| IED ID | IndEnz0016000178 |
| Enzyme Type ID | tyrosinase000178 |
| Protein Name |
Phenoloxidase 1 EC 1.14.18.1 Prophenoloxidase 1 Slppo1 |
| Gene Name | PPO1 |
| Organism | Spodoptera litura (Asian cotton leafworm) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Amphiesmenoptera Lepidoptera (butterflies and moths) Glossata Neolepidoptera Heteroneura Ditrysia Obtectomera Noctuoidea Noctuidae (owlet moths) Amphipyrinae Spodoptera Spodoptera litura (Asian cotton leafworm) |
| Enzyme Sequence | MSDMSGDVVEHPKLLFDRPNEPLITPKGDNKAVFQLSEKLVPPEYANNGVELNDRFGDDATEKIPLKTLDSYPAFTKASQLPSDADFSLLLPKHQEMATEVIDAFMNVPLNQLQDFLSTCVYARANLNPQLFNYCYSVALMHRDDTKNVPIQNFAETFPSKFMDSQVFQRAREVTAVLPQNVPRIPIIIPRDYTATDLEEEHRLAYWREDIGVNLHHWHWHLVYPFTASQRSIVAKDRRGELFFHMHQQLIARYNCERLNHSLKRVKKFSNWREPIPEAYFPKLDSLTSARGWPPRQANMYWQDLNRPVDGLNITINDMERWRRNVEEAISTGRVTKADGSSAELDIDTLGNMLEASILSPNRELYGSIHNNGHSFAAYMHDPTHRYLESFGVIADEATTMRDPFFYRWHAWIDDTCQRHKESAYVRPYTRSELENPGVQVTSVSVETAGGQPNTLNTFWMSSDVDLSKGLDFSDRGAVYARFTYLNNRPFRYVININNTGSARRTTVRIFMAPKFDERNLVWSLADQRKMFIEMDRFVQPLNAGQNTITRNSTDSSVTIPFEQTFRDLSPQGSDPRRTSLAEFNFCGCGWPQHMLVPKGTEAGAAYQLFVMLSNYDLDSVDQPGGNQLSCVEASSFCGLKDKKYPDRRSMGFPFDRPSSIATNIEDFILPNMALQDITIRLSNVVEQNPRNPPSAV |
| Enzyme Length | 697 |
| Uniprot Accession Number | Q3ZPT5 |
| Absorption | |
| Active Site | ACT_SITE 355; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q8MZM3 |
| Activity Regulation | ACTIVITY REGULATION: Activated by a cationic detergent cetyl pyridinium chloride (CPC) (PubMed:16185666, PubMed:19557749). Inhibited by phenyl thio-urea (PTU) (PubMed:16185666). {ECO:0000269|PubMed:16185666, ECO:0000269|PubMed:19557749}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | 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:0000250|UniProtKB:C0HJM0}; 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:0000250|UniProtKB:C0HJM0}; |
| 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). Catalyzes the oxidation of 4-methylcatechol (PubMed:16185666, PubMed:19557749). Binds to the surface of hemocytes and is involved in hemocyte melanization (By similarity). {ECO:0000250|UniProtKB:Q25519, ECO:0000269|PubMed:16185666, ECO:0000269|PubMed:19557749}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Glycosylation (4); Metal binding (6); Propeptide (1) |
| Keywords | Copper;Disulfide bond;Glycoprotein;Melanin biosynthesis;Metal-binding;Monooxygenase;Oxidoreductase;Secreted;Zymogen |
| Interact With | |
| Induction | INDUCTION: Immediately upon microbial challenge with E.coli K-12. Expression increases 2.6-fold 6 hours after the challenge and 10.19-fold after 18 hours. No significant up-regulation in response to injury. {ECO:0000269|PubMed:16185666}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16185666}. Note=Secreted in the hemolymph. {ECO:0000269|PubMed:16185666}. |
| Modified Residue | |
| Post Translational Modification | PTM: Activated by the cleavage of the N-terminal propeptide by PPAE1. {ECO:0000269|PubMed:19557749}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 79,822 |
| Kinetics | |
| Metal Binding | METAL 217; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q25519; METAL 221; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q25519; METAL 247; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q25519; METAL 370; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q25519; METAL 374; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q25519; METAL 410; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q25519 |
| Rhea ID | RHEA:18117; RHEA:34287 |
| Cross Reference Brenda |