| IED ID | IndEnz0016000119 |
| Enzyme Type ID | tyrosinase000119 |
| Protein Name |
Polyphenol oxidase 4 PPO4 Phenolase 4 EC 1.14.18.1 Cresolase Tyrosinase 4 |
| Gene Name | PPO4 |
| Organism | Agaricus bisporus (White button mushroom) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Agaricomycetes Agaricomycetidae Agaricales Agaricaceae Agaricus Agaricus bisporus (White button mushroom) |
| Enzyme Sequence | MSLLATVGPTGGVKNRLDIVDFVRDEKFFTLYVRALQAIQDKDQADYSSFFQLSGIHGLPFTPWAKPKDTPTVPYESGYCTHSQVLFPTWHRVYVSIYEQVLQEAAKGIAKKFTVHKKEWVQAAEDLRQPYWDTGFALVPPDEIIKLEQVKITNYDGTKITVRNPILRYSFHPIDPSFSGYPNFDTWRTTVRNPDADKKENIPALIAKLDLEADSTREKTYNMLKFNANWEAFSNHGEFDDTHANSLEAVHDDIHGFVGRGAIRGHMTHALFAAFDPIFWLHHSNVDRHLSLWQALYPGVWVTQGPEREGSMGFAPGTELNKDSALEPFYETEDKPWTSVPLTDTALLNYSYPDFDKVKGGTPDLVRDYINDHIDRRYGIKKSEGGKNPALDLLSDFKGVTHDHNEDLKMFDWTIQASWKKFELDDSFAIIFYFAADGSTNVTKENYIGSINIFRGTTPTNCANCRTQDNLVQEGFVHLDRFIARDLDTFDPQAVHRYLKEKKLSYKVVADDHSVTLKSLRIRVQGRPLHLPPGVSFPRLDKNIPIVNFDDVLDLVTGVVNIGLTAVGATAGVAIGVVGATAGTAIGVAGAATDAVTNIAKGGLGALGRIF |
| Enzyme Length | 611 |
| Uniprot Accession Number | C7FF05 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 255; /note=Substrate; /evidence=ECO:0000250 |
| 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; 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; |
| DNA Binding | |
| EC Number | 1.14.18.1 |
| Enzyme Function | FUNCTION: Copper-containing oxidase that catalyzes both the o-hydroxylation of monophenols and the subsequent oxidation of the resulting o-diphenols into reactive o-quinones, which evolve spontaneously to produce intermediates, which associate in dark brown pigments. Involved in the initial step of melanin synthesis. Melanins constitute a mechanism of defense and resistance to stress such as UV radiations, free radicals, gamma rays, dehydratation and extreme temperatures, and contribute to the fungal cell-wall resistance against hydrolytic enzymes in avoiding cellular lysis. Fungal pigments are also involved in the formation and stability of spores (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (20); Binding site (1); Chain (1); Cross-link (1); Helix (18); Metal binding (6); Propeptide (1); Site (1); Turn (6) |
| Keywords | 3D-structure;Copper;Melanin biosynthesis;Metal-binding;Monooxygenase;Oxidoreductase;Thioether bond |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: The C-ter is probably cleaved after Gly-379 since the mature active protein is smaller than the protein encoded by the gene. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5M6B; |
| Mapped Pubmed ID | 28500345; |
| Motif | |
| Gene Encoded By | |
| Mass | 68,318 |
| Kinetics | |
| Metal Binding | METAL 57; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 82; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 91; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 251; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 255; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 283; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19 |
| Rhea ID | RHEA:34287; RHEA:18117 |
| Cross Reference Brenda | 1.14.18.1; |