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ENZYME entry: EC 1.7.2.9
| Accepted Name |
|---|
| hydroxylamine oxidase.
|
| Alternative Name(s) |
|---|
| HOX. |
| HOX2. |
| Reaction catalysed |
|---|
| 3 Fe(III)-[cytochrome c] + hydroxylamine <=> 3 Fe(II)-[cytochrome c] + 3 H(+) + nitric oxide |
| Comment(s) |
|---|
- The enzyme, characterized from the anaerobic ammonium-oxidizing
(anammox) bacterium Kuenenia stuttgartiensis, is very similar to
EC 1.7.2.6.
- Both enzymes are homotrimeric enzymes in which each subunit contains
seven c-type hemes and one specialized P460-type heme that is bound
to a tyrosine residue in an adjacent subunit.
- However, this enzyme catalyzes only the 3 electron oxidation of
hydroxylamine, forming nitric oxide, and is not capable of performing
further oxidation to form nitrite.
|
| Cross-references |
|---|
| BRENDA | 1.7.2.9 |
| EC2PDB | 1.7.2.9 |
| ExplorEnz | 1.7.2.9 |
| PRIAM enzyme-specific profiles | 1.7.2.9 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.7.2.9 |
| IUBMB Enzyme Nomenclature | 1.7.2.9 |
| IntEnz | 1.7.2.9 |
| MEDLINE | Find literature relating to 1.7.2.9 |
| MetaCyc | 1.7.2.9 |
| Rhea expert-curated reactions | 1.7.2.9 |
| UniProtKB/Swiss-Prot |
|
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ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.7.2.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.7.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-