CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.720 | NAD(P)-binding Rossmann-like Domain |
Domain Context
CATH Clusters
| Superfamily | NAD(P)-binding Rossmann-like Domain |
| Functional Family | Pteridine reductase |
Enzyme Information
| 1.5.1.33 |
Pteridine reductase.
based on mapping to UniProt Q01782
5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = biopterin + 2 NADPH.
-!- 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.
|
UniProtKB Entries (1)
| Q01782 |
PTR1_LEIMA
Leishmania major
Pteridine reductase 1
|
PDB Structure
| PDB | 1W0C |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Inhibition of Leishmania Major Pteridine Reductase by 2,4,6-Triaminoquinazoline: Structure of the Nadph Ternary Complex
Acta Crystallogr.,Sect.D
|
