EC Number   |
Protein Variants |
Reference |
|---|
   3.4.19.5 | D285A |
kcat/Km for beta-Asp-Leu is 85000fold lower than wild-type value |
667676 |
| 3.4.19.5 | D285N |
kcat/Km for beta-Asp-Leu is 5667fold lower than wild-type value |
667676 |
| 3.4.19.5 | E166A |
the mutant exhibits a complete loss of activity and a considerable decrease in melting temperature |
-, 755151 |
| 3.4.19.5 | E166K |
the mutant exhibits a complete loss of activity and a considerable decrease in melting temperature |
-, 755151 |
| 3.4.19.5 | E77D |
kcat/Km for beta-Asp-Leu is 137837fold lower than wild-type value |
667676 |
| 3.4.19.5 | E77Q |
kcat/Km for beta-Asp-Leu is 14571fold lower than wild-type value |
667676 |
| 3.4.19.5 | E80Q |
the mutant has no catalytic activity toward beta-Asp-Leu, but its CD spectra and denaturation temperature are similar to wild-type, indicating that this mutation affects catalytic activity but not the overall folding and integrity of the enzyme |
-, 755151 |
| 3.4.19.5 | R169K |
kcat/Km for beta-Asp-Leu is 378fold lower than wild-type value |
667676 |
| 3.4.19.5 | R169M |
kcat/Km for beta-Asp-Leu is 1672131fold lower than wild-type value |
667676 |
| 3.4.19.5 | R233K |
kcat/Km for beta-Asp-Leu is 192fold lower than wild-type value |
667676 |
