ENZYME entry: EC 1.3.98.3
Accepted Name |
Coproporphyrinogen dehydrogenase.
|
Alternative Name(s) |
Coproporphyrinogen III oxidase. |
Oxygen-independent coproporphyrinogen-III oxidase. |
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.
- Formerly EC 1.3.99.22.
|
Cross-references |
BRENDA | 1.3.98.3 |
EC2PDB | 1.3.98.3 |
ExplorEnz | 1.3.98.3 |
PRIAM enzyme-specific profiles | 1.3.98.3 |
KEGG Ligand Database for Enzyme Nomenclature | 1.3.98.3 |
IUBMB Enzyme Nomenclature | 1.3.98.3 |
IntEnz | 1.3.98.3 |
MEDLINE | Find literature relating to 1.3.98.3 |
MetaCyc | 1.3.98.3 |
Rhea expert-curated reactions | 1.3.98.3 |
UniProtKB/Swiss-Prot |
P33770, HEMF_CERS4; | O67886, HEMN_AQUAE; | O31381, HEMN_BRADU; |
P51008, HEMN_CERS4; | P95651, HEMN_CERS5; | O34162, HEMN_CUPNH; |
P32131, HEMN_ECOLI; | Q9ZLH0, HEMN_HELPJ; | O25376, HEMN_HELPY; |
P95506, HEMN_MANHA; | Q51676, HEMN_PARDP; | P77915, HEMN_PSEAE; |
P0A1E2, HEMN_SALTI; | P0A1E1, HEMN_SALTY; | P74132, HEMN_SYNY3; |
O31067, HEMN_THEVL; |
|
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