Sepiapterin reductase is an enzyme that in humans is encoded by the SPRgene.[5][6][7]
Function
Sepiapterin reductase (7,8-dihydrobiopterin:NADP+ oxidoreductase; EC 1.1.1.153) catalyzes the NADPH-dependent reduction of various carbonyl substances, including derivatives of pteridines, and belongs to a group of enzymes called aldo-keto reductases. SPR plays an important role in the biosynthesis of tetrahydrobiopterin.[7]
Sepiapterin reductase deficiency belongs to the rare diseases. The clinical phenotype can include progressive psychomotor retardation, altered tone, seizures, choreoathetosis, temperature instability, hypersalivation, microcephaly, and irritability. Patients with sepiapterin reductase deficiency also manifest dystonia with diurnal variation, oculogyric crises, tremor, hypersomnolence, oculomotor apraxia, and weakness.[9] Response to treatment is variable and the long-term and functional outcome is unknown. To provide a basis for improving the understanding of the epidemiology, genotype/phenotype correlation and outcome of these diseases their impact on the quality of life of patients, and for evaluating diagnostic and therapeutic strategies a patient registry was established by the noncommercial International Working Group on Neurotransmitter Related Disorders (iNTD).[10]
Katoh S (1971). "Sepiapterin Reductase from Horse Liver: Purification and Properties of the Enzyme". Arch. Biochem. Biophys. 146 (1): 202–214. doi:10.1016/S0003-9861(71)80057-7. PMID4401291.
Takikawa S; Curtius HC; Redweik U; et al. (1987). "Biosynthesis of tetrahydrobiopterin. Purification and characterization of 6-pyruvoyl-tetrahydropterin synthase from human liver". Eur. J. Biochem. 161 (2): 295–302. doi:10.1111/j.1432-1033.1986.tb10446.x. PMID3536512. {{cite journal}}: Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)
Thöny B, Heizmann CW, Mattei MG (1995). "Human GTP-cyclohydrolase I gene and sepiapterin reductase gene map to region 14q21-q22 and 2p14-p12, respectively, by in situ hybridization". Genomics. 26 (1): 168–170. doi:10.1016/0888-7543(95)80101-Q. PMID7782081.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Maier J; Schott K; Werner T; et al. (1994). "Northern blot analysis of sepiapterin reductase mRNA in mammalian cell lines and tissues". Adv. Exp. Med. Biol. 338: 195–8. doi:10.1007/978-1-4615-2960-6_39. PMID8304109. {{cite journal}}: Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)
Maier J; Schott K; Werner T; et al. (1993). "Detection of a novel sepiapterin reductase mRNA: assay of mRNA in various cells and tissues of various species". Exp. Cell Res. 204 (2): 217–222. doi:10.1006/excr.1993.1027. PMID8440319. {{cite journal}}: Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)
Suzuki Y; Yoshitomo-Nakagawa K; Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID9373149. {{cite journal}}: Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)
Blau N; Thöny B; Renneberg A; et al. (1998). "Dihydropteridine reductase deficiency localized to the central nervous system". J. Inherit. Metab. Dis. 21 (4): 433–434. doi:10.1023/A:1005327313348. PMID9700606. {{cite journal}}: Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)
Ohye T; Hori TA; Katoh S; et al. (1998). "Genomic organization and chromosomal localization of the human sepiapterin reductase gene". Biochem. Biophys. Res. Commun. 251 (2): 597–602. doi:10.1006/bbrc.1998.9503. PMID9792819. {{cite journal}}: Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)
Blau N; Thöny B; Renneberg A; et al. (1999). "Variant of dihydropteridine reductase deficiency without hyperphenylalaninaemia: effect of oral phenylalanine loading". J. Inherit. Metab. Dis. 22 (3): 216–220. doi:10.1023/A:1005584627797. PMID10384371. {{cite journal}}: Unknown parameter |name-list-format= ignored (|name-list-style= suggested) (help)