DPYS

From Wikipedia, the free encyclopedia

Dihydropyrimidinase

Identifiers

DPYS; DHP; DHPase

External IDs

OMIM: 222748 MGI: 1928679 HomoloGene: 20359

Gene ontology
Molecular Function:	• dihydropyrimidinase activity • hydrolase activity
Biological Process:	• nucleobase, nucleoside, nucleotide and nucleic acid metabolic process • response to toxin

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001385 (mRNA)
NP_001376 (protein)

NM_022722 (mRNA)
NP_073559 (protein)

Location

Chr 8: 105.46 - 105.55 Mb

Chr 15: 39.6 - 39.69 Mb

Pubmed search

[1]

[2]

Dihydropyrimidinase, also known as DPYS, is a human gene.^[1]

Dihydropyrimidinase catalyzes the conversion of 5,6-dihydrouracil to 3-ureidopropionate in pyrimidine metabolism. Dihydropyrimidinase is expressed at a high level in liver and kidney as a major 2.5-kb transcript and a minor 3.8-kb transcript. Defects in the DPYS gene are linked to dihydropyrimidinuria.^[1]

[edit] References

^ ^a ^b Entrez Gene: DPYS dihydropyrimidinase.

[edit] Further reading

Thomas HR, Ezzeldin HH, Guarcello V, et al. (2008). "Genetic regulation of beta-ureidopropionase and its possible implication in altered uracil catabolism.". Pharmacogenet. Genomics 18 (1): 25–35. doi:10.1097/FPC.0b013e3282f2f134. PMID 18216719.
Thomas HR, Ezzeldin HH, Guarcello V, et al. (2008). "Genetic regulation of dihydropyrimidinase and its possible implication in altered uracil catabolism.". Pharmacogenet. Genomics 17 (11): 973–87. doi:10.1097/FPC.0b013e3282f01788. PMID 18075467.
van Kuilenburg AB, Meijer J, Dobritzsch D, et al. (2007). "Clinical, biochemical and genetic findings in two siblings with a dihydropyrimidinase deficiency.". Mol. Genet. Metab. 91 (2): 157–64. doi:10.1016/j.ymgme.2007.02.008. PMID 17383919.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
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.
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.
Fukada M, Watakabe I, Yuasa-Kawada J, et al. (2001). "Molecular characterization of CRMP5, a novel member of the collapsin response mediator protein family.". J. Biol. Chem. 275 (48): 37957–65. doi:10.1074/jbc.M003277200. PMID 10956643.
Hamajima N, Kouwaki M, Vreken P, et al. (1998). "Dihydropyrimidinase deficiency: structural organization, chromosomal localization, and mutation analysis of the human dihydropyrimidinase gene.". Am. J. Hum. Genet. 63 (3): 717–26. PMID 9718352.
Hamajima N, Matsuda K, Sakata S, et al. (1997). "A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution.". Gene 180 (1-2): 157–63. PMID 8973361.
Naguib FN, el Kouni MH, Cha S (1985). "Enzymes of uracil catabolism in normal and neoplastic human tissues.". Cancer Res. 45 (11 Pt 1): 5405–12. PMID 3931905.

This article on a gene on chromosome 8 is a stub. You can help Wikipedia by expanding it.

v • d • e

Metabolism: amino acid metabolism - nucleotide enzymes

Purine metabolism

Pyrimidine metabolism

Anabolism	CAD (Carbamoyl phosphate synthase II, Aspartate carbamoyltransferase, Dihydroorotase) Dihydroorotate dehydrogenase - Orotidine 5'-phosphate decarboxylase/Uridine monophosphate synthetase CTP synthase

Catabolism	Dihydropyrimidine dehydrogenase - Dihydropyrimidinase/DPYS - Beta-ureidopropionase/UPB1