EC Number   |
Protein Variants |
Reference |
|---|
    2.7.1.35 | A243G |
naturally occuring mutation from a patient with diabetes, the mutant shows reduced catalytic activity and/or reduced affinity for PLP precursors, the mutant cannot complement the inactive Drosophila melanogaster dPdxk1 mutant when expressed in the mutant flies. Mutant A243G displays a damaging score of 0.72. The A243Q mutation somewhat reduces the affinity for ATP when using PL as substrate and the affinity for PM, while it does not affect KM for PL and PN. In addition, it has the effect to halve kcat with PL |
760178 |
| 2.7.1.35 | C110A |
residue C110 is mandatory for pyridoxal, but not for pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine turnover |
-, 738451 |
| 2.7.1.35 | C124A |
the mutant shows about 2fold increased catalytic efficiency compared to the wild type enzyme |
-, 737622 |
| 2.7.1.35 | 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 |
| 2.7.1.35 | D225A |
inactive |
-, 737622 |
| 2.7.1.35 | D231A |
site-directed mutagenesis of a GXGD motif residue, inactive mutant |
-, 759342 |
| 2.7.1.35 | D235A |
active site residue |
702038 |
| 2.7.1.35 | D235N |
active site residue |
702038 |
| 2.7.1.35 | D87H |
naturally occuring mutation, the mutant shows reduced catalytic activity and/or reduced affinity for PLP precursors, the mutant cannot complement the inactive Drosophila melanogaster dPdxk1 mutant when expressed in the mutant flies. Mutant D87H displays the highest damaging score (1.0). The D87H mutation strongly increases KM for PL, and to a lesser extent also increases KM for PN and PM, leaving KM for ATP and kcat almost unaltered |
760178 |
| 2.7.1.35 | G228A |
site-directed mutagenesis of a GXGD motif residue, inactive mutant |
-, 759342 |
