EC Number   |
Protein Variants |
Reference |
|---|
   3.4.14.10 | D387G |
mutant shows an increase in pKa for kcat |
731331 |
| 3.4.14.10 | D387G |
mutant shows bell-shaped pH-dependence of kcat, possibly due to an impaired protonation of the leaving group |
731331 |
| 3.4.14.10 | D387G |
the pKa values of mutant D387G for kcat (app) increase when Asp-387 is changed to glycine. Mutant shows a bell-shaped pH-dependence of kcat(app), possibly due to an impaired protonation of the leaving group. Mutant shows a decresed kcat for all substrates and a highly decreased kcat/Km compared to wild-type. In contrast to wild-type at higher pH the kcat (app) value decreases |
731331 |
| 3.4.14.10 | D44A |
catalytic activity of the mutant enzyme is at least one order of magnitude lower than that of the wild-type enzyme |
647158 |
| 3.4.14.10 | E305K |
the mutant shows extremely low activity |
696417 |
| 3.4.14.10 | E305Q |
the mutant shows extremely low activity |
696417 |
| 3.4.14.10 | E331K |
the catalytic efficiency is reduced 20000fold for the E331K variant compared to the wild type enzyme |
696417 |
| 3.4.14.10 | E331Q |
mutant has a 2-3 orders of magnitude decreased kcat app/KM compared to wild-type, mostly dependent on an increase in KM |
731331 |
| 3.4.14.10 | E331Q |
the catalytic efficiency is reduced 400fold for the E331Q variant compared to the wild type enzyme |
696417 |
| 3.4.14.10 | G375D |
less than 0.1% of wild-type activity |
731331 |
