| IED ID | IndEnz0018000692 |
| Enzyme Type ID | peroxidase000692 |
| Protein Name |
Chorion peroxidase EC 1.11.1.7 |
| Gene Name | pxt AAEL004386 |
| Organism | Aedes aegypti (Yellowfever mosquito) (Culex aegypti) |
| 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) Culicinae Aedini Aedes Stegomyia Aedes aegypti (Yellowfever mosquito) (Culex aegypti) |
| Enzyme Sequence | MAKKVLLLSLYSAVLSTWFGFGYVQCKLPTSRSEIPNFDYTVAQQPDQSDACEQNEVCMVSVECILDAKKKAILKPCSTVPSVDGVCCPSSEYNGTSSRVQQNSEEHAADHLVLQAIHEGRREYDEKLRFEDEHRAVMTAKEKPEAMFHRMFLPGGLKTHGKEVVDAEEQANVYGHVFASRKYAELTNMTLKQRQGDRFARIPRAIRKRCLPPVPCNPHSRYRTIDGSCNNPLPDRTSWGMEGYPFDRVLEPAYEDGVWAPRIHSVTGNLLPSARVISVALFPDEYRPDPRLNILFMQMGQFISHDFTLSRGFTTKHGQAIECCTPNCTAPLFGPHRHFACFPIEVPPNDPFYSRFGVRCLNLVRIRLAQGPECQLGYAKQADLVTHFLDASTVYGSTNDVAAELRAFQQGRLKDSFPNGIELLPFARNRTACVPWARVCYEGGDIRTNQLLGLTMVHTLFMREHNRLAVGLSKINPHWDDERLYQEARRILIAEYQNVVYNEFLPILLGHERVQQLGLADPFDTYTNYYDPNLRPMTLAEVGAAAHRYGHSLVEGFFRFLTRESPPEDVFIKDIFNDPSKTLEPNSFDVMMFSFNQQPMEQMDRFLTYGLTRFLFKERKPFGSDLASLNIQRGRDFAVRPYNDYREWAGLGRITDFNQLGEVGALLAQVYESPDDVDLWPGGVLEPPAEGAVVGSTFVALLSAGYTRYKRADRYYFTNGPEVNPGAFTLQQLGEIRRTTLAGIICANADHKEDFYQAQEALRQSSADNVPVPCTRYDTVNLGLWREEGF |
| Enzyme Length | 790 |
| Uniprot Accession Number | P82600 |
| Absorption | |
| Active Site | ACT_SITE 305; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Activity Regulation | ACTIVITY REGULATION: Extremely resistant to denaturating agents, such as SDS and organic solvents. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7; |
| DNA Binding | |
| EC Number | 1.11.1.7 |
| Enzyme Function | FUNCTION: Involved in the formation of a rigid and insoluble egg chorion by catalyzing chorion protein cross-linking through dityrosine formation and phenol oxidase-catalyzed chorion melanization. {ECO:0000269|PubMed:10871050, ECO:0000269|PubMed:16150691, ECO:0000269|PubMed:8900599}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 with guaiacol as the reducing agent.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Erroneous initiation (1); Glycosylation (5); Metal binding (1); Modified residue (2); Propeptide (1); Sequence conflict (16); Signal peptide (1); Site (1) |
| Keywords | Acetylation;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Hydroxylation;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Expression levels increase 24 hours following blood feeding. Peak peroxidase activity is reached at 36-48 hours after a blood-meal. {ECO:0000269|PubMed:8900599}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. Note=In the chorion layer of the mature eggs. |
| Modified Residue | MOD_RES 210; /note="N-acetylcysteine; in Chorion peroxidase light chain"; /evidence="ECO:0000305|PubMed:16150691"; MOD_RES 353; /note="3',4'-dihydroxyphenylalanine"; /evidence="ECO:0000269|PubMed:16150691" |
| Post Translational Modification | PTM: N-glycosylated on Trp by mannose and on Asn by N-acetylglucosamine.; PTM: There is a hexose glycosylation of an unidentified residue between 654 and 708; Trp-680 is conserved in closely related species and is probably mannosylated. |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 89,605 |
| Kinetics | |
| Metal Binding | METAL 551; /note=Iron (heme b axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00298 |
| Rhea ID | RHEA:56136 |
| Cross Reference Brenda |