ENZYME entry: EC 1.14.15.17
| Accepted Name |
|---|
| Pheophorbide a oxygenase.
|
| Alternative Name(s) |
|---|
| PaO. |
| PAO. |
| Pheide a monooxygenase. |
| Pheide a oxygenase. |
| Reaction catalysed |
|---|
| Pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) <=> red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster |
| Comment(s) |
|---|
- This enzyme catalyzes a key reaction in chlorophyll degradation,
which occurs during leaf senescence and fruit ripening in higher
plants.
- The enzyme from Arabidopsis contains a Rieske-type iron-sulfur
cluster and requires reduced ferredoxin, which is generated either by
NADPH through the pentose-phosphate pathway or by the action of
photosystem I.
- While still attached to this enzyme, the product is rapidly converted
into primary fluorescent chlorophyll catabolite by the action of
EC 1.3.7.12.
- Pheophorbide b acts as an inhibitor.
- In (18)O(2) labeling experiments, only the aldehyde oxygen is
labeled, suggesting that the other oxygen atom may originate from
H(2)O.
- Formerly EC 1.14.12.20.
|
| Cross-references |
|---|
| BRENDA | 1.14.15.17 |
| EC2PDB | 1.14.15.17 |
| ExplorEnz | 1.14.15.17 |
| PRIAM enzyme-specific profiles | 1.14.15.17 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.14.15.17 |
| IUBMB Enzyme Nomenclature | 1.14.15.17 |
| IntEnz | 1.14.15.17 |
| MEDLINE | Find literature relating to 1.14.15.17 |
| MetaCyc | 1.14.15.17 |
| Rhea expert-curated reactions | 1.14.15.17 |
| UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
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.-.-.-