Coproporphyrinogen dehydrogenase

In enzymology, a coproporphyrinogen dehydrogenase (EC 1.3.99.22) is an enzyme that catalyzes the chemical reaction

coproporphyrinogen III + 2 S-adenosyl-L-methionine ${\displaystyle \rightleftharpoons }$ protoporphyrinogen IX + 2 CO₂ + 2 L-methionine + 2 5'-deoxyadenosine

coproporphyrinogen dehydrogenase
Identifiers
EC no.	1.3.99.22
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

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]