Coproporphyrinogen III oxidase

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

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

CPOX
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2AEX
Identifiers
Aliases	CPOX, CPO, CPX, HCP, coproporphyrinogen oxidase, COX, HARPO
External IDs	OMIM: 612732; MGI: 104841; HomoloGene: 76; GeneCards: CPOX; OMA:CPOX - orthologs
EC number	1.3.3.3
Gene location (Mouse)
Chr.	Chromosome 16 (mouse)
End	58,537,999 bp
RNA expression pattern
	Top expressed in
	trabecular bone; ; jejunal mucosa; ; corpus callosum; ; right lobe of liver; ; bone marrow; ; inferior ganglion of vagus nerve; ; bone marrow cells; ; rectum; ; monocyte; ; duodenum;
	Top expressed in
	human fetus; ; atrium; ; tibiofemoral joint; ; fetal liver hematopoietic progenitor cell; ; yolk sac; ; epithelium of small intestine; ; right kidney; ; pontine nuclei; ; ventral tegmental area; ; habenula;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	coproporphyrinogen oxidase activity; protein homodimerization activity; structural constituent of eye lens; identical protein binding; oxidoreductase activity;
Cellular component	membrane; mitochondrial intermembrane space; mitochondrion; mitochondrial inner membrane; cytosol; cytoplasm;
Biological process	response to arsenic-containing substance; protoporphyrinogen IX biosynthetic process; porphyrin-containing compound biosynthetic process; response to iron ion; heme biosynthetic process; response to lead ion; response to inorganic substance; response to insecticide; response to methylmercury; protoporphyrinogen IX biosynthetic process from glutamate;
	Sources:Amigo / QuickGO
Orthologs
	1371
	12892
	n/a
	ENSMUSG00000022742
	P36551
	P36552
	NM_000097
	NM_007757
	NP_000088
	NP_031783
	Wikidata
View/Edit Human	View/Edit Mouse

Coproporphyrinogen-III oxidase, mitochondrial (abbreviated as CPOX) is an enzyme that in humans is encoded by the CPOX gene.^[4]^[5]^[6] 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.^[7]^[8]

CPOX, the sixth enzyme of the haem biosynthetic pathway, converts coproporphyrinogen III to protoporphyrinogen IX through two sequential steps of oxidative decarboxylation.^[9] The activity of the CPOX enzyme, located in the mitochondrial membrane, is measured in lymphocytes.^[10]

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000022742 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Lamoril J, Martasek P, Deybach JC, Da Silva V, Grandchamp B, Nordmann Y (February 1995). "A molecular defect in coproporphyrinogen oxidase gene causing harderoporphyria, a variant form of hereditary coproporphyria". Human Molecular Genetics. 4 (2): 275–8. doi:10.1093/hmg/4.2.275. PMID 7757079.
^ Kohno H, Furukawa T, Yoshinaga T, Tokunaga R, Taketani S (October 1993). "Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation". The Journal of Biological Chemistry. 268 (28): 21359–63. doi:10.1016/S0021-9258(19)36931-5. PMID 8407975.
^ "Entrez Gene: CPOX coproporphyrinogen oxidase".
^ "Hereditary coproporphyria". Genetic and Rare Diseases Information Center. National Institutes of Health. Archived from the original on 7 August 2012. Retrieved 8 August 2011.
^ "CPOX". Genetics Home Reference. Retrieved 8 August 2011.
^ Sano S, Granick S (April 1961). "Mitochondrial coproporphyrinogen oxidase and protoporphyrin formation". The Journal of Biological Chemistry. 236 (4): 1173–80. doi:10.1016/S0021-9258(18)64262-0. PMID 13746277.
^ Guo R, Lim CK, Peters TJ (October 1988). "Accurate and specific HPLC assay of coproporphyrinogen III oxidase activity in human peripheral leucocytes". Clinica Chimica Acta; International Journal of Clinical Chemistry. 177 (3): 245–52. doi:10.1016/0009-8981(88)90069-1. PMID 3233772.

[refGRCm38Ensembl-1] GRCm38: Ensembl release 89: ENSMUSG00000022742 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7757079-4] Lamoril J, Martasek P, Deybach JC, Da Silva V, Grandchamp B, Nordmann Y (February 1995). "A molecular defect in coproporphyrinogen oxidase gene causing harderoporphyria, a variant form of hereditary coproporphyria". Human Molecular Genetics. 4 (2): 275–8. doi:10.1093/hmg/4.2.275. PMID 7757079.

[pmid8407975-5] Kohno H, Furukawa T, Yoshinaga T, Tokunaga R, Taketani S (October 1993). "Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation". The Journal of Biological Chemistry. 268 (28): 21359–63. doi:10.1016/S0021-9258(19)36931-5. PMID 8407975.

[entrez-6] "Entrez Gene: CPOX coproporphyrinogen oxidase".

[7] "Hereditary coproporphyria". Genetic and Rare Diseases Information Center. National Institutes of Health. Archived from the original on 7 August 2012. Retrieved 8 August 2011.

[8] "CPOX". Genetics Home Reference. Retrieved 8 August 2011.

[pmid13746277-9] Sano S, Granick S (April 1961). "Mitochondrial coproporphyrinogen oxidase and protoporphyrin formation". The Journal of Biological Chemistry. 236 (4): 1173–80. doi:10.1016/S0021-9258(18)64262-0. PMID 13746277.

[pmid3233772-10] Guo R, Lim CK, Peters TJ (October 1988). "Accurate and specific HPLC assay of coproporphyrinogen III oxidase activity in human peripheral leucocytes". Clinica Chimica Acta; International Journal of Clinical Chemistry. 177 (3): 245–52. doi:10.1016/0009-8981(88)90069-1. PMID 3233772.

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