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 | Peroxidasin homolog |
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 | 5MFA |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structure of human promyeloperoxidase (proMPO) and the role of the propeptide in processing and maturation.
J. Biol. Chem.
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