EC Number   |
Protein Variants |
Reference |
|---|
    2.7.7.24 | Q83A |
0.2% relative activity compared to the wild type enzyme, using dTTP as a substrate |
674813 |
| 2.7.7.24 | Q83D |
0.2% relative activity compared to the wild type enzyme, using dTTP as a substrate |
-, 674813 |
| 2.7.7.24 | Q83N |
0.3% relative activity compared to the wild type enzyme, using dTTP as a substrate |
-, 674813 |
| 2.7.7.24 | Q83S |
0.3% relative activity compared to the wild type enzyme, using dTTP as a substrate |
-, 674813 |
| 2.7.7.24 | Q83E |
1.0% relative activity compared to the wild type enzyme, using dTTP as a substrate |
674813 |
| 2.7.7.24 | more |
a truncated enzyme form lacking the 170-residues C-terminal domain has decreased thermostability |
-, 662454 |
| 2.7.7.24 | more |
analysis of a deletion mutant lacking the 170-residue C-terminal domain indicated that this region has an important role in the thermostability and activity of the protein. Specific initial velocity (glucose-1-phosphate thymidylyltransferase activity) is 23 times lower than that of the native enzyme when measured at 37°C |
-, 748158 |
| 2.7.7.24 | more |
deletion of the C-terminal sequence of isoform DnmL increases the expression level of truncated DnmL, albeit without enzymic activity. Substitution of the C-terminal sequence of DnmL with that of isoform RmbA also leads to expression of the recombinant protein in soluble form. The fusion protein is catalytically active |
-, 723689 |
| 2.7.7.24 | T80A |
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions |
725308 |
| 2.7.7.24 | Y97A |
enhanced UDP-N-acetylglucosamine diphosphorylase activity under optimal conditions |
725308 |
