IED ID | IndEnz0016000092 |
Enzyme Type ID | tyrosinase000092 |
Protein Name |
Phenoloxidase 3 EC 1.14.18.1 Tyrosinase 3 Fragment |
Gene Name | PPO3 |
Organism | Sarcophaga argyrostoma (Flesh fly) (Liopygia argyrostoma) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Calyptratae Oestroidea Sarcophagidae (flesh flies) Sarcophaginae Sarcophaga Liopygia Sarcophaga argyrostoma (Flesh fly) (Liopygia argyrostoma) |
Enzyme Sequence | HWHLVYPIEAPDRSIVDKDRRGELFYYMHQQIIARYNAERYNAERLSNHMARVQPFNNLDEPIAEGYFPKM |
Enzyme Length | 71 |
Uniprot Accession Number | C0HJM0 |
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|Ref.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; Evidence={ECO:0000269|Ref.1}; |
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. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone (By similarity). {ECO:0000250|UniProtKB:O44249}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Metal binding (2); Non-terminal residue (2) |
Keywords | Copper;Direct protein sequencing;Melanin biosynthesis;Metal-binding;Monooxygenase;Oxidoreductase;Secreted;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O44249}. |
Modified Residue | |
Post Translational Modification | PTM: Upon activation, a trypsin type protease cleaves prophenol oxidase to yield the active enzyme. {ECO:0000250|UniProtKB:Q9W1V6}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 8,623 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.159 mM for L-dopa {ECO:0000269|Ref.1}; Vmax=151.3 umol/min/ug enzyme with L-dopa as substrate {ECO:0000269|Ref.1}; Note=Enzymes were activated using methanol. {ECO:0000269|Ref.1}; |
Metal Binding | METAL 3; /note=Copper A; /evidence=ECO:0000250|UniProtKB:O44249; METAL 29; /note=Copper A; /evidence=ECO:0000250|UniProtKB:O44249 |
Rhea ID | RHEA:34287; RHEA:18117 |
Cross Reference Brenda |