EC Number   |
Protein Variants |
Reference |
|---|
    2.7.1.49 | C110A |
residue C110 is mandatory for pyridoxal, but not for pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine turnover |
-, 738451 |
| 2.7.1.49 | C214A |
mutant does not turn over pyridoxal, pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine. Residue C214 acts as the catalytic base in the phosphorylation reaction |
-, 738451 |
| 2.7.1.49 | M134K |
detrimental to HMP kinase activity |
671903 |
| 2.7.1.49 | M134K/T472D |
double mutant with 25% activity compared to the wild type enzyme |
671903 |
| 2.7.1.49 | more |
construction of a thiD knockout mutant strain, complementation of the Escherichia coli DELTA thiD knockout mutant is possible by heterologous expression of gene ThiD2, ThiD2 proteins catalyze phosphorylation of HMP monophosphate, but not of HMP or its toxic analogues and damage products such as bacimethrin and 5-(hydroxymethyl)-2-methylpyrimidin-4-ol. As strictly monofunctional HMP monophosphate kinases (EC 2.7.4.7), ThiD2 proteins eliminate a potentially fatal vulnerability of canonical ThiD, at the cost of the ability to reclaim HMP formed by thiamin turnover |
-, 758754 |
| 2.7.1.49 | more |
phosphomethylpyrimidine kinase activity, EC 2.7.4.7, is abolished in C-terminally truncated isozymes Thi20p and Thi21p, the mutant yeast strains sow no thiamin phosphate synthesis activity |
-, 661537 |
| 2.7.1.49 | Q373L |
30% reduced HMP kinase activity |
671903 |
| 2.7.1.49 | Q98L |
detrimental to HMP kinase activity |
671903 |
| 2.7.1.49 | Q98L/Q373L |
double mutant with 10% activity compared to the wild type enzyme |
671903 |
| 2.7.1.49 | S444A |
without any effect on activity |
671903 |
