| IED ID | IndEnz0016000027 |
| Enzyme Type ID | tyrosinase000027 |
| Protein Name |
Polyphenol oxidase PPO EC 1.10.3.1 Catechol oxidase Fragment |
| Gene Name | |
| Organism | Zingiber officinale (Ginger) (Amomum zingiber) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Zingiberales Zingiberaceae Zingiber Zingiber officinale (Ginger) (Amomum zingiber) |
| Enzyme Sequence | EQGVGGDDGL |
| Enzyme Length | 10 |
| Uniprot Accession Number | P85026 |
| 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|Ref.1}; |
| DNA Binding | |
| EC Number | 1.10.3.1 |
| Enzyme Function | FUNCTION: Catalyzes the oxidation of mono- and o-diphenols to o-diquinones. {ECO:0000269|Ref.1}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. There is only a slight decrease in activity at 75 degrees Celsius and a sharp decrease in activity at 90 degrees Celsius. {ECO:0000269|Ref.1}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5. Active from pH 3.0 to 8.0. The activity decreases sharply above pH 7.5. {ECO:0000269|Ref.1}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (1) |
| Keywords | Copper;Direct protein sequencing;Metal-binding;Oxidoreductase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000269|Ref.1}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 946 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21632 |
| Cross Reference Brenda |