Pteridine reductase (EC 1.5.1.33) is an enzyme that catalyzes the chemical reaction
| 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 | ||||||||
| |||||||||
-Tetrahydrobiopterin_structure.svg)
The substrates of this enzyme are biopterin, reduced nicotinamide adenine dinucleotide phosphate (NADPH), and two protons. Its products are tetrahydrobiopterin and oxidised NADP+.[1][2] It was isolated from the parasite Leishmania major.[3]
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.[4]
Structural studies
editReferences
edit- ↑ Enzyme 1.5.1.33 at KEGG Pathway Database.
- ↑ 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.
- ↑ 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.
- ↑ 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.
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