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Literature summary for 3.4.21.6 extracted from

  • Whinna, H.C.; Lesesky, E.B.; Monroe, D.M.; High, K.A.; Larson, P.J.; Church, F.C.
    Role of the gamma-carboxyglutamic acid domain of activated factor X in the presence of calcium during inhibition by antithrombin-heparin (2004), J. Thromb. Haemost., 2, 1127-1134.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E14D E14 is posttranslationally carboxylated in wild-type enzyme. Heparin activated inhibition of mutant enzyme by antithrombin with and without Ca2+ is enhanced compared to wild-type recombinant FXa Homo sapiens
E16D E16 is posttranslationally carboxylated in wild-type enzyme. Heparin activated inhibition of mutant enzyme by antithrombin is not activated by Ca2+ Homo sapiens
E19D E19 is posttranslationally carboxylated in wild-type enzyme. Heparin activated inhibition of mutant enzyme by antithrombin is the same as wild-type recombinant FXa Homo sapiens
E26D E26 is posttranslationally carboxylated in wild-type enzyme. Heparin activated inhibition of mutant enzyme by antithrombin is not activated by Ca2+ Homo sapiens
E29D E29D is posttranslationally carboxylated in wild-type enzyme. Heparin activated inhibition by antithrombin with and without Ca2+ is enhanced compared to wild-type recombinant FXa Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
antithrombin inhibition is enhanced by heparin. Ca2+ increases about 3fold the inhibition rate of wild-type recombinant enzyme over that in presence of EDTA Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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