IED ID | IndEnz0002007691 |
Enzyme Type ID | protease007691 |
Protein Name |
Phenoloxidase 8 EC 1.10.3.- EC 1.14.18.- Prophenoloxidase 8 |
Gene Name | PPO8 1275798 AgaP_AGAP004976 |
Organism | Anopheles gambiae (African malaria mosquito) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Nematocera Culicomorpha Culicoidea Culicidae (mosquitos) Anophelinae Anopheles Cellia Pyretophorus gambiae species complex Anopheles gambiae (African malaria mosquito) |
Enzyme Sequence | MATLTQKFHGLLQHPLEPLFLPKNDGTLFYDLPERFLTSRYSPIGQNLANRFGPNSPASSQVSNDTGVPPTVVTIKDLDELPDLTFATWIKRRDSFSLFNPEHRKAAGKLTKLFLDQPNADRLVDVAAYARDRLNAPLFQYALSVALLHRPDTKSVSVPSLLHLFPDQFIDPAAQVRMMEEGSIVLDENRMPIPIPMNYTATDAEPEQRMAFFREDIGVNLHHWHWHLVYPASGPPDVVRKDRRGELFYYMHQQLLARYQIDRYAQGLGRIEPLANLREPVREAYYPKLLRTSNNRTFCPRYPGMTISDVARSADRLEVRIADIESWLPRVLEAIDAGFAVSDDGVRVPLDETRGIDVLGNILERSAISINRNLYGDVHNMGHVLLAFIHDPRGTYLESSGVMGGVATAMRDPIFYRWHKFIDNIFLRNKARLAPYTMAELSNSNVTLEALETQLDRAGGAVNSFVTFWQRSQVDLRAGIDFSAAGSAFVSFTHLQCAPFVYRLRINSTARSNRQDTVRIFLLPRQNEQGRPLSFEDRRLLAIELDSFRVNLRPGMNNIVRQSSNSSVTIPFERTFGNVEQANAGNAQSRFCGCGWPAHMLLPKGNANGVEFDLFAMVSRFEDDNANVNYDENAGCDDSYAFCGLRDRVYPSRRAMGFPFDRRASNGVRSVADFVAPYKNMRLATVTLRFMNTIIDRPTN |
Enzyme Length | 700 |
Uniprot Accession Number | Q8MZM3 |
Absorption | |
Active Site | ACT_SITE 364; /note=Proton acceptor; /evidence=ECO:0000305|PubMed:26732497 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=O2 + 2 tyramine = 2 dopamine; Xref=Rhea:RHEA:66596, ChEBI:CHEBI:15379, ChEBI:CHEBI:59905, ChEBI:CHEBI:327995; Evidence={ECO:0000269|PubMed:26732497}; CATALYTIC ACTIVITY: Reaction=2 dopamine + O2 = 2 dopamine quinone + 2 H2O; Xref=Rhea:RHEA:66600, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:59905, ChEBI:CHEBI:167191; Evidence={ECO:0000269|PubMed:26732497}; |
DNA Binding | |
EC Number | 1.10.3.-; 1.14.18.- |
Enzyme Function | FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds (Probable). Catalyzes the oxidation of o-diphenols such as dopamine (PubMed:26732497). Also oxidizes monophenols such as tyramine (PubMed:26732497). {ECO:0000269|PubMed:26732497, ECO:0000305|PubMed:26732497}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Beta strand (21); Chain (1); Disulfide bond (2); Glycosylation (6); Helix (34); Metal binding (6); Mutagenesis (1); Propeptide (1); Turn (9) |
Keywords | 3D-structure;Copper;Disulfide bond;Glycoprotein;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Secreted;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8I6K1}. |
Modified Residue | |
Post Translational Modification | PTM: Upon activation, a trypsin type protease cleaves prophenol oxidase to yield the active enzyme. {ECO:0000250|UniProtKB:Q9V521}. |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 4YZW; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 79,293 |
Kinetics | |
Metal Binding | METAL 223; /note="Copper 1; via tele nitrogen"; /evidence="ECO:0000269|PubMed:26732497, ECO:0007744|PDB:4YZW"; METAL 227; /note="Copper 1; via tele nitrogen"; /evidence="ECO:0000269|PubMed:26732497, ECO:0007744|PDB:4YZW"; METAL 252; /note="Copper 1; via tele nitrogen"; /evidence="ECO:0000269|PubMed:26732497, ECO:0007744|PDB:4YZW"; METAL 379; /note="Copper 2; via tele nitrogen"; /evidence="ECO:0000269|PubMed:26732497, ECO:0007744|PDB:4YZW"; METAL 383; /note="Copper 2; via tele nitrogen"; /evidence="ECO:0000269|PubMed:26732497, ECO:0007744|PDB:4YZW"; METAL 419; /note="Copper 2; via tele nitrogen"; /evidence="ECO:0000269|PubMed:26732497, ECO:0007744|PDB:4YZW" |
Rhea ID | RHEA:66596; RHEA:66600 |
Cross Reference Brenda |