| Accepted Name |
| Pteridine reductase.
|
| Alternative Name(s) |
| Pteridine reductase 1. |
| PTR1. |
| Reaction catalysed |
| 5,6,7,8-tetrahydrobiopterin + 2 NADP(+) <=> biopterin + 2 NADPH |
| Comment(s) |
- The enzyme from Leishmania (both amastigote and promastigote forms)
catalyzes the NADPH-dependent reduction of folate and a wide variety
of unconjugated pterins, including biopterin, to their tetrahydro
forms.
- It also catalyzes the reduction of 7,8-dihydropterins and 7,8-
dihydrofolate to their tetrahydro forms.
- In contrast to EC 1.5.1.3 and EC 1.5.1.34, pteridine reductase will
not catalyze the reduction of the quinonoid form of dihydrobiopterin.
- The enzyme is specific for NADPH; no activity has been detected with
NADH.
- It also differs from EC 1.5.1.3 in being specific for the B side of
NADPH.
- Formerly EC 1.1.1.253.
|
| Cross-references |
| PROSITE | PDOC00060 |
| BRENDA | 1.5.1.33 |
| EC2PDB | 1.5.1.33 |
| PRIAM enzyme-specific profiles | 1.5.1.33 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.5.1.33 |
| IUBMB Enzyme Nomenclature | 1.5.1.33 |
| IntEnz | 1.5.1.33 |
| MEDLINE | Find literature relating to 1.5.1.33 |
| MetaCyc | 1.5.1.33 |
| UniProtKB/Swiss-Prot |
|