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 |
|---|
| BRENDA | 1.14.15.20 |
| EC2PDB | 1.14.15.20 |
| ExplorEnz | 1.14.15.20 |
| PRIAM enzyme-specific profiles | 1.14.15.20 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.14.15.20 |
| IUBMB Enzyme Nomenclature | 1.14.15.20 |
| IntEnz | 1.14.15.20 |
| MEDLINE | Find literature relating to 1.14.15.20 |
| MetaCyc | 1.14.15.20 |
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.14.15.-
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