| IED ID | IndEnz0002007690 |
| Enzyme Type ID | protease007690 |
| Protein Name |
Phenoloxidase 2 EC 1.14.18.- Prophenoloxidase-II |
| Gene Name | PPO2 proPO-II |
| Organism | Holotrichia diomphalia (Korean black chafer) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Coleoptera Polyphaga Scarabaeiformia Scarabaeoidea Scarabaeidae (scarab beetles) Melolonthinae (May beetles & June bugs) Holotrichia Holotrichia diomphalia (Korean black chafer) |
| Enzyme Sequence | MSNTAVLNDLVALYDRPTEPMFRVKAKKSFKVPKEYVTDRFKNVAVEISNRFGEDDSETVTIDSVPLPDLADILTLGREENFSLFIPKHRNLSAKLINIFLQAENPKHLLSIACYAHDRVNPYLFIYALSVALIHRKDTKSLKIPNQIQTFPDKYFDSQVFSQGKEEMTVVPQGLRRPIEIPRDYTASDLEEEHRVAYWREDLGINLHHWHWHLVYPTDGGEIVTKKDRRGELFYYSHQQIVARYNFERFCNALKRVERLTDWQGPIKEAYFPKLDSLVAKRAYPARVQDMTMQDLDIPGQNIKVDVDDMIRWRDRIYRAIADGFITATNGSKMNLDDVTGIDILGNIMESSELSPNRQLYGNLHGFGHLMLSYIHDPRSHHLEPFGVIGDFTTAMRDPIFYRWHAFVDDVFQQFNGSLPRYTAEQLDYAGVQITDVNIKTPNAPDNEFRTFWQQSDVDMSRGVDFQDPGSVFVRFTHLNHEPFSYNITVNNTGNGVQEGTCRIFLAPATDERGNPWLFNNQRVMFVEMDRFKVTLRQGQNTITRNSTQSSVTIPFERTFRDLDTNRPAEGSEELDIFNFCGCGWPHHLLVPKGTPDGFKAQLFVMISNYADDKVEQDLSGSCNDAESYCGVRGGKYPDKRPMGYPFNRVARQGADTLQRFLTGNMIVQNCRIVHSDRTVRPRS |
| Enzyme Length | 684 |
| Uniprot Accession Number | Q8I6K2 |
| Absorption | |
| Active Site | ACT_SITE 350; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q8MZM3 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 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 (By similarity). Catalyzes the oxidation of o-diphenols (N-acetyldopamine, 4-methylcatechol and dopamine) (PubMed:12185078, PubMed:9085271, PubMed:16362048). Cannot oxidize monophenols and p-phenols (L-tyrosine, tyramine, gentisic acid and hydroquinone) (PubMed:9085271). Binds to the surface of hemocytes and is involved in hemocyte melanization (By similarity). Activation of the enzyme in response to bacterial lipopolysaccharides (LPS) suggests it may play a role in innate immunity (PubMed:9839951). {ECO:0000250|UniProtKB:O44249, ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:16362048, ECO:0000269|PubMed:9085271, ECO:0000269|PubMed:9839951}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:9085271}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:9085271}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Glycosylation (7); Metal binding (6); Propeptide (1) |
| Keywords | Copper;Direct protein sequencing;Disulfide bond;Glycoprotein;Immunity;Innate immunity;Melanin biosynthesis;Metal-binding;Monooxygenase;Oxidoreductase;Secreted;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9085271}. Note=Secreted in the hemolymph. {ECO:0000269|PubMed:9085271}. |
| Modified Residue | |
| Post Translational Modification | PTM: Precursor cleaved by PPAF1. {ECO:0000269|PubMed:12185078, ECO:0000269|PubMed:9085271}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 78,820 |
| Kinetics | |
| Metal Binding | METAL 209; /note=Copper A; /evidence=ECO:0000250|UniProtKB:O44249; METAL 213; /note=Copper A; /evidence=ECO:0000250|UniProtKB:O44249; METAL 238; /note=Copper A; /evidence=ECO:0000250|UniProtKB:O44249; METAL 365; /note=Copper B; /evidence=ECO:0000250|UniProtKB:O44249; METAL 369; /note=Copper B; /evidence=ECO:0000250|UniProtKB:O44249; METAL 405; /note=Copper B; /evidence=ECO:0000250|UniProtKB:O44249 |
| Rhea ID | |
| Cross Reference Brenda |