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Literature summary extracted from
- Characterization of the dihydropterin reductase activity of pig liver methylenetetrahydrofolate reductase (1980), J. Biol. Chem., 255, 6014-6017.
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.5.1.20 | additional information | - |
additional information | Km for various dihydropterin derivatives | Sus scrofa |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.5.1.20 | Sus scrofa | - |
- |
- |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.20 | 1.2 | - |
- |
Sus scrofa |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.5.1.20 | 5,10-methylenetetrahydrofolate + NADPH | enzyme catalyzes the reduction of quinoid dihydropterins without a 5-substituent | Sus scrofa | 5-methyltetrahydrofolate + NADP+ | - |
? |  |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.5.1.20 | FAD | flavoprotein | Sus scrofa | |
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Release 2023.1 (January 2023)
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