| IED ID | IndEnz0016000013 |
| Enzyme Type ID | tyrosinase000013 |
| Protein Name |
Tyrosinase EC 1.14.18.1 |
| Gene Name | tyr1 |
| Organism | Pholiota nameko |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetidae Agaricales Strophariaceae Pholiota Pholiota nameko |
| Enzyme Sequence | MSRVVITGVSGTIANRLEINDFVKNDKFFSLYIQALQVMSSVPPQENVRSFFQIGGIHGLPYTPWDGITGDQPFDPNTQWGGYCTHGSVLFPTWHRPYVLLYEQILHKHVQDIAATYTTSDKAAWVQAAANLRQPYWDWAANAVPPDQVIVSKKVTITGSNGHKVEVDNPLYHYKFHPIDSSFPRPYSEWPTTLRQPNSSRPNATDNVAKLRNVLRASQENITSNTYSMLTRVHTWKAFSNHTVGDGGSTSNSLEAIHDGIHVDVGGGGHMGDPAVAAFDPIFFLHHCNVDRLLSLWAAINPGVWVSPGDSEDGTFILPPEAPVDVSTPLTPFSNTETTFWASGGITDTTKLGYTYPEFNGLDLGNAQAVKAAIGNIVNRLYGASVFSGFAAATSAIGAGSVASLAADVPLEKAPAPAPEAAAQPPVPAPAHVEPAVRAVSVHAAAAQPHAEPPVHVSAGGHPSPHGFYDWTARIEFKKYEFGSSFSVLLFLGPVPEDPEQWLVSPNFVGAHHAFVNSAAGHCANCRSQGNVVVEGFVHLTKYISEHAGLRSLNPEVVEPYLTNELHWRVLKADGSVGQLESLEVSVYGTPMNLPVGAMFPVPGNRRHFHGITHGRVGGSRHAIV |
| Enzyme Length | 625 |
| Uniprot Accession Number | A7BHQ9 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, ChEBI:CHEBI:57924; EC=1.14.18.1; Evidence={ECO:0000269|PubMed:17617709}; CATALYTIC ACTIVITY: Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924, ChEBI:CHEBI:58315; EC=1.14.18.1; Evidence={ECO:0000269|PubMed:17617709}; |
| DNA Binding | |
| EC Number | 1.14.18.1 |
| Enzyme Function | FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. {ECO:0000250|UniProtKB:Q92396}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (6); Propeptide (1); Sequence conflict (5) |
| Keywords | Copper;Direct protein sequencing;Melanin biosynthesis;Metal-binding;Monooxygenase;Oxidoreductase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:17617709}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 67,499 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1930 uM for L-dopa {ECO:0000269|PubMed:17617709}; KM=119 uM for t-butylphenol {ECO:0000269|PubMed:17617709}; KM=30.6 uM for p-cresol {ECO:0000269|PubMed:17617709}; KM=163 uM for t-butylcatechol {ECO:0000269|PubMed:17617709}; KM=1240 uM for 3-(3,4-dihydroxyphenyl) propionic acid {ECO:0000269|PubMed:17617709}; KM=122 uM for dopamine {ECO:0000269|PubMed:17617709}; |
| Metal Binding | METAL 58; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 86; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 95; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 258; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 262; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 287; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19 |
| Rhea ID | RHEA:34287; RHEA:18117 |
| Cross Reference Brenda | 1.14.18.1; |