CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family

Enzyme Information
Pteridine reductase.
based on mapping to UniProt O76290
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 and EC, 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 in being specific for the B side of NADPH. -!- Formerly EC
6,7-dihydropteridine reductase.
based on mapping to UniProt O76290
A 5,6,7,8-tetrahydropteridine + NAD(P)(+) = a 6,7-dihydropteridine + NAD(P)H.
-!- The substrate is the quinonoid form of dihydropteridine. -!- Not identical with EC -!- Formerly EC and EC

UniProtKB Entries (1)

Trypanosoma brucei brucei
Pteridine reductase

PDB Structure

External Links
Primary Citation
Structure-Based Design and Synthesis of Antiparasitic Pyrrolopyrimidines Targeting Pteridine Reductase 1.
Khalaf, A.I., Huggan, J.K., Suckling, C.J., Gibson, C.L., Stewart, K., Giordani, F., Barrett, M.P., Wong, P.E., Barrack, K.L., Hunter, W.N.