Coproporphyrinogen dehydrogenase
| 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 | ||||||||
| |||||||||
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 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]
References
[edit]- ^ 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. hdl:11577/3402980. ISSN 0175-7598. PMID 20157809.
- ^ 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 291839. PMID 14633981.
- ^ 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.
- Layer G, Verfurth K, Mahlitz E, Jahn D (2002). "Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli". J. Biol. Chem. 277 (37): 34136–42. doi:10.1074/jbc.M205247200. PMID 12114526.
- Layer G, Moser J, Heinz DW, Jahn D, Schubert WD (2003). "Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes". EMBO J. 22 (23): 6214–24. doi:10.1093/emboj/cdg598. PMC 291839. PMID 14633981.
