Coproporphyrinogen dehydrogenase
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In enzymology, coproporphyrinogen dehydrogenase (EC 1.3.98.3) is an enzyme that catalyzes the chemical reaction
| coproporphyrinogen dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.98.3 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The two substrates of this enzyme are coproporphyrinogen III and S-adenosyl methionine (SAM). Its products are protoporphyrinogen IX, carbon dioxide, methionine, and 5'-deoxyadenosine.[1][2] It is an example of a radical SAM enzyme.[3][4]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is coproporphyrinogen-III:S-adenosyl-L-methionine oxidoreductase (decarboxylating). Other names in common use include oxygen-independent coproporphyrinogen-III oxidase, HemF, HemN, radical SAM enzyme, and coproporphyrinogen III oxidase. This enzyme participates in the biosynthesis of porphyrins and chlorophyll. HemN is the oxygen-independent oxidase produced in Escherichia coli. HemF is the oxygen-dependent oxidase within E. coli. Importantly, only HemN utilizes S-adenosyl methionine. Human variants of Coproporphyrinogen oxidase are cofactor-independent.[5][6]
See also
- Coproporphyrinogen III oxidase, which catalyses the same reaction but using oxygen as oxidant
