EC Number | Cloned (Comment) | Organism |
---|---|---|
1.3.1.2 | expression in Escherichia coli | Sus scrofa |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.3.1.2 | 5-Ethynyluracil | covalently inactivates DPD by cross-linking with the active-site general acid cysteine in the pyrimidine binding site. This reaction is dependent on the simultaneous binding of 5-ethynyluracil and NADPH. The ternary complex induces DPD to become activated by taking up two electrons from the NADPH. The covalent inactivation of DPD by 5-ethynyluracil occurs concomitantly with this reductive activation with a rate constant of about 0.2 per s. This kinact value is correlated with the rate of reduction of one of the two flavin cofactors and the localization of a mobile loop in the pyrimidine active site | Sus scrofa |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.3.1.2 | Sus scrofa | Q28943 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.1.2 | 5-fluorouracil + NADPH + H+ | - |
Sus scrofa | 5-fluoro-5,6-dihydrouracil + NADP+ | - |
? |