EC - Pteridine reductase

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IntEnz Enzyme Nomenclature


Accepted name:
pteridine reductase
Other names:
pteridine reductase 1
Systematic name:
5,6,7,8-tetrahydrobiopterin:NADP+ oxidoreductase



The enzyme from Leishmania (both amastigote and promastigote forms) catalyses the reduction by NADPH of folate and a wide variety of unconjugated pterins, including biopterin, to their tetrahydro forms. It also catalyses the reduction of 7,8-dihydropterins and 7,8-dihydrofolate to their tetrahydro forms. In contrast to EC (dihydrofolate reductase) and EC (6,7-dihydropteridine reductase), pteridine reductase will not catalyse 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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00060
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047040
CAS Registry Number: 131384-61-7


  1. Nare, B., Hardy, L. and Beverley, S.M.
    The roles of pteridine reductase 1 and dihydrofolate reductase-thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major.
    J. Biol. Chem. 272: 13883-13891 (1997). [PMID: 9153248]
  2. Gourley, D.G., Schüttelkopf, A.W., Leonard, G.A., Luba, J., Hardy, L.W., Beverley, S.M. and Hunter, W.N.
    Pteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites.
    Nat. Struct. Biol. 8: 521-525 (2001). [PMID: 11373620]
  3. Fitzpatrick, P.F.
    The aromatic amino acid hydroxylases.
    Adv. Enzymol. Relat. Areas Mol. Biol. 74: 235-294 (2000). [PMID: 10800597]

[EC created 1999 as EC, transferred 2003 to EC]