Sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming)
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+ 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
- ↑ Cho, S.H.; Na, J.U.; Youn, H.; Hwang, C.S.; Lee, C.H.; Kang, S.O. (1999). "Sepiapterin reductase producing L-threo-dihydrobiopterin from Chlorobium tepidum". Biochem. J. 340: 497–503. doi:10.1042/0264-6021:3400497. PMC 1220277. PMID 10333495.
- ↑ Supangat, S.; Choi, Y.K.; Park, Y.S.; Son, D.; Han, C.D.; Lee, K.H. (2005). "Expression, purification, crystallization and preliminary X-ray analysis of sepiapterin reductase from Chlorobium tepidum". Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (Pt 2): 202–204. doi:10.1107/S174430910403444X. PMC 1952253. 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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