EC Number |
Protein Variants |
Reference |
---|
3.4.21.6 | D322N/S419A |
no proteolytic activity |
81430 |
3.4.21.6 | D70K |
mutation of E2FXa mutant, loss of ability to bind Ca2+, activity is retained |
649955 |
3.4.21.6 | 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 |
666179 |
3.4.21.6 | E16D |
E16 is posttranslationally carboxylated in wild-type enzyme. Heparin activated inhibition of mutant enzyme by antithrombin is not activated by Ca2+ |
666179 |
3.4.21.6 | 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 |
666179 |
3.4.21.6 | E217A |
affinity for interaction with Na+ is impaired. 3-4fold decrease in activity towards both natural and synthetic substrates. Presence of factor Va restores most of the catalytic defect with substrate prothrombin |
696269 |
3.4.21.6 | E217Q |
affinity for interaction with Na+ is impaired. Presence of factor Va restores most of the catalytic defect with substrate prothrombin |
696269 |
3.4.21.6 | E26D |
E26 is posttranslationally carboxylated in wild-type enzyme. Heparin activated inhibition of mutant enzyme by antithrombin is not activated by Ca2+ |
666179 |
3.4.21.6 | 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 |
666179 |
3.4.21.6 | E80K |
mutation of E2FXa mutant, loss of ability to bind Ca2+, activity is retained |
649955 |