Pteridine reductase

Pteridine reductase

In enzymology, a pteridine reductase is an enzyme that catalyzes the chemical reaction

5,6,7,8-tetrahydrobiopterin + 2 NADP+ rightleftharpoons biopterin + 2 NADPH + 2 H+

Thus, the two substrates of this enzyme are 5,6,7,8-tetrahydrobiopterin and NADP+, whereas its 3 products are biopterin, NADPH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5,6,7,8-tetrahydrobiopterin:NADP+ oxidoreductase. Other names in common use include PTR1, and pteridine reductase 1.

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and .


  • Nare B, Hardy LW, Beverley SM "The roles of pteridine reductase 1 and dihydrofolate reductase-thymidylate synthase in pteridine metabolism in the protozoan parasite Leishmania major". J. Biol. Chem. 272 13883–91.
  • SM, Hunter WN "Pteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites". Nat. Struct. Biol. 8 521–5.
  • Fitzpatrick PF "The aromatic amino acid hydroxylases". Adv. Enzymol. Relat. Areas. Mol. Biol. 74 235–94.

External links

The CAS registry number for this enzyme class is .

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