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ENZYME entry: EC 1.14.15.20

Accepted Name
Heme oxygenase (biliverdin-producing, ferredoxin).
Reaction catalysed
Protoheme + 6 reduced ferredoxin [iron-sulfur] cluster + 3 O(2) + 6 H(+) <=> biliverdin + Fe(2+) + CO + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H(2)O
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
PRIAM enzyme-specific profiles1.14.15.20
KEGG Ligand Database for Enzyme Nomenclature1.14.15.20
IUBMB Enzyme Nomenclature1.14.15.20
IntEnz1.14.15.20
MEDLINEFind literature relating to 1.14.15.20
MetaCyc1.14.15.20

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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.-.-.-