Biology:Sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming)
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| Sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming) | |||||||||
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| Identifiers | |||||||||
| EC number | 1.1.1.325 | ||||||||
| CAS number | 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 | ||||||||
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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
- (1) L-threo-7,8-dihydrobiopterin + NADP+ [math]\displaystyle{ \rightleftharpoons }[/math] sepiapterin + NADPH + H+
- (2) L-threo-tetrahydrobiopterin + 2 NADP+ [math]\displaystyle{ \rightleftharpoons }[/math] 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
- ↑ "Sepiapterin reductase producing L-threo-dihydrobiopterin from Chlorobium tepidum". The Biochemical Journal 340 ( Pt 2): 497–503. June 1999. doi:10.1042/0264-6021:3400497. PMID 10333495.
- ↑ "Expression, purification, crystallization and preliminary X-ray analysis of sepiapterin reductase from Chlorobium tepidum". Acta Crystallographica Section F 61 (Pt 2): 202–4. February 2005. doi:10.1107/S174430910403444X. PMID 16510994.
External links
- Sepiapterin+reductase+(L-threo-7,8-dihydrobiopterin+forming) at the US National Library of Medicine Medical Subject Headings (MeSH)
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