Coproporphyrinogen III oxidase

Coproporphyrinogen oxidase
PDB rendering based on 2aex.
Available structures PDB 2aex
Identifiers
Symbols	CPOX; CPO; CPX; HCP
External IDs	OMIM: 612732 MGI: 104841 HomoloGene: 76 GeneCards: CPOX Gene
EC number	1.3.3.3
Gene Ontology Molecular function • coproporphyrinogen oxidase activity • oxidoreductase activity • protein homodimerization activity Cellular component • cytoplasm • mitochondrion • mitochondrial inner membrane • mitochondrial intermembrane space Biological process • porphyrin metabolic process • protoporphyrinogen IX biosynthetic process • heme biosynthetic process • response to iron ion • response to lead ion • response to insecticide • response to arsenic-containing substance • response to methylmercury Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1371	12892
Ensembl	ENSG00000080819	ENSMUSG00000022742
UniProt	P36551	Q3U029
RefSeq (mRNA)	NM_000097.5	NM_007757.2
RefSeq (protein)	NP_000088.3	NP_031783.2
Location (UCSC)	Chr 3: 98.24 – 98.31 Mb	Chr 16: 58.67 – 58.68 Mb
PubMed search	[1]	[2]

Coprogen_oxidas
coproporphyrinogen iii oxidase from leishmania major
Identifiers
Symbol	Coprogen_oxidas
Pfam	PF01218
InterPro	IPR001260
PROSITE	PDOC00783
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

Coproporphyrinogen-III oxidase, mitochondrial is an enzyme that in humans is encoded by the CPOX gene.^[1][2][3] A genetic defect in the enzyme results in a reduced production of heme in animals. The medical condition associated with this enzyme defect is called hereditary coproporphyria.^{[4] [5]}

It is an enzyme involved in the sixth step of porphyrin metabolism it catalyses the oxidative decarboxylation of coproporphyrinogen III to proto-porphyrinogen IX in the haem and chlorophyll biosynthetic pathways.^[2][6] The protein is a homodimer containing two internally bound iron atoms per molecule of native protein.^[7] The enzyme is active in the presence of molecular oxygen that acts as an electron acceptor. The enzyme is widely distributed having been found in a variety of eukaryotic and prokaryotic sources.

References

1. ^ Lamoril J, Martasek P, Deybach JC, Da Silva V, Grandchamp B, Nordmann Y (Jun 1995). "A molecular defect in coproporphyrinogen oxidase gene causing harderoporphyria, a variant form of hereditary coproporphyria". Hum Mol Genet 4 (2): 275–8. doi:10.1093/hmg/4.2.275. PMID 7757079. 
2. ^ ^{a b} Kohno H, Furukawa T, Yoshinaga T, Tokunaga R, Taketani S (Nov 1993). "Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation". J Biol Chem 268 (28): 21359–63. PMID 8407975. 
3. ^ "Entrez Gene: CPOX coproporphyrinogen oxidase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1371. 
4. ^ "Hereditary coproporphyria". Genetic and Rare Diseases Information Center. National Institutes of Health. http://rarediseases.info.nih.gov/GARD/Condition/6619/Coproporphyria.aspx. Retrieved 8 August 2011. 
5. ^ "CPOX". Genetics Home Reference. http://ghr.nlm.nih.gov/gene/CPOX. Retrieved 8 August 2011. 
6. ^ Madsen O, Sandal L, Sandal NN, Marcker KA (October 1993). "A soybean coproporphyrinogen oxidase gene is highly expressed in root nodules". Plant Mol. Biol. 23 (1): 35–43. doi:10.1007/BF00021417. PMID 8219054. 
7. ^ Camadro JM, Chambon H, Jolles J, Labbe P (May 1986). "Purification and properties of coproporphyrinogen oxidase from the yeast Saccharomyces cerevisiae". Eur. J. Biochem. 156 (3): 579–87. doi:10.1111/j.1432-1033.1986.tb09617.x. PMID 3516695. 

Further reading

• 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. doi:10.1093/hmg/3.10.1807. 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. doi:10.1007/BF00211026. 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. doi:10.1093/hmg/3.8.1325. 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. doi:10.1093/hmg/3.3.477. 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. doi:10.1016/0378-1119(94)90802-8. 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. doi:10.1073/pnas.91.8.3024. PMC 43507. PMID 8159699. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=43507. 
• 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. doi:10.1016/0005-2728(94)90083-3. PMID 8286403. 
• 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. doi:10.1007/s004390050338. 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. doi:10.1016/S0378-1119(97)00411-3. 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. doi:10.1002/(SICI)1096-8628(19981116)80:3<204::AID-AJMG4>3.0.CO;2-G. 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. doi:10.1046/j.1432-1327.2001.02045.x. 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. doi:10.1086/320118. PMC 1226094. PMID 11309681. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1226094. 
• 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. doi:10.1385/JMN:18:3:229. 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)

External links

• MeSH Coproporphyrinogen+III+Oxidases

This article includes text from the public domain Pfam and InterPro IPR001260