ENZYME entry: EC 2.1.1.342
| Accepted Name |
|---|
| anaerobilin synthase.
|
| Reaction catalysed |
|---|
| heme b + 2 reduced [flavodoxin] + 2 S-adenosyl-L-methionine <=> 5'-deoxyadenosine + anaerobilin + Fe(2+) + L-methionine + 2 oxidized [flavodoxin] + S-adenosyl-L-homocysteine |
| Comment(s) |
|---|
- The enzyme, studied from the bacterium Escherichia coli O157:H7, is a
radical SAM (AdoMet) enzyme that is involved in heme degradation and
iron utilization under anaerobic conditions.
- The enzyme uses two SAM molecules for the reaction.
- The first molecule is used to generate a 5'-deoxyadenosyl radical,
which abstracts a hydrogen atom from the methyl group of the second
SAM molecule.
- The newly formed methylene radical attacks the substrate, causing a
rearrangement of the porphyrin ring that results in the liberation of
iron.
|
| Cross-references |
|---|
| BRENDA | 2.1.1.342 |
| EC2PDB | 2.1.1.342 |
| ExplorEnz | 2.1.1.342 |
| PRIAM enzyme-specific profiles | 2.1.1.342 |
| KEGG Ligand Database for Enzyme Nomenclature | 2.1.1.342 |
| IUBMB Enzyme Nomenclature | 2.1.1.342 |
| IntEnz | 2.1.1.342 |
| MEDLINE | Find literature relating to 2.1.1.342 |
| MetaCyc | 2.1.1.342 |
| Rhea expert-curated reactions | 2.1.1.342 |
| UniProtKB/Swiss-Prot |
|
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