Detail Information for IndEnz0016000115
IED ID IndEnz0016000115
Enzyme Type ID tyrosinase000115
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