Coproporphyrinogen dehydrogenase explained
coproporphyrinogen dehydrogenase |
Ec Number: | 1.3.99.22 |
Go Code: | 0051989 |
In enzymology, a coproporphyrinogen dehydrogenase is an enzyme that catalyzes the chemical reaction
coproporphyrinogen III + 2 S-adenosyl-L-methionine
protoporphyrinogen IX + 2 CO
2 + 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
- Layer G, Verfurth K, Mahlitz E, Jahn D . 2002 . Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli . J. Biol. Chem. . 277 . 34136 - 42 . 12114526 . 10.1074/jbc.M205247200 . 37 . free .
- 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 . 6214 - 24 . 14633981 . 10.1093/emboj/cdg598 . 23 . 291839 .
Notes and References
- Fetzner. Susanne. Steiner. Roberto A.. 2010-02-16. Cofactor-independent oxidases and oxygenases. Applied Microbiology and Biotechnology. en. 86. 3. 791–804. 10.1007/s00253-010-2455-0. 20157809. 0175-7598. 11577/3402980. free.
- 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. 10.1093/emboj/cdg598. 0261-4189. 291839. 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. 10.1074/jbc.M308553200. 0021-9258. 12975365. free.