Pteridine reductase

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In enzymology, a pteridine reductase (EC 1.5.1.33) is an enzyme that catalyzes the chemical reaction

5,6,7,8-tetrahydrobiopterin + 2 NADP+ 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 1W0C, 2BF7, 2BFA, 2BFM, 2BFO, 2BFP, and 2C7V.

References

  • IUBMB entry for 1.5.1.33
  • BRENDA references for 1.5.1.33 (Recommended.)
  • PubMed references for 1.5.1.33
  • PubMed Central references for 1.5.1.33
  • Google Scholar references for 1.5.1.33
  • Nare B, Hardy LW, Beverley SM (1997). "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&ndash, 91. PMID 9153248.
  • SM, Hunter WN (2001). "Pteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites". Nat. Struct. Biol. 8: 521&ndash, 5. PMID 11373620.
  • Fitzpatrick PF (2000). "The aromatic amino acid hydroxylases". Adv. Enzymol. Relat. Areas. Mol. Biol. 74: 235&ndash, 94. PMID 10800597.

External links

The CAS registry number for this enzyme class is 131384-61-7.

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