Structural highlights
Function
SPRE_CHLTE Catalyzes the final reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Cho SH, Na JU, Youn H, Hwang CS, Lee CH, Kang SO. Sepiapterin reductase producing L-threo-dihydrobiopterin from Chlorobium tepidum. Biochem J. 1999 Jun 1;340 ( Pt 2):497-503. PMID:10333495
- ↑ Choi YK, Jun SR, Cha EY, Park JS, Park YS. Sepiapterin reductases from Chlorobium tepidum and Chlorobium limicola catalyze the synthesis of L-threo-tetrahydrobiopterin from 6-pyruvoyltetrahydropterin. FEMS Microbiol Lett. 2005 Jan 1;242(1):95-9. PMID:15621425 doi:http://dx.doi.org/10.1016/j.femsle.2004.10.044
- ↑ Supangat S, Park SO, Seo KH, Lee SY, Park YS, Lee KH. Role of Phe-99 and Trp-196 of sepiapterin reductase from Chlorobium tepidum in the production of L-threo-tetrahydrobiopterin. Acta Biochim Biophys Sin (Shanghai). 2008 Jun;40(6):513-8. PMID:18542834