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
| 1.11.1.16 |
Versatile peroxidase.
based on mapping to UniProt O94753
(1) 1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H(2)O(2) = 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H(2)O. (2) 2 manganese(II) + 2 H(+) + H(2)O(2) = 2 manganese(III) + 2 H(2)O.
-!- This ligninolytic peroxidase combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, EC 1.11.1.13 and EC 1.11.1.14. -!- Unlike these two enzymes, it is also able to oxidize phenols, hydroquinones and both low- and high-redox-potential dyes, due to a hybrid molecular architecture that involves multiple binding sites for substrates.
|
UniProtKB Entries (1)
| O94753 |
VPL2_PLEER
Pleurotus eryngii
Versatile peroxidase VPL2
|
PDB Structure
| PDB | 4FCS |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Two Oxidation Sites for Low Redox Potential Substrates: A DIRECTED MUTAGENESIS, KINETIC, AND CRYSTALLOGRAPHIC STUDY ON PLEUROTUS ERYNGII VERSATILE PEROXIDASE.
J.Biol.Chem.
|
