CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.520 | Peroxidase; domain 1 |
|
1.10.520.10 |
Domain Context
CATH Clusters
| Superfamily | 1.10.520.10 |
| Functional Family |
Enzyme Information
| 1.11.1.13 |
Manganese peroxidase.
based on mapping to UniProt Q02567
2 Mn(2+) + 2 H(+) + H(2)O(2) = 2 Mn(3+) + 2 H(2)O.
-!- The enzyme from white rot basidiomycetes is involved in the oxidative degradation of lignin. -!- The enzyme oxidizes a bound Mn(2+) ion to Mn(3+) in the presence of hydrogen peroxide. -!- The product, Mn(3+), is released from the active site in the presence of a chelator (mostly oxalate and malate) that stabilizes it against disproportionation to Mn(2+) and insoluble Mn(4+). -!- The complexed Mn(3+) ion can diffuse into the lignified cell wall, where it oxidizes phenolic components of lignin and other organic substrates. -!- It is inactive with veratryl alcohol or nonphenolic substrates.
|
UniProtKB Entries (1)
| Q02567 |
PEM1_PHACH
Phanerochaete chrysosporium
Manganese peroxidase 1
|
PDB Structure
| PDB | 3M5Q |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Ultrahigh (0.93A) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: implications for the catalytic mechanism.
J.Inorg.Biochem.
|
