EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.18.1 | 0.0077 | - |
tyramine | pH 5.0, 25°C | Vitis vinifera | |
1.14.18.1 | 0.0161 | - |
L-Dopa | pH 5.0, 25°C | Vitis vinifera |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.18.1 | Cu2+ | two copper ions, CuA and CuB | Vitis vinifera |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.14.18.1 | 38000 | - |
analytical ultracentrifugation, native PAGE, and gel filtration | Vitis vinifera |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.18.1 | 2 L-dopa + O2 | Vitis vinifera | - |
2 dopaquinone + 2 H2O | - |
? | |
1.14.18.1 | additional information | Vitis vinifera | polyphenoloxidases, PPOs, from Dornfelder and Riesling grapes display both monophenolase and diphenolase activity | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.18.1 | Vitis vinifera | - |
cvs. Riesling and Dornfelder | - |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.14.18.1 | berry | - |
Vitis vinifera | - |
1.14.18.1 | fruit | - |
Vitis vinifera | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.18.1 | 2 L-dopa + O2 | - |
Vitis vinifera | 2 dopaquinone + 2 H2O | - |
? | |
1.14.18.1 | 4-coumaric acid + O2 | - |
Vitis vinifera | ? | - |
? | |
1.14.18.1 | additional information | polyphenoloxidases, PPOs, from Dornfelder and Riesling grapes display both monophenolase and diphenolase activity | Vitis vinifera | ? | - |
? | |
1.14.18.1 | tyramine + O2 | - |
Vitis vinifera | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.18.1 | monomer | 1 * 38000-40000, SDS-PAGE | Vitis vinifera |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.18.1 | polyphenoloxidase | - |
Vitis vinifera |
1.14.18.1 | PPO | - |
Vitis vinifera |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.14.18.1 | 25 | - |
assay at | Vitis vinifera |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.18.1 | 2.88 | - |
tyramine | pH 5.0, 25°C | Vitis vinifera | |
1.14.18.1 | 72.12 | - |
L-Dopa | pH 5.0, 25°C | Vitis vinifera |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.14.18.1 | 5 | - |
assay at | Vitis vinifera |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.18.1 | evolution | the enzyme belongs to the type-3 copper protein family | Vitis vinifera |
1.14.18.1 | additional information | molecular dynamic analysis indicate that the hydroxyl group of monophenolic substrates can bind to copper ion CuA after the flexible but sterically hindering Phe259 swings away on a picosecond time scale. The hydroxide is replaced by a peroxide ion bridging CuA with CuB. The substrate 4-coumaric acid is orientated in a similar position as described previously for tyrosine which hydroxylic oxygen is pointing to the free coordination point above CuA and the phenolic ring was in a Pi-Pi interaction with the imidazol ring of His243, molecular dynamic simulations, overview | Vitis vinifera |
1.14.18.1 | physiological function | polyphenoloxidases (PPO) of the type-3 copper protein family are considered to be catecholoxidases catalyzing the oxidation of o-diphenols to their corresponding quinones | Vitis vinifera |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.18.1 | 374 | - |
tyramine | pH 5.0, 25°C | Vitis vinifera | |
1.14.18.1 | 4479.5 | - |
L-Dopa | pH 5.0, 25°C | Vitis vinifera |