IED ID | IndEnz0016000090 |
Enzyme Type ID | tyrosinase000090 |
Protein Name |
Polyphenol oxidase latent form, chloroplastic L-PaPPO PA-PPO Cleaved into: Polyphenol oxidase active form, chloroplastic A-PaPPO EC 1.10.3.1 |
Gene Name | PPO |
Organism | Prunus armeniaca (Apricot) (Armeniaca vulgaris) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids fabids Rosales Rosaceae Amygdaloideae Amygdaleae Prunus Prunus armeniaca (Apricot) (Armeniaca vulgaris) |
Enzyme Sequence | MATAPSPTTMGTYSSLISTNSFSTFLPNKSQLSLSGKSKHYVARRSSISCKATNNNNSNNQNEQQEESSRLLGKLDRRNILIGLGGLYGATTLDRKPFAFADPIAPPDLTTCKPAEITPGGSETVPCCPPVTTKIKTFKPDLSIPLRTSPAAHQVTDEYLAKFKKAQAAMRALPDDDPRSMVQQAKVHCAYCNGAYPQVGFTDNDIQVHFSWLFFPFHRMYLYFYERILGKLIDDPTFALPYWNWDSPVGFPIPDIYTDTSSPLYDQYRNADHQPPVLVDLSYGGKDDDVDEQTRIDENLAIMYRQMVSGAKTPDLFFGHAYRAGNLNTGKYPGTIENMPHNNIHIWVGDPSQTHQEDMGNFYSAGRDPLFYAHHANVDRMWNIWKTLGGKRKDITDTDWLDAEFLFYDENAELVRVKVRDSLEPEKQLRYNYEPVSLPWLFTKPTARKTKNKTKAKVAATQLTSKFPATLVEVTTVEVARPKPRKRSKKEKVDEEELLIIKDIEFEGTEAVKFDVFINDDAESLSRRDKSEFAGSFVHVPQGKTTKAKTKTNLKLGITDLLEDLGAEDDSSVLVTLVPRVSNSPITIGGFKIEYSS |
Enzyme Length | 597 |
Uniprot Accession Number | O81103 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Activated in the presence of substrate at low pH (PubMed:28812349). Specific activity fluctuates during fruit ripening, starting at immature-green stage, reaching a peak at the breaker stage, followed by a sharp decrease until the half-ripe stage to remain stable during the following development stages (PubMed:10198084). Triggered by CuSO(4) and by low concentrations of SDS. Repressed by several inhibitors including 4-hexylresorcinol, ascorbic acid, benzoic acid, kojic acid, glutathione (reduced form), L-cysteine and sodium metabisulfite. Inhibited by various salt such as FeSO(4), KCl, NaCl, CaCl(2), MnCl(2), NiCl(2) and AlCl(3). Spontaneously activated during storage at 4 degrees Celsius (PubMed:28812349). {ECO:0000269|PubMed:10198084, ECO:0000269|PubMed:28812349}. |
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:10198084, ECO:0000269|PubMed:28812349}; |
DNA Binding | |
EC Number | 1.10.3.1 |
Enzyme Function | FUNCTION: [Polyphenol oxidase active form, chloroplastic]: Catalyzes the oxidation of mono- and o-diphenols to o-diquinones. Uses preferentially 4-methylcatechol and chlorogenic acid as substrates, followed by caffeic acid, pyrogallol, and catechol, but barely active toward dopamine and L-dopa. No activity detected with monophenols (e.g. phenol and tyramine). {ECO:0000269|PubMed:28812349}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius with catechol as substrate. Completely inactivated after heating at 70 degrees Celsius for 10 min. {ECO:0000269|PubMed:28812349}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5 with catechol as substrate. {ECO:0000269|PubMed:28812349}; |
Pathway | |
nucleotide Binding | |
Features | Chain (2); Compositional bias (1); Cross-link (1); Disulfide bond (2); Metal binding (6); Region (1); Site (1); Transit peptide (2) |
Keywords | Chloroplast;Copper;Direct protein sequencing;Disulfide bond;Metal-binding;Oxidoreductase;Plastid;Thioether bond;Thylakoid;Transit peptide |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen {ECO:0000250|UniProtKB:Q6UIL3}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 67,133 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 mM for 4-methylcatechol {ECO:0000269|PubMed:28812349}; KM=2.7 mM for chlorogenic acid {ECO:0000269|PubMed:28812349}; KM=5.3 mM for catechol {ECO:0000269|PubMed:28812349}; KM=11 mM for pyrogallol {ECO:0000269|PubMed:28812349}; Note=kcat is 700 sec(-1) with 4-methylcatechol as substrate. kcat is 1400 sec(-1) with chlorogenic acid as substrate. kcat is 210 sec(-1) with catechol as substrate. kcat is 590 sec(-1) with pyrogallol as substrate. {ECO:0000269|PubMed:28812349}; |
Metal Binding | METAL 188; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 209; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 218; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 341; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 345; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 375; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19 |
Rhea ID | RHEA:21632 |
Cross Reference Brenda |