CATH Classification

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 2BFA
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structures of Leishmania Major Pteridine Reductase Complexes Reveal the Active Site Features Important for Ligand Binding and to Guide Inhibitor Design
Schuettelkopf, A.W., Hardy, L.W., Beverley, S.M., Hunter, W.N.
J.Mol.Biol.