Home  |  Contact

ENZYME entry: EC

Accepted Name
Anaerobilin synthase.
Reaction catalysed
2 S-adenosyl-L-methionine + protoheme + 2 reduced flavodoxin <=> S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + anaerobilin + Fe(2+) + 2 oxidized flavodoxin
  • 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.
PRIAM enzyme-specific profiles2.1.1.342
KEGG Ligand Database for Enzyme Nomenclature2.1.1.342
IUBMB Enzyme Nomenclature2.1.1.342
MEDLINEFind literature relating to
A0A384LP51, CHUW_ECO57

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-