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Literature summary extracted from
- The effect of oxaloacetic acid on tyrosinase activity and structure Integration of inhibition kinetics with docking simulation (2017), Int. J. Biol. Macromol., 101, 59-66 .
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.18.1 | 2-oxoglutaric acid | AKG, a reversible inhibitor of tyrosinase, inhibition kinetics integrated with molecular dynamics simulations reveal a complex induced parabolic slope mixed-type inhibition. AKG significantly inhibits the L-dopa oxidation of tyrosinase in a dose-dependent manner, complete inactivation at about 25 mM. Enzyme residues His85, His259, Asn260, Phe264, Met280, Gly281, and Val283 interact with the inhibitor | Agaricus bisporus |  |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.18.1 | Cu2+ | a copper-containing enzyme | Agaricus bisporus | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.14.18.1 | 128000 | - |
- |
Agaricus bisporus |
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 | Agaricus bisporus | - |
2 dopaquinone + 2 H2O | - |
? | |
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 | 2 L-dopa + O2 | - |
Agaricus bisporus | 2 dopaquinone + 2 H2O | - |
? | |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.18.1 | 25 | - |
assay at | Agaricus bisporus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.18.1 | 7 | - |
assay at | Agaricus bisporus |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.18.1 | additional information | - |
additional information | inhibition kinetics, double-reciprocal kinetic analysis, overview | Agaricus bisporus | |
| 1.14.18.1 | 7.93 | - |
2-oxoglutaric acid | pH 7.0, 25°C | Agaricus bisporus | |
IC50 Value
| EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|---|
| 1.14.18.1 | 15 | - |
pH 7.0, 25°C | Agaricus bisporus | 2-oxoglutaric acid | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.18.1 | physiological function | tyrosinase is a multifunctional copper-containing metalloenzyme that is critical for melanin pigment production anddetoxification of phenol compounds. The catalytic roles of tyrosinase include multifunctional distinctions such as hydroxylaseand oxidase functions, and tyrosinase possesses catalase, peroxygenase, phenolase, and catecholase activities | Agaricus bisporus |
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Release 2023.1 (January 2023)
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