IED ID | IndEnz0015000138 |
Enzyme Type ID | laccase000138 |
Protein Name |
Laccase EC 1.10.3.2 Benzenediol:oxygen oxidoreductase Diphenol oxidase Urishiol oxidase Fragment |
Gene Name | |
Organism | Hericium coralloides (Coral tooth fungus) (Hericium ramosum) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetes incertae sedis Russulales Hericiaceae Hericium Hericium coralloides (Coral tooth fungus) (Hericium ramosum) |
Enzyme Sequence | AVGDDTPQLY |
Enzyme Length | 10 |
Uniprot Accession Number | B3A0L4 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Strongly activated by Mg(2+) and Al(3+). At concentrations <50 mM, activated by Ca(2+), Mn(2+), Co(2+) and K(+). Strongly inhibited by Hg(2+) and, in a concentration-dependent manner, by Fe(2+). {ECO:0000269|PubMed:22367940}. |
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:22367940}; |
DNA Binding | |
EC Number | 1.10.3.2 |
Enzyme Function | FUNCTION: Lignin degradation and detoxification of lignin-derived products. Has activity towards ABTS and, to a much lesser extent, towards N,N-dimethyl-1,4-phenylenediamine, catechol and 2-methylcatechol. {ECO:0000269|PubMed:22367940}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. Retains 65% activity at 20 degrees Celsius and 24% activity at 100 degrees Celsius. {ECO:0000269|PubMed:22367940}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 2.2. Activity declines sharply with decreases or increases in pH and is absent above pH 6.6. {ECO:0000269|PubMed:22367940}; |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Non-terminal residue (1) |
Keywords | Copper;Direct protein sequencing;Lignin degradation;Metal-binding;Oxidoreductase;Secreted |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:D0VWU3}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 1,078 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:11276 |
Cross Reference Brenda |