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Literature summary extracted from

  • del Mar Garcia-Molina, M.; Munoz-Munoz, J.L.; Berna, J.; Garcia-Ruiz, P.A.; Rodriguez-Lopez, J.N.; Garcia-Canovas, F.
    Catalysis and inactivation of tyrosinase in its action on hydroxyhydroquinone (2014), IUBMB Life, 66, 122-127 .
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.18.1 additional information
-
additional information possible kinetic mechanism for explaining the action of tyrosinase on hydroxyhydroquinone, detailed overview Agaricus bisporus
1.14.18.1 0.4
-
Hydroxyhydroquinone pH and temperature not specified in the publication Agaricus bisporus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.18.1 Cu2+ a copper-containing enzyme Agaricus bisporus

Organism

EC Number Organism UniProt Comment Textmining
1.14.18.1 Agaricus bisporus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.18.1 commercial preparation
-
Agaricus bisporus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.18.1 hydroxyhydroquinone + O2 the oxidation of hydroxyhydroquinone by O2 catalyzed by tyrosinase occurs simultaneously with the non-enzymatic oxidation of hydroxyhydroquinone at pH 7.0, the identical isosbestic points indicating that there is a stoichiometric transformation from hydroxyhydroquinone to 2-hydroxy p-benzoquinone, a red p-quinone Agaricus bisporus 2-hydroxy-p-benzoquinone + H2O
-
?
1.14.18.1 additional information hydroxyhydroquinone autooxidation depends on the pH, overview Agaricus bisporus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.14.18.1 mushroom tyrosinase
-
Agaricus bisporus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.18.1 229
-
Hydroxyhydroquinone pH and temperature not specified in the publication Agaricus bisporus