CPOX
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "CPOX".

content
Coproporphyrinogen oxidase
PDB rendering based on 2aex.
Available structures: 2aex
Identifiers
Symbol(s) CPOX; HCP; CPO; CPX
External IDs OMIM: 121300 MGI: 104841 HomoloGene: 76
EC number 1.3.3.3
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 1371 12892
Ensembl ENSG00000080819 ENSMUSG00000022742
Uniprot P36551 Q3U029
Refseq NM_000097 (mRNA)
NP_000088 (protein)		 NM_007757 (mRNA)
NP_031783 (protein)
Location Chr 3: 99.78 - 99.8 Mb Chr 16: 58.61 - 58.62 Mb
Pubmed search [1] [2]

Coproporphyrinogen oxidase, also known as CPOX, is a human gene.[1]

Coproporphyrinogen III oxidase is an enzyme involved in the sixth step of porphyrin metabolism, converting coproporphyrinogen III to protoporphyrinogen IX.

References

  1. ^ "Entrez Gene: CPOX coproporphyrinogen oxidase".

Further reading

  • Lamoril J, Martasek P, Deybach JC, et al. (1995). "A molecular defect in coproporphyrinogen oxidase gene causing harderoporphyria, a variant form of hereditary coproporphyria.". Hum. Mol. Genet. 4 (2): 275–8. PMID 7757079. 
  • Fujita H, Kondo M, Taketani S, et al. (1995). "Characterization and expression of cDNA encoding coproporphyrinogen oxidase from a patient with hereditary coproporphyria.". Hum. Mol. Genet. 3 (10): 1807–10. PMID 7849704. 
  • Cacheux V, Martasek P, Fougerousse F, et al. (1994). "Localization of the human coproporphyrinogen oxidase gene to chromosome band 3q12.". Hum. Genet. 94 (5): 557–9. PMID 7959694. 
  • Delfau-Larue MH, Martasek P, Grandchamp B (1995). "Coproporphyrinogen oxidase: gene organization and description of a mutation leading to exon 6 skipping.". Hum. Mol. Genet. 3 (8): 1325–30. PMID 7987309. 
  • Martasek P, Nordmann Y, Grandchamp B (1994). "Homozygous hereditary coproporphyria caused by an arginine to tryptophane substitution in coproporphyrinogen oxidase and common intragenic polymorphisms.". Hum. Mol. Genet. 3 (3): 477–80. PMID 8012360. 
  • 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. 
  • Martasek P, Camadro JM, Delfau-Larue MH, et al. (1994). "Molecular cloning, sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase.". Proc. Natl. Acad. Sci. U.S.A. 91 (8): 3024–8. PMID 8159699. 
  • Taketani S, Kohno H, Furukawa T, et al. (1994). "Molecular cloning, sequencing and expression of cDNA encoding human coproporphyrinogen oxidase.". Biochim. Biophys. Acta 1183 (3): 547–9. PMID 8286403. 
  • Kohno H, Furukawa T, Yoshinaga T, et al. (1993). "Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation.". J. Biol. Chem. 268 (28): 21359–63. PMID 8407975. 
  • Lamoril J, Deybach JC, Puy H, et al. (1997). "Three novel mutations in the coproporphyrinogen oxidase gene.". Hum. Mutat. 9 (1): 78–80. doi:10.1002/(SICI)1098-1004(1997)9:1<78::AID-HUMU17>3.0.CO;2-M. PMID 8990017. 
  • Daimon M, Gojyou E, Sugawara M, et al. (1997). "A novel missense mutation in exon 4 of the human coproporphyrinogen oxidase gene in two patients with hereditary coproporphyria.". Hum. Genet. 99 (2): 199–201. PMID 9048920. 
  • Schreiber WE, Zhang X, Senz J, Jamani A (1997). "Hereditary coproporphyria: exon screening by heteroduplex analysis detects three novel mutations in the coproporphyrinogen oxidase gene.". Hum. Mutat. 10 (3): 196–200. doi:10.1002/(SICI)1098-1004(1997)10:3<196::AID-HUMU3>3.0.CO;2-H. PMID 9298818. 
  • 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. 
  • Lamoril J, Puy H, Gouya L, et al. (1998). "Neonatal hemolytic anemia due to inherited harderoporphyria: clinical characteristics and molecular basis.". Blood 91 (4): 1453–7. PMID 9454777. 
  • Susa S, Daimon M, Kondo H, et al. (1999). "Identification of a novel mutation of the CPO gene in a Japanese hereditary coproporphyria family.". Am. J. Med. Genet. 80 (3): 204–6. PMID 9843038. 
  • Rosipal R, Lamoril J, Puy H, et al. (1999). "Systematic analysis of coproporphyrinogen oxidase gene defects in hereditary coproporphyria and mutation update.". Hum. Mutat. 13 (1): 44–53. doi:10.1002/(SICI)1098-1004(1999)13:1<44::AID-HUMU5>3.0.CO;2-Q. PMID 9888388. 
  • Taketani S, Furukawa T, Furuyama K (2001). "Expression of coproporphyrinogen oxidase and synthesis of hemoglobin in human erythroleukemia K562 cells.". Eur. J. Biochem. 268 (6): 1705–11. PMID 11248690. 
  • Lamoril J, Puy H, Whatley SD, et al. (2001). "Characterization of mutations in the CPO gene in British patients demonstrates absence of genotype-phenotype correlation and identifies relationship between hereditary coproporphyria and harderoporphyria.". Am. J. Hum. Genet. 68 (5): 1130–8. PMID 11309681. 
  • Elkon H, Don J, Melamed E, et al. (2003). "Mutant and wild-type alpha-synuclein interact with mitochondrial cytochrome C oxidase.". J. Mol. Neurosci. 18 (3): 229–38. PMID 12059041. 
  • Wiman A, Floderus Y, Harper P (2002). "Two novel mutations and coexistence of the 991C>T and the 1339C>T mutation on a single allele in the coproporphyrinogen oxidase gene in Swedish patients with hereditary coproporphyria.". J. Hum. Genet. 47 (8): 407–12. doi:10.1007/s100380200059. PMID 12181641. 


Heme synthesis—note that some reactions occur in the cytoplasm and some in the mitochondrion (yellow)
Heme synthesis—note that some reactions occur in the cytoplasm and some in the mitochondrion (yellow)

External links

 This oxidoreductase article is a stub. You can help Wikipedia by expanding it.
v • d • e
Oxidoreductases: CH-CH oxidoreductases (EC 1.3)
1.3.1. NAD/NADP acceptor
1.3.3. Oxygen acceptor
Dihydroorotate dehydrogenase - Coproporphyrinogen III oxidase - Protoporphyrinogen oxidase -
1.3.5. Quinone
1.3.99. Other acceptors
v • d • e
Metabolism: amino acid metabolism - porphyrin enzymes
Porphyrin biosynthesis
Heme breakdown to bile


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