Pteridine reductase

Pteridine reductase
Identifiers
EC no.	1.5.1.33
CAS no.	131384-61-7
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

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⁺${\displaystyle \rightleftharpoons }$ 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 1W0C, 2BF7, 2BFA, 2BFM, 2BFO, 2BFP, and 2C7V.

References

• 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 (21): 13883–91. doi: 10.1074/jbc.272.21.13883 . PMID   9153248.
• Gourley DG, Schüttelkopf AW, Leonard GA, Luba J, Hardy LW, Beverley SM, Hunter WN (2001). "Pteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites". Nat. Struct. Biol. 8 (6): 521–5. doi:10.1038/88584. PMID   11373620. S2CID   32379320.
• Fitzpatrick PF (2000). "The Aromatic Amino Acid Hydroxylases". Advances in Enzymology and Related Areas of Molecular Biology. Vol. 74. pp. 235–94. doi:10.1002/9780470123201.ch6. ISBN   978-0-470-12320-1. PMID   10800597.