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Literature summary extracted from

  • Garcia-Jimenez, A.; Teruel-Puche, J.A.; Berna, J.; Rodriguez-Lopez, J.N.; Tudela, J.; Garcia-Canovas, F.
    Action of tyrosinase on alpha and beta-arbutin A kinetic study (2017), PLoS ONE, 12, e0177330 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.18.1 H2O2 the addition of hydrogen peroxide transforms Em to Eox, which is able to hydroxylate alpha/beta-arbutin, although the o-quinone that is originated is unstable Agaricus bisporus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.18.1 4-hexylresorcinol
-
 Agaricus bisporus
1.14.18.1 4-n-butylresorcinol
-
 Agaricus bisporus
1.14.18.1 alpha-arbutin inhibition of monophenolase activity, the inhibitory activity of beta-arbutin is higher compared to alpha-arbutin, molecular docking, overview. The hydroxyl group establishes hydrogen bonds with the peroxide ion and polar contacts with a copper ion as well as with residues H259 and H263. The aromatic ring position cannot be stabilized by Pi-Pi-interactions Agaricus bisporus
1.14.18.1 ascorbic acid
-
 Agaricus bisporus
1.14.18.1 beta-arbutin inhibition of monophenolase activity, the inhibitory activity of beta-arbutin is higher compared to alpha-arbutin, molecular docking, overview. The hydroxyl group establishes hydrogen bonds with the peroxide ion and polar contacts with a copper ion as well as with residues H259 and H263. The aromatic ring position cannot be stabilized by Pi-Pi-interactions Agaricus bisporus
1.14.18.1 ellagic acid
-
 Agaricus bisporus
1.14.18.1 hydroquinone
-
 Agaricus bisporus
1.14.18.1 additional information the compounds with resorcinol structure can also act as substrates, react with tyrosinase producing reactive quinones Agaricus bisporus
1.14.18.1 oxyresveratrol
-
 Agaricus bisporus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.18.1 additional information
-
 additional information Michaelis-Menten steady-state kinetics Agaricus bisporus
1.14.18.1 3
-
 beta-arbutin pH 7.0, 25°C Agaricus bisporus
1.14.18.1 6.5
-
 alpha-arbutin pH 7.0, 25°C 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 4-hexylresorcinol + O2
-
 Agaricus bisporus ?
-
 ?
1.14.18.1 4-n-butylresorcinol + O2
-
 Agaricus bisporus ?
-
 ?
1.14.18.1 alpha-arbutin + O2 alpha-arbutin also has a weaker inhibitory effect on the monophenolase activity of the enzyme, molecular docking, overview. The hydroxyl group establishes hydrogen bonds with the peroxide ion and polar contacts with a copper ion as well as with residues H259 and H263. The aromatic ring position cannot be stabilized by Pi-Pi-interactions Agaricus bisporus ?
-
 ?
1.14.18.1 beta-arbutin + O2 alpha-arbutin also has a weaker inhibitory effect on the monophenolase activity of the enzyme, molecular docking, overview. The hydroxyl group establishes hydrogen bonds with the peroxide ion and polar contacts with a copper ion as well as with residues H259 and H263. The aromatic ring position cannot be stabilized by Pi-Pi-interactions Agaricus bisporus ?
-
 ?
1.14.18.1 ellagic acid + O2
-
 Agaricus bisporus ?
-
 ?
1.14.18.1 hydroquinone + O2
-
 Agaricus bisporus ?
-
 ?
1.14.18.1 additional information the oxy form of tyrosinase (oxytyrosinase) hydroxylates alpha and beta-arbutin in ortho position of the phenolic hydroxyl group, giving rise to a complex formed by met-tyrosinase with the hydroxylated alpha or beta-arbutin. This complex can evolve in two ways: by oxidizing the originated o-diphenol to o-quinone and deoxy-tyrosinase, or by delivering the o-diphenol and met-tyrosinase to the medium, which would produce the self-activation of the system. If 3-methyl-2-benzothiazolinone hydrazone hydrochloride hydrate is used, the o-quinone is attacked, so that it becomes an adduct, which can be oxidized by another molecule of o-quinone, generating o-diphenol in the medium. In this way, the system reaches the steady state and originates a chromophore, which, in turn, has a high absorptivity in the visible spectrum and can be measured. The catalysis cannot be quantified because the quinones generated in both cases are unstable. 3-Methyl-2-benzothiazolinone hydrazone, MBTH, is a very potent nucleophile, which, in its deprotonated form, attacks the o-quinone generated by the action of tyrosinase on alpha- and beta-arbutin. The addition of hydrogen peroxide is required and transforms Em to Eox, which is able to hydroxylate arbutin, although the o-quinone that is originated is unstable Agaricus bisporus ?
-
 ?
1.14.18.1 oxyresveratrol + O2
-
 Agaricus bisporus ?
-
 ?
1.14.18.1 rhododendrol + O2
-
 Agaricus bisporus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.18.1 mushroom tyrosinase
-
 Agaricus bisporus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.18.1 25
-
 assay at 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 3.7
-
 beta-arbutin pH 7.0, 25°C Agaricus bisporus
1.14.18.1 4.43
-
 alpha-arbutin pH 7.0, 25°C Agaricus bisporus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.18.1 7
-
 assay at Agaricus bisporus