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Literature summary extracted from

  • Fronk, P.; Hartmann, H.; Bauer, M.; Solem, E.; Jaenicke, E.; Tenzer, S.; Decker, H.
    Polyphenoloxidase from Riesling and Dornfelder wine grapes (Vitis vinifera) is a tyrosinase (2015), Food Chem., 183, 49-57 .
    View publication on PubMed

KM Value [mM]

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.18.1 Cu2+ two copper ions, CuA and CuB Vitis vinifera

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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 ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.18.1 Vitis vinifera
-
cvs. Riesling and Dornfelder
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.18.1 berry
-
Vitis vinifera
-
1.14.18.1 fruit
-
Vitis vinifera
-

Substrates and Products (Substrate)

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 ?
-
?

Subunits

EC Number Subunits Comment Organism
1.14.18.1 monomer 1 * 38000-40000, SDS-PAGE Vitis vinifera

Synonyms

EC Number Synonyms Comment Organism
1.14.18.1 polyphenoloxidase
-
Vitis vinifera
1.14.18.1 PPO
-
Vitis vinifera

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.18.1 25
-
assay at Vitis vinifera

Turnover Number [1/s]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.18.1 5
-
assay at Vitis vinifera

General Information

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

kcat/KM [mM/s]

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