| IED ID | IndEnz0019000006 |
| Enzyme Type ID | polyphenol oxidase000006 |
| Protein Name |
Polyphenol oxidase, chloroplastic PPO EC 1.10.3.1 Catechol oxidase |
| Gene Name | |
| Organism | Vitis vinifera (Grape) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids rosids incertae sedis Vitales Vitaceae Viteae Vitis Vitis vinifera (Grape) |
| Enzyme Sequence | MASLPWSLTTSTAIANTTNISAFPPSPLFQRASHVPVARNRSRRFAPSKVSCNSANGDPNSDSTSDVRETSSGKLDRRNVLLGIGGLYGAAGGLGATKPLAFGAPIQAPDISKCGTATVPDGVTPTNCCPPVTTKIIDFQLPSSGSPMRTRPAAHLVSKEYLAKYKKAIELQKALPDDDPRSFKQQANVHCTYCQGAYDQVGYTDLELQVHASWLFLPFHRYYLYFNERILAKLIDDPTFALPYWAWDNPDGMYMPTIYASSPSSLYDEKRNAKHLPPTVIDLDYDGTEPTIPDDELKTDNLAIMYKQIVSGATTPKLFLGYPYRAGDAIDPGAGTLEHAPHNIVHKWTGLADKPSEDMGNFYTAGRDPIFFGHHANVDRMWNIWKTIGGKNRKDFTDTDWLDATFVFYDENKQLVKVKVSDCVDTSKLRYQYQDIPIPWLPKNTKAKAKTTTKSSKSGVAKAAELPKTTISSIGDFPKALNSVIRVEVPRPKKSRSKKEKEDEEEVLLIKGIELDRENFVKFDVYINDEDYSVSRPKNSEFAGSFVNVPHKHMKEMKTKTNLRFAINELLEDLGAEDDESVIVTIVPRAGGDDVTIGGIEIEFVSD |
| Enzyme Length | 607 |
| Uniprot Accession Number | P43311 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O; Xref=Rhea:RHEA:21632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17253, ChEBI:CHEBI:18135; EC=1.10.3.1; Evidence={ECO:0000269|PubMed:20039636}; |
| DNA Binding | |
| EC Number | 1.10.3.1 |
| Enzyme Function | FUNCTION: Catalyzes the oxidation of mono- and o-diphenols to o-diquinones. {ECO:0000269|PubMed:20039636}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (9); Chain (1); Compositional bias (1); Cross-link (1); Disulfide bond (2); Helix (16); Metal binding (6); Region (1); Transit peptide (1); Turn (4) |
| Keywords | 3D-structure;Chloroplast;Copper;Disulfide bond;Metal-binding;Oxidoreductase;Plastid;Thioether bond;Thylakoid;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2P3X; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 67,347 |
| Kinetics | |
| Metal Binding | METAL 190; /note=Copper A; /evidence=ECO:0000269|PubMed:20039636; METAL 211; /note=Copper A; /evidence=ECO:0000269|PubMed:20039636; METAL 220; /note=Copper A; /evidence=ECO:0000269|PubMed:20039636; METAL 342; /note=Copper B; /evidence=ECO:0000269|PubMed:20039636; METAL 346; /note=Copper B; /evidence=ECO:0000269|PubMed:20039636; METAL 375; /note=Copper B; /evidence=ECO:0000269|PubMed:20039636 |
| Rhea ID | RHEA:21632 |
| Cross Reference Brenda | 1.10.3.1; |