| IED ID | IndEnz0015000004 |
| Enzyme Type ID | laccase000004 |
| Protein Name |
Laccase-C2 EC 1.10.3.2 Benzenediol:oxygen oxidoreductase C2 Diphenol oxidase C2 Lac C2 Urishiol oxidase C2 Fragments |
| Gene Name | |
| Organism | Cerrena unicolor (Canker rot fungus) (Daedalea unicolor) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Polyporales Cerrenaceae Cerrena Cerrena unicolor (Canker rot fungus) (Daedalea unicolor) |
| Enzyme Sequence | AIGPVADLDIVNDQLTDASMIKWDCLPYDVRSPNPLGTTGFAGGNYRSVPADLHLTTLADPR |
| Enzyme Length | 62 |
| Uniprot Accession Number | P86327 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by sodium azide. {ECO:0000269|PubMed:20175123}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000269|PubMed:20175123}; |
| DNA Binding | |
| EC Number | 1.10.3.2 |
| Enzyme Function | FUNCTION: Lignin degradation and detoxification of lignin-derived products (Probable). Oxidation of a broad range of substrates including mono-, di- and polyphenols, aromatic amines and methoxy-substituted phenols accompanied by reduction of oxygen to water. {ECO:0000269|PubMed:20175123, ECO:0000305}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Half-life at 60 degrees Celsius is 20 minutes. Half-life at 70 degrees Celsius is 3 minutes. {ECO:0000269|PubMed:20175123}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.8 with 2,6-dimethoxyphenol as substrate, and less than 2.7 with ABTS as substrate. {ECO:0000269|PubMed:20175123}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (1); Non-adjacent residues (4); Non-terminal residue (1); Sequence uncertainty (9) |
| Keywords | Copper;Direct protein sequencing;Lignin degradation;Metal-binding;Oxidoreductase;Secreted |
| Interact With | |
| Induction | INDUCTION: By copper ions. {ECO:0000269|PubMed:20175123}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20175123}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated; contains 6% carbohydrates. {ECO:0000269|PubMed:20175123}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 6,626 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 uM for 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS) {ECO:0000269|PubMed:20175123}; KM=127 uM for 2-methoxyphenol {ECO:0000269|PubMed:20175123}; KM=518 uM for hydroquinone {ECO:0000269|PubMed:20175123}; KM=4.9 uM for 2,6-dimethoxyphenol {ECO:0000269|PubMed:20175123}; KM=140 uM for pyrogallol {ECO:0000269|PubMed:20175123}; Vmax=92.6 umol/min/mg enzyme toward 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS) {ECO:0000269|PubMed:20175123}; Vmax=2.4 umol/min/mg enzyme toward 2-methoxyphenol {ECO:0000269|PubMed:20175123}; Vmax=16.4 umol/min/mg enzyme toward hydroquinone {ECO:0000269|PubMed:20175123}; Vmax=0.1 umol/min/mg enzyme toward 2,6-dimethoxyphenol {ECO:0000269|PubMed:20175123}; Vmax=8.3 umol/min/mg enzyme toward pyrogallol {ECO:0000269|PubMed:20175123}; |
| Metal Binding | METAL 54; /note=Copper 1; type 2; /evidence=ECO:0000250|UniProtKB:D0VWU3 |
| Rhea ID | RHEA:11276 |
| Cross Reference Brenda |