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Literature summary for 1.14.18.1 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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0077
-
tyramine pH 5.0, 25°C Vitis vinifera
0.0161
-
L-Dopa pH 5.0, 25°C Vitis vinifera

Metals/Ions

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
analytical ultracentrifugation, native PAGE, and gel filtration Vitis vinifera

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 L-dopa + O2 Vitis vinifera
-
2 dopaquinone + 2 H2O
-
?
additional information Vitis vinifera polyphenoloxidases, PPOs, from Dornfelder and Riesling grapes display both monophenolase and diphenolase activity ?
-
?

Organism

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

Source Tissue

Source Tissue Comment Organism Textmining
berry
-
Vitis vinifera
-
fruit
-
Vitis vinifera
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 L-dopa + O2
-
Vitis vinifera 2 dopaquinone + 2 H2O
-
?
4-coumaric acid + O2
-
Vitis vinifera ?
-
?
additional information polyphenoloxidases, PPOs, from Dornfelder and Riesling grapes display both monophenolase and diphenolase activity Vitis vinifera ?
-
?
tyramine + O2
-
Vitis vinifera ?
-
?

Subunits

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

Synonyms

Synonyms Comment Organism
polyphenoloxidase
-
Vitis vinifera
PPO
-
Vitis vinifera

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.88
-
tyramine pH 5.0, 25°C Vitis vinifera
72.12
-
L-Dopa pH 5.0, 25°C Vitis vinifera

pH Optimum

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

General Information

General Information Comment Organism
evolution the enzyme belongs to the type-3 copper protein family Vitis vinifera
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
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]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
374
-
tyramine pH 5.0, 25°C Vitis vinifera
4479.5
-
L-Dopa pH 5.0, 25°C Vitis vinifera