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SPR (gene)

Introduction

Sepiapterin reductase (7,8-dihydrobiopterin:NADP+ oxidoreductase), also known as SPR, is a human gene.[1]

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 (see MIM 261640).[supplied by OMIM][1]

References

References

  1. ↑ 1.0 1.1 “Entrez Gene: SPR sepiapterin reductase (7,8-dihydrobiopterin:NADP+ oxidoreductase)”.
Further reading

Further reading

  • Ichinose H, Katoh S, Sueoka T; et al. (1991). “Cloning and sequencing of cDNA encoding human sepiapterin reductase–an enzyme involved in tetrahydrobiopterin biosynthesis”. Biochem. Biophys. Res. Commun. 179 (1): 183–9. PMID 1883349.
  • 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. PMID 3536512.
  • 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): 168–70. PMID 7782081.
  • Maruyama K, Sugano S (1994). “Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene. 138 (1–2): 171–4. PMID 8125298.
  • 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. PMID 8304109.
  • 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): 217–22. doi:10.1006/excr.1993.1027. PMID 8440319.
  • 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): 149–56. PMID 9373149.
  • Blau N, Thöny B, Renneberg A; et al. (1998). “Dihydropteridine reductase deficiency localized to the central nervous system”. J. Inherit. Metab. Dis. 21 (4): 433–4. PMID 9700606.
  • 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. PMID 9792819.
  • 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): 216–20. PMID 10384371.
  • Bonafé L, Thöny B, Penzien JM; et al. (2001). “Mutations in the sepiapterin reductase gene cause a novel tetrahydrobiopterin-dependent monoamine-neurotransmitter deficiency without hyperphenylalaninemia”. Am. J. Hum. Genet. 69 (2): 269–77. PMID 11443547.
  • Fujimoto K, Takahashi SY, Katoh S (2002). “Mutational analysis of sites in sepiapterin reductase phosphorylated by Ca2+/calmodulin-dependent protein kinase II”. Biochim. Biophys. Acta. 1594 (1): 191–8. PMID 11825621.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Franscini N, Bachli EB, Blau N; et al. (2005). “Functional tetrahydrobiopterin synthesis in human platelets”. Circulation. 110 (2): 186–92. doi:10.1161/01.CIR.0000134281.82972.57. PMID 15197144.
  • Steinberger D, Blau N, Goriuonov D; et al. (2005). “Heterozygous mutation in 5′-untranslated region of sepiapterin reductase gene (SPR) in a patient with dopa-responsive dystonia”. Neurogenetics. 5 (3): 187–90. doi:10.1007/s10048-004-0182-3. PMID 15241655.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Sharma M, Mueller JC, Zimprich A; et al. (2006). “The sepiapterin reductase gene region reveals association in the PARK3 locus: analysis of familial and sporadic Parkinson’s disease in European populations”. J. Med. Genet. 43 (7): 557–62. doi:10.1136/jmg.2005.039149. PMID 16443856.
  • Farrugia R, Scerri CA, Montalto SA; et al. (2007). “Molecular genetics of tetrahydrobiopterin (BH4) deficiency in the Maltese population”. Mol. Genet. Metab. 90 (3): 277–83. doi:10.1016/j.ymgme.2006.10.013. PMID 17188538.
  • Tobin JE, Cui J, Wilk JB; et al. (2007). “Sepiapterin reductase expression is increased in Parkinson’s disease brain tissue”. Brain Res. 1139: 42–7. doi:10.1016/j.brainres.2007.01.001. PMID 17270157.

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