| IED ID | IndEnz0019000007 |
| Enzyme Type ID | polyphenol oxidase000007 |
| Protein Name |
+ -larreatricin hydroxylase, chloroplastic EC 1.14.99.47 Polyphenol oxidase |
| Gene Name | |
| Organism | Larrea tridentata (Creosote bush) (Zygophyllum tridentatum) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Zygophyllales Zygophyllaceae Larreoideae Larrea Larrea tridentata (Creosote bush) (Zygophyllum tridentatum) |
| Enzyme Sequence | MASLSSQSKLLATPYSFPYHTKPSRVSLRRVSCKASNDNKDKPNDQEKTFSIDRRNMLIGLGGLYGASNVFPSNQSTLAAPIQPPVLPDSCHPPEDLAEGVNVLCCPPDVKDPIDFQMPSNPSRLRIRPAAHLADPTYIEKYKKALAAMKALPQNDPRSFYQQANIHCAYCNGAYDQVGFPDVNIQVHHSWLFLPFHRWYLYFYERILGSLIDDPTFAIPFWNWDAPKGMHMPHMFIDPNSPLYDAKRNPAHFPDTIVDLDFSSGEAPSHNPRQIGNNLSIMYKQVVRAKKARLFHGRPLQAGSFPDESGDGSLEGTPHGNIHLWSGDPRQSNFENMGNFYSAGRDPLFYAHHANVDRMWYIWKNSLGRKDYKKKDWLNAGFLLFDENAQPVRVYVRDALDERKLGYAYQEVDIPWINSKPKPRKANPWPNRLRSKATTTTKLINKFPLTLDSTVSFEVKRPKKSRSKSEKEDEEEVLVIEKIKHEPQFPLKFDVYINDEDEDPSAADQTEFAGSFVNVPHFHRHGDKKDKRQTTNLSIGISEVLDELDVDGDDSIVVTLVPRVGSGQITIGGAKIEFVRDEED |
| Enzyme Length | 584 |
| Uniprot Accession Number | Q6UIL3 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(+)-larreatricin + AH2 + O2 = (+)-3'-hydroxylarreatricin + A + H2O; Xref=Rhea:RHEA:34259, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:67153, ChEBI:CHEBI:67154; EC=1.14.99.47; Evidence={ECO:0000269|PubMed:12960376}; |
| DNA Binding | |
| EC Number | 1.14.99.47 |
| Enzyme Function | FUNCTION: Enantio-specific polyphenol oxidase involved in aromatic ring hydroxylation. Involved in the biosynthesis of the creosote bush 8-8' linked lignans. Has a strong preference for the 3' position of (+)-larreatricin. {ECO:0000269|PubMed:12960376}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Cross-link (1); Disulfide bond (2); Metal binding (6); Propeptide (1); Transit peptide (2) |
| Keywords | Chloroplast;Copper;Disulfide bond;Metal-binding;Oxidoreductase;Plastid;Thioether bond;Thylakoid;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen {ECO:0000305|PubMed:12960376}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 66,352 |
| Kinetics | |
| Metal Binding | METAL 167; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 188; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 197; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 319; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 323; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 353; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19 |
| Rhea ID | RHEA:34259 |
| Cross Reference Brenda | 1.14.18.1;1.14.99.47; |