| Official Name |
|---|
| Coproporphyrinogen dehydrogenase.
|
| Alternative Name(s) |
|---|
| Coproporphyrinogen III oxidase. |
| Oxygen-independent coproporphyrinogen-III oxidase. |
| Radical SAM enzyme. |
| Reaction catalysed |
|---|
| Coproporphyrinogen-III + 2 S-adenosyl-L-methionine <=> protoporphyrinogen-IX + 2 CO(2) + 2 L-methionine + 2 5'-deoxyadenosine |
| Cofactor(s) |
|---|
| Iron-sulfur.
|
| Comment(s) |
|---|
- Differs from EC 1.3.3.3 by using S-adenosyl-L-methionine (AdoMet)
instead of oxygen as oxidant.
- Occurs mainly in bacteria, whereas eukaryotes use the oxygen-
dependent oxidase.
- The reaction starts by using an electron from the reduced form of the
enzyme's [4Fe-4S] cluster to split AdoMet into methionine and the
radical 5'-deoxyadenosin-5'-yl; this radical initiates attack on the
2-carboxyethyl groups, leading to their conversion into vinyl groups.
- This conversion, -.CH-CH(2)-COO- -> -CH=CH(2) + CO(2) + e(-) replaces
the electron initially used.
|
| Cross-references |
|---|
| BRENDA | 1.3.99.22 |
| PUMA2 | 1.3.99.22 |
| PRIAM enzyme-specific profiles | 1.3.99.22 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.3.99.22 |
| IUBMB Enzyme Nomenclature | 1.3.99.22 |
| IntEnz | 1.3.99.22 |
| MEDLINE | Find literature relating to 1.3.99.22 |
| MetaCyc | 1.3.99.22 |
ExPASy Home page