CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 1 | Mainly Alpha | 
|   | 1.10 | Orthogonal Bundle | 
|   | 1.10.489 | Chloroperoxidase | 
|   | 1.10.489.10 | Chloroperoxidase-like | 
Domain Context
CATH Clusters
| Superfamily | Chloroperoxidase-like | 
| Functional Family | Aromatic peroxygenase | 
Enzyme Information
| 1.11.2.1 | Unspecific peroxygenase. based on mapping to UniProt B9W4V6 RH + H(2)O(2) = ROH + H(2)O. -!- Enzymes of this type include glycoproteins secreted by agaric basidiomycetes. -!- They catalyze the insertion of an oxygen atom from H(2)O(2) into a wide variety of substrates, including aromatic rings such as naphthalene, toluene, phenanthrene, pyrene and p-nitrophenol, recalcitrant heterocycles such as pyridine, dibenzofuran, various ethers (resulting in O-dealkylation) and alkanes such as propane, hexane and cyclohexane. -!- Reactions catalyzed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, O- and N-dealkylation, bromination and one-electron oxidations. -!- They have little or no activity toward chloride. -!- Mechanistically, the catalytic cycle of unspecific (mono)- peroxygenases combines elements of the 'shunt' pathway of cytochrome P450s (a side activity that utilizes a peroxide in place of dioxygen and NAD(P)H) and the classic heme peroxidase cycle. | 
UniProtKB Entries (1)
| B9W4V6 | APO1_AGRAE Agrocybe aegerita Aromatic peroxygenase | 
PDB Structure
| PDB | 6EL4 | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | Structural Insights into the Substrate Promiscuity of a Laboratory-Evolved Peroxygenase. Acs Chem.Biol. | 
