EC Number   |
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Reference |
|---|
   3.4.21.6 | -999 |
- |
meizothrombin |
pH 7.4, 22°C, in absence of factor Va |
652501 |
| 3.4.21.6 | -999 |
- |
more |
kcat values of prothrombinase assembled with mutant cofactor factor Va D334K/Y335F or D334A/Y335A is reduced. Prothrombinase assembled with quadruple mutant molecules E323Y/E330Y/D334K/Y335F or E323Y/E330Y/D334A/Y335A displays a second-order rate constant up to 400fold lower than the value obtained with wild-type factor Va |
696276 |
| 3.4.21.6 | -999 |
- |
prothrombin |
and monomer. Dimer is about 1000000fold less active toward prothrombin than the monomer, mainly due to a substantial decrease in kcat. Dimerization results in substantial change in tertiary or quarternary structure with a concomitant decrease in alpha-helix |
696780 |
| 3.4.21.6 | 0.0000000018 |
- |
prothrombin |
dimer, presence of 3 mM Ca2+ |
696780 |
| 3.4.21.6 | 0.000000002 |
- |
prothrombin |
dimer, presence of 5 mM Ca2+ |
696780 |
| 3.4.21.6 | 0.0029 |
- |
prothrombin |
monomer, presence of 3 mM Ca2+ |
696780 |
| 3.4.21.6 | 0.004 |
- |
prothrombin |
monomer, presence of 5 mM Ca2+ |
696780 |
| 3.4.21.6 | 0.0045 |
- |
prothrombin |
pH 7.4, 22°C, in absence of factor Va |
652501 |
| 3.4.21.6 | 0.0057 |
- |
fragment 1.2:prethrombin-2 |
pH 7.4, 22°C, in absence of factor Va |
652501 |
| 3.4.21.6 | 0.0068 |
- |
recombinant prothrombin R155A/R284A/R271A mutant rMZ-II |
pH 7.4, 22°C, in absence of factor Va |
652501 |
