SPR (gene)

From Wikipedia, the free encyclopedia

Sepiapterin reductase (7,8-dihydrobiopterin:NADP+ oxidoreductase)

PDB rendering based on 1z6z.

Available structures: 1z6z

Identifiers

Symbol(s)

SPR;

External IDs

OMIM: 182125 MGI: 103078 HomoloGene: 37735

Gene ontology
Molecular Function:	• aldo-keto reductase activity • sepiapterin reductase activity • oxidoreductase activity • NADP binding
Biological Process:	• electron transport • tetrahydrobiopterin biosynthetic process • nitric oxide biosynthetic process • metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003124 (mRNA)
NP_003115 (protein)

NM_011467 (mRNA)
NP_035597 (protein)

Location

Chr 2: 72.97 - 72.97 Mb

Chr 6: 85.1 - 85.1 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: SPR sepiapterin reductase (7,8-dihydrobiopterin:NADP+ oxidoreductase).

[edit] 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.