Coproporphyrinogen dehydrogenase

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coproporphyrinogen dehydrogenase
EC number
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

In enzymology, a coproporphyrinogen dehydrogenase (EC is an enzyme that catalyzes the chemical reaction

coproporphyrinogen III + 2 S-adenosyl-L-methionine protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine

Thus, the two substrates of this enzyme are coproporphyrinogen III and S-adenosyl-L-methionine, whereas its 4 products are protoporphyrinogen IX, CO2, L-methionine, and 5'-deoxyadenosine.

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 porphyrin and chlorophyll metabolism. HemN is the Oxygen-independent oxidase produced in E. coli. HemF is the oxygen-dependent oxidase within E. coli. Importantly, only HemN utilizes S-adenosyl Methionine (SAM). Human variants of Coproporphyrinogen oxidase are cofactor-independent.[1][2][3]


  1. ^ Fetzner, Susanne; Steiner, Roberto A. (2010-02-16). "Cofactor-independent oxidases and oxygenases". Applied Microbiology and Biotechnology. 86 (3): 791–804. doi:10.1007/s00253-010-2455-0. ISSN 0175-7598. 
  2. ^ Layer, Gunhild; Moser, Jürgen; Heinz, Dirk W.; Jahn, Dieter; Schubert, Wolf-Dieter (2003-12-01). "Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes". The EMBO Journal. 22 (23): 6214–6224. doi:10.1093/emboj/cdg598. ISSN 0261-4189. PMC 291839Freely accessible. PMID 14633981. 
  3. ^ Breckau, Daniela; Mahlitz, Esther; Sauerwald, Anselm; Layer, Gunhild; Jahn, Dieter (2003-11-21). "Oxygen-dependent coproporphyrinogen III oxidase (HemF) from Escherichia coli is stimulated by manganese". The Journal of Biological Chemistry. 278 (47): 46625–46631. doi:10.1074/jbc.M308553200. ISSN 0021-9258. PMID 12975365.