CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.640 | Myeloperoxidase, subunit C |
|
1.10.640.10 | Haem peroxidase domain superfamily, animal type |
Domain Context
CATH Clusters
| Superfamily | Haem peroxidase domain superfamily, animal type |
| Functional Family | Myeloperoxidase |
Enzyme Information
| 1.11.2.2 |
Myeloperoxidase.
based on mapping to UniProt P05164
Cl(-) + H(2)O(2) + H(+) = HClO + H(2)O.
-!- Is present in phagosomes of neutrophils and monocytes, where the hypochlorite produced is strongly bactericidal. -!- It differs from EC 1.11.1.10 in its preference for formation of hypochlorite over the chlorination of organic substrates under physiological conditions (pH 5-8). -!- Hypochlorite in turn forms a number of antimicrobial products (Cl(2), chloramines, hydroxyl radical, singlet oxygen). -!- MPO also oxidizes bromide, iodide and thiocyanate. -!- In the absence of halides, it oxidizes phenols and has a moderate peroxygenase activity toward styrene.
|
UniProtKB Entries (1)
| P05164 |
PERM_HUMAN
Homo sapiens
Myeloperoxidase
|
PDB Structure
| PDB | 1DNU |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution.
Biochemistry
|
