo sapiens