| IED ID | IndEnz0018000081 |
| Enzyme Type ID | peroxidase000081 |
| Protein Name |
Aromatic peroxygenase Fragments |
| Gene Name | APO |
| Organism | Coprinellus radians (Coprophilous mushroom) (Coprinus radians) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetidae Agaricales Psathyrellaceae Coprinellus Coprinellus radians (Coprophilous mushroom) (Coprinus radians) |
| Enzyme Sequence | VPGGLXPPPEYVGPKLVNDADHPWEPLRPGDIRGPCPGLNTLASHGYLPRNGVATPAQIINAIVEGFNFNYEGAVFVTYFAHIVDGNLVTDLLSIGGKTNLTGEDTGAPAIIGGLNTHSVFEGDASMTRDDFHFGDNHSFNQTLFDQFVEYSNTYGGGFYNQEVAGHLRRRRIEQSIATNPEFDFTSPRFFTAFAESSFPYSFFVDGRITERPGGLSMENATLFFRDHKMPDDFWRNVNGEMTFTGTPDPNSAPSNLALGH |
| Enzyme Length | 261 |
| Uniprot Accession Number | B9W4V8 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Aromatic peroxidase that oxidizes aryl alcohols into the corresponding aldehydes and then into the corresponding benzoic acids. Catalyzes the regioselective peroxide-dependent hydroxylation of naphthalene to 1-naphthol and to a far lesser extent 2-naphthol via a naphthalene 1,2-oxide intermediate. Halogenates phenol to 2-bromophenol and 4-bromophenol. Oxidizes the sulfur-containing heterocycle dibenzothiophene to yield sulfoxidation products, and trace amounts of ring-hydroxylation products. {ECO:0000269|PubMed:17601809, ECO:0000269|PubMed:19039585}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0 with ABTS as substrate. Optimum pH is 6.0 with dimethoxyphenol as substrate. Optimum pH is 8.0 with benzyl alcohol as substrate, and there is another optimum at pH 4.5. Optimum pH is 6.0 with naphthalene as substrate. Optimum pH is 7.0 with pyridine as substrate. Optimum pH is 7.5 with veratryl alcohol as substrate, and there is another optimum at pH 4.5. {ECO:0000269|PubMed:17601809}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (4); Metal binding (1); Non-adjacent residues (2); Non-terminal residue (2); Region (1); Sequence conflict (1) |
| Keywords | Direct protein sequencing;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:17601809}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,641 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=49 uM for ABTS (at pH 4.5) {ECO:0000269|PubMed:17601809}; KM=635 uM for benzyl alcohol (at pH 7) {ECO:0000269|PubMed:17601809}; KM=342 uM for dimethoxyphenol (at pH 4.5) {ECO:0000269|PubMed:17601809}; KM=1201 uM for hydrogen peroxide (at pH 7) {ECO:0000269|PubMed:17601809}; KM=584 uM for naphthalene (at pH 7) {ECO:0000269|PubMed:17601809}; KM=88 uM for veratryl alcohol (at pH 7) {ECO:0000269|PubMed:17601809}; |
| Metal Binding | METAL 36; /note=Iron (heme axial ligand); /evidence=ECO:0000250|UniProtKB:P04963 |
| Rhea ID | |
| Cross Reference Brenda |