| IED ID | IndEnz0016000189 |
| Enzyme Type ID | tyrosinase000189 |
| Protein Name |
Tyrosinase EC 1.14.18.1 Monophenol monooxygenase |
| Gene Name | TYR TYRS |
| Organism | Pelophylax nigromaculatus (Black-spotted frog) (Rana nigromaculata) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Neobatrachia Ranoidea Ranidae (riparian frogs) Pelophylax Pelophylax nigromaculatus (Black-spotted frog) (Rana nigromaculata) |
| Enzyme Sequence | MESTTVLLATSTLLLVLHASYGQFPRACSTAQVLLSKECCPVWPGDNSSCGEVSGRGVCQDVVPSNSPVGAQFPFSGIDDRENWPIVFYNRTCQCQGNFMGYNCGECRFGYTGPNCTVRRNMIRKDIFRMTTAEKDKLIAYLNLAKHTISPDYVIATGTYEQMNNGSNPMFADISAYDLFVWIHYYASRDAFLEDGSVWADIDFAHEAPGFLPWHRFYLLLWEREIQKVTGDDNFTIPFWDWRDAQQCELCTDEFFGGTHPTSNNLLSPASFFSSWQIICSRPEEYNSLRIICNGTNEGPLLRSPGRHDRNRTPRLPTSADVEACLSLTDYETGAMDRSANFSFRNTLEGFAVPTSGIANRSQSSMHNSLHVFLNGSMSSVQGSANDPIFVLHHAFVDSLFEQWLRRHQPSLDVYPEANAPVGHNREYNMVPFIPLFTNGEFFVQSRDLGYDYDYLAESGSIEDFLLPYLEQARQIWQWLLGAAVLGGLITAVIATIISLTCRRKRKTKISEETRPLLMEAEDYQATYQSNL |
| Enzyme Length | 532 |
| Uniprot Accession Number | Q04604 |
| 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:0000250|UniProtKB:Q0MVP0}; 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:0000250|UniProtKB:Q0MVP0}; |
| 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 (By similarity). Catalyzes the initial and rate limiting step in the cascade of reactions leading to melanin production from tyrosine. In addition to hydroxylating tyrosine to DOPA (3,4-dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA-quinone (By similarity). {ECO:0000250|UniProtKB:P11344, ECO:0000250|UniProtKB:Q0MVP0}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (6); Metal binding (6); Natural variant (1); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Copper;Glycoprotein;Melanin biosynthesis;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Signal;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000250|UniProtKB:Q0MVP0, ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 60,116 |
| Kinetics | |
| Metal Binding | METAL 184; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 206; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 215; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 367; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 371; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 394; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19 |
| Rhea ID | RHEA:34287; RHEA:18117 |
| Cross Reference Brenda |