Sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming) (EC 1.1.1.325) is an enzyme with systematic name L-threo-7,8-dihydrobiopterin:NADP+ oxidoreductase.[1][2] This enzyme catalyses the following chemical reaction
| Sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.325 | ||||||||
| CAS no. | 9059-48-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- (1) L-threo-7,8-dihydrobiopterin + NADP+ sepiapterin + NADPH + H+
- (2) L-threo-tetrahydrobiopterin + 2 NADP+ 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH + 2 H+
This bacterial (Chlorobium tepidum) enzyme catalyses the final step in the de novo synthesis of tetrahydrobiopterin from GTP.
References
edit- ^ Cho SH, Na JU, Youn H, Hwang CS, Lee CH, Kang SO (June 1999). "Sepiapterin reductase producing L-threo-dihydrobiopterin from Chlorobium tepidum". The Biochemical Journal. 340 ( Pt 2): 497–503. doi:10.1042/0264-6021:3400497. PMC 1220277. PMID 10333495.
- ^ Supangat S, Choi YK, Park YS, Son D, Han CD, Lee KH (February 2005). "Expression, purification, crystallization and preliminary X-ray analysis of sepiapterin reductase from Chlorobium tepidum". Acta Crystallographica Section F. 61 (Pt 2): 202–4. doi:10.1107/S174430910403444X. PMC 1952253. PMID 16510994.
External links
edit- Sepiapterin+reductase+(L-threo-7,8-dihydrobiopterin+forming) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
