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ENZYME

ENZYME entry: EC 1.14.15.20

PURL: https://purl.expasy.org/enzyme/EC/1.14.15.20
Accepted Name
heme oxygenase (biliverdin-producing, ferredoxin)
Reaction catalysed
heme b + 6 reduced [2Fe-2S]-[ferredoxin] + 3 O2 + 8 H(+) = biliverdin IXalpha + CO + Fe(2+) + 6 oxidized [2Fe-2S]-[ferredoxin] + 3 H2O
Comment(s)
  • The enzyme, found in plants, algae, and cyanobacteria, participates in the biosynthesis of phytochromobilin and phytobilins.
  • The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules.
  • The third oxygen molecule provides the oxygen atom that converts the alpha-carbon to CO.
  • Unlike this enzyme, which uses ferredoxin as its electron donor, the electron source for the related mammalian enzyme (EC 1.14.14.18) is EC 1.6.2.4.
Cross-references
BRENDA1.14.15.20
EC2PDB1.14.15.20
ExplorEnz1.14.15.20
KEGG Ligand Database for Enzyme Nomenclature1.14.15.20
IUBMB Enzyme Nomenclature1.14.15.20
MEDLINEFind literature relating to 1.14.15.20
MetaCyc1.14.15.20
Rhea expert-curated reactions1.14.15.20

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.15.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-