EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.18.1 | ascorbic acid | - |
Agaricus bisporus | |
1.14.18.1 | beta-arbutin | competitive | Agaricus bisporus | |
1.14.18.1 | deoxyarbutin | competitive, a potent inhibitor of tyrosinase that can also act as substrate of the enzyme, shows membrane breaking and toxicity towards melanosomes, induces hydroxyl free radicals. Inhibition mechanism, overview | Agaricus bisporus | |
1.14.18.1 | deoxyfuran | - |
Agaricus bisporus | |
1.14.18.1 | fluorodeoxyarbutin | - |
Agaricus bisporus | |
1.14.18.1 | hydroquinone | shows membrane breaking and toxicity towards melanosomes, and induces hydroxyl free radicals | Agaricus bisporus | |
1.14.18.1 | thiodeoxyarbutin | - |
Agaricus bisporus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.18.1 | 0.033 | - |
deoxyarbutin | pH and temperature not specified in the publication | Agaricus bisporus | |
1.14.18.1 | 3 | - |
beta-arbutin | pH and temperature not specified in the publication | Agaricus bisporus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.18.1 | Cu2+ | a copper-containing enzyme, the catalytic centre of tyrosinase has two copper atoms each coordinated with three histidine residues. These copper atoms have different oxidation and coordination modes, depending on the enzymatic form: Cu2+Cu2+ in Em (metatyrosinase), Cu1+Cu1+ in Ed (deoxytyrosinase), and Cu2+Cu2+O22- in Eox (oxytyrosinase) | Agaricus bisporus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.18.1 | Agaricus bisporus | C7FF04 | - |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.14.18.1 | commercial preparation | - |
Agaricus bisporus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.18.1 | beta-arbutin + O2 | - |
Agaricus bisporus | ? | - |
? | |
1.14.18.1 | deoxyarbutin + O2 | oxytyrosinase is able to hydroxylate deoxyarbutin and finishes the catalytic cycle by oxidizing the formed o-diphenol to quinone, while the enzyme becomes deoxytyrosinase, which evolves to oxytyrosinase in the presence of oxygen. deoxyarbutin can alsio act as enzyme inhibitor. This compound is the only one described that does not release o-diphenol after the hydroxylation step. Oxytyrosinase hydroxylates the deoxyarbutin in ortho position of the phenolic hydroxyl group by means of an aromatic electrophilic substitution. As the oxygen orbitals and the copper atoms are not coplanar, but in axial/equatorial position, the concerted oxidation/reduction cannot occur and the release of a copper atom to bind again in coplanar position, enabling the oxidation/reduction or release of the o-diphenol from the active site to the medium. In the case of deoxyarbutin, the o-diphenol formed is repulsed by the water due to its hydrophobicity, and so can bind correctly and be oxidized to a quinone before being released | Agaricus bisporus | ? | - |
? | |
1.14.18.1 | additional information | tyrosinase uses molecular oxygen as cosubstrate to catalyse the ortho-hydroxylation of monophenols to o-diphenols (monophenolase activity), and the oxidation of o-diphenols to o-quinones (diphenolase activity) | Agaricus bisporus | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.18.1 | mushroom tyrosinase | - |
Agaricus bisporus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.18.1 | 1.95 | - |
deoxyarbutin | pH and temperature not specified in the publication | Agaricus bisporus | |
1.14.18.1 | 3.77 | - |
beta-arbutin | pH and temperature not specified in the publication | Agaricus bisporus |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.18.1 | 0.04 | - |
deoxyarbutin | inhibition of diphenolase activity, pH and temperature not specified in the publication | Agaricus bisporus | |
1.14.18.1 | 0.078 | - |
deoxyarbutin | inhibition of monophenolase activity, pH and temperature not specified in the publication | Agaricus bisporus | |
1.14.18.1 | 0.9 | - |
beta-arbutin | inhibition of diphenolase activity, pH and temperature not specified in the publication | Agaricus bisporus | |
1.14.18.1 | 1.42 | - |
beta-arbutin | inhibition of monophenolase activity, pH and temperature not specified in the publication | Agaricus bisporus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.18.1 | additional information | molecular dynamic computational simulations of tyrosinase and the interaction of beta-arbutin, deoxyarbutin and their o-diphenol products with tyrosinase show how these ligands bind at the copper centre of tyrosinase, using enzyme crystal structure, PDB ID 2Y9W. The presence of an energy barrier in the release of the o-diphenol product of deoxyarbutin, which is not present in the case of beta-arbutin, together with the differences in polarity and, consequently differences in their interaction with water explain the differences in the kinetic behaviour of both compounds. The release of the o-diphenol product of deoxyarbutin from the active site might be slower than in the case of beta-arbutin, contributing to its oxidation to a quinone before being released from the protein into the water phase. Computational simulations of o-diphenol binding | Agaricus bisporus |
1.14.18.1 | physiological function | the enzyme is responsible for the browning of fruits, vegetables, fungi and crustaceans and is essential in the melanogenesis process of human skin pigmentation for protection from UV-induced damage. Nevertheless, its excessive accumulation can produce hyperpigmentation disorders such as freckles, solar lentigines, ephelide, and melasma | Agaricus bisporus |