EC Number   |
Protein Variants |
Reference |
|---|
   3.4.21.21 | 306X |
mutation studies show that the interaction between protein cofactor tissue factor and methionine-306 in the serine protease domain of FVIIa triggers the activation process and suggested some ensuing steps on the pathway to the active conformation |
710606 |
| 3.4.21.21 | A294V |
mutant enzyme shows delayed activation by activated factor X as well as reduced activity towards peptidyl and macromolecular substrates without impairing the catalytic efficiency of the triad |
654496 |
| 3.4.21.21 | C164V/V299C-FVIIa |
introduction of a new disulfide bridge between Cys-159 and an introduced Cys at position 299 |
667588 |
| 3.4.21.21 | D102Q |
inactive mutant enzyme |
654583 |
| 3.4.21.21 | D186A |
turnover-number for activation of factor X is 5.5fold lower than that of the wild-type factor VII, Km-value for activation of factor X is 1.2fold lower than that of the wild-type factor VII |
654583 |
| 3.4.21.21 | D343H |
mutant enzyme shows no activity with methanesulfonyl-D-cyclohexylalanyl-butyl-arginine p-nitroanilide, factor X and factor IX |
654508 |
| 3.4.21.21 | D72N |
the mutant shows 13% of wild type FVIIa signaling activity towards protease-activated receptor 2 |
717790 |
| 3.4.21.21 | DELTA360-329 |
lower affinity for soluble tissue factor as compared to wild-type factor VIIa, 7fold smaller tissue factor-mediated acceleration of amidolytic activity compared to wild type factor VIIa |
656000 |
| 3.4.21.21 | E154A |
slightly increased Km-value and decreased turnover number compared to the wild-type enzyme |
95334 |
| 3.4.21.21 | E154R |
site-directed mutagenesis, activity and active site structure in comparison to the wild-type |
683477 |
