EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
    1.14.16.1 | -999 |
- |
thermal inactivation profiles of the purified wild-type enzyme, and mutants I65T, R261Q and V388M in absence or presence of 1% glycerol or trimethylamine N-oxide, overview |
689888 |
| 1.14.16.1 | 20 |
60 |
holo-phenylalanine hydroxylase displays a large increase in thermal stability (approximately 15°C upshift in the Tm value) compared with the apoenzyme (melting temperature at 64°C), holo-caPAH shows higher kinetic stability at optimal growth temperature (denaturing approximately 8 times more slowly than the apo form at 55°C) |
699022 |
| 1.14.16.1 | 44 |
76 |
pH 7.4, kinetics of thermal unfolding of apo- and holo-enzymes within the temperature range and with different metal cofactors: native Fe2+, or artificial Zn2+ or Co2+, unfolding profiles, transition-state analysis shows a common mechanism for all enzyme variants, at higher temperatures the unfolding rates of Zn- and Co-PAH are affected significantly by entropy, while the unfolding rates of apo- and Fe-PAH are dominated by enthalpy even at higher temperatures, overview |
687083 |
| 1.14.16.1 | 47 |
- |
50% residual activity after 66 min, presence of Fe(II), after 8 min in presence of EDTA |
659645 |
| 1.14.16.1 | 50 |
- |
the residual activity of the enzyme is 8.6% and the half-life is 9 min when incubated at 50°C for 1 h |
744732 |
| 1.14.16.1 | 50 |
- |
V388M mutant enzyme, 50% activity after 10 min |
438748 |
| 1.14.16.1 | 51 |
- |
L348V mutant enzyme, 50% activity after 10 min |
438748 |
| 1.14.16.1 | 52 |
- |
Tm, inactivation |
687580 |
| 1.14.16.1 | 53 |
- |
melting temperature of enzyme, presence of EDTA |
659645 |
| 1.14.16.1 | 59 |
- |
recombinant wild-type enzyme, 50% activity after 10 min |
438748 |
