IED ID | IndEnz0019000013 |
Enzyme Type ID | polyphenol oxidase000013 |
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 |