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 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
Mcluskey, K., Gibellini, F., Carvalho, P., Avery, M., Hunter, W.
Acta Crystallogr.,Sect.D