EC Number   |
Protein Variants |
Reference |
|---|
    1.3.1.2 | A551T |
natural mutation identified in a human with complete loss of enzymic activity. Crystallization data of Sus scrofa recombinant mutant, mutation might prevent binding of the prosthetic group FMN and affect folding of the enzyme protein |
672471 |
| 1.3.1.2 | A551T |
natural mutation identified in a patient with complete loss of enzymic activity |
672471 |
| 1.3.1.2 | C126A |
site-directed mutagenesis, a potential [4Fe-4S]-cluster binding residue, the mutant shows slightly increased activity compared to the wild-type enzyme |
711309 |
| 1.3.1.2 | C671A |
1% activity compared to that of the wild-type enzyme |
349226 |
| 1.3.1.2 | C671A |
mutation eliminates the proton-coupled electron transfer required to reduce pyrimidine substrates |
762737 |
| 1.3.1.2 | C671S |
mutation of the pyrimidine site candidate general acid, slows the turnover of the enzyme by approximately 60fold for uracil and 1600fold for thymine |
762734 |
| 1.3.1.2 | C671S |
variant exhibits both delineation of reductive activation into two phases at low pH values and exceptionally slow turnover with thymine |
762737 |
| 1.3.1.2 | E244V |
natural mutation identified in a human with complete loss of enzymic activity. Crystallization data of Sus scrofa recombinant mutant, mutation interferes with the electron flow between NADPH and the pyrimidine binding site of the enzyme |
672471 |
| 1.3.1.2 | E244V |
natural mutation identified in a patient with complete loss of enzymic activity |
672471 |
| 1.3.1.2 | G366A |
natural mutation, marked decrease in enzyme affinity to NADPH, reduction of Vmax for 5-fluorouracil degrading activity |
673116 |
