EC Number   |
Protein Variants |
Reference |
|---|
    2.7.1.40 | A137T |
increased instability, increased sensitivity to the allosteric inhibitor/product |
674082 |
| 2.7.1.40 | A154T |
the mutation is associated with pyruvate kinase deficiency |
708661 |
| 2.7.1.40 | A394S/R479H |
the mutation is associated with pyruvate kinase deficiency |
708196 |
| 2.7.1.40 | Arg488X |
the mutation is associated with pyruvate kinase deficiency |
708661 |
| 2.7.1.40 | C436A |
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme |
721690 |
| 2.7.1.40 | C436D |
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme |
721690 |
| 2.7.1.40 | C436H |
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme |
721690 |
| 2.7.1.40 | C436M |
site-directed mutagenesis, crystal structure analysis, the mutant of L-PYK is the only residue 436 mutation that strengthens PEP affinity, revealing that the methionine substitution results in the ordering of several N-terminal residues that have not been ordered in previous structures |
721690 |
| 2.7.1.40 | C436N |
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme |
721690 |
| 2.7.1.40 | C436S |
site-directed mutagenesis, the mutant shows decreased affinity for phosphoenolpyruvate compared to the wild-type enzyme |
721690 |
