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Literature summary extracted from

  • Selinheimo, E.; NiEidhin, D.; Steffensen, C.; Nielsen, J.; Lomascolo, A.; Halaouli, S.; Record, E.; OBeirne, D.; Buchert, J.; Kruus, K.
    Comparison of the characteristics of fungal and plant tyrosinases (2007), J. Biotechnol., 130, 471-480.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.18.1 2-mercaptoethanol
-
Agaricus bisporus
1.14.18.1 2-mercaptoethanol
-
Solanum tuberosum
1.14.18.1 2-mercaptoethanol
-
Trametes sanguinea
1.14.18.1 2-mercaptoethanol
-
Trichoderma reesei
1.14.18.1 benzaldehyde
-
Agaricus bisporus
1.14.18.1 benzaldehyde
-
Malus domestica
1.14.18.1 benzaldehyde
-
Solanum tuberosum
1.14.18.1 benzaldehyde
-
Trametes sanguinea
1.14.18.1 benzaldehyde
-
Trichoderma reesei
1.14.18.1 beta-mercaptoethanol
-
Malus domestica
1.14.18.1 EDTA
-
Agaricus bisporus
1.14.18.1 EDTA
-
Malus domestica
1.14.18.1 EDTA
-
Solanum tuberosum
1.14.18.1 EDTA
-
Trametes sanguinea
1.14.18.1 EDTA
-
Trichoderma reesei
1.14.18.1 glutathione
-
Agaricus bisporus
1.14.18.1 glutathione
-
Malus domestica
1.14.18.1 glutathione
-
Solanum tuberosum
1.14.18.1 glutathione
-
Trametes sanguinea
1.14.18.1 glutathione
-
Trichoderma reesei
1.14.18.1 kojic acid
-
Agaricus bisporus
1.14.18.1 kojic acid
-
Malus domestica
1.14.18.1 kojic acid
-
Solanum tuberosum
1.14.18.1 kojic acid
-
Trametes sanguinea
1.14.18.1 kojic acid
-
Trichoderma reesei
1.14.18.1 NaCl
-
Agaricus bisporus
1.14.18.1 NaCl
-
Malus domestica
1.14.18.1 NaCl
-
Solanum tuberosum
1.14.18.1 NaCl
-
Trametes sanguinea
1.14.18.1 NaCl
-
Trichoderma reesei
1.14.18.1 SDS
-
Agaricus bisporus
1.14.18.1 SDS
-
Malus domestica
1.14.18.1 SDS
-
Solanum tuberosum
1.14.18.1 SDS
-
Trametes sanguinea
1.14.18.1 SDS
-
Trichoderma reesei
1.14.18.1 Sodium azide
-
Agaricus bisporus
1.14.18.1 Sodium azide
-
Malus domestica
1.14.18.1 Sodium azide
-
Solanum tuberosum
1.14.18.1 Sodium azide
-
Trametes sanguinea
1.14.18.1 Sodium azide
-
Trichoderma reesei

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.18.1 13400
-
2 * 13400 + 2 * 43000, SDS-PAGE Agaricus bisporus
1.14.18.1 43000
-
2 * 13400 + 2 * 43000, SDS-PAGE Agaricus bisporus
1.14.18.1 43500
-
determined by mass spectrometry Trichoderma reesei
1.14.18.1 45000
-
determined by SDS-PAGE Trametes sanguinea
1.14.18.1 45000
-
determined by SDS-PAGE Malus domestica
1.14.18.1 45000
-
determined by SDS-PAGE Solanum tuberosum
1.14.18.1 112800
-
-
Agaricus bisporus

Organism

EC Number Organism UniProt Comment Textmining
1.14.18.1 Agaricus bisporus O42713
-
-
1.14.18.1 Malus domestica
-
-
-
1.14.18.1 Solanum tuberosum Q41428 tyrosinases from apple, potato, the white rot fungus Pycnoporus sanguineus, the filamentous fungus Trichoderma reesei and the edible mushroom Agaricus bisporus are compared for their biochemical characteristics
-
1.14.18.1 Trametes sanguinea
-
-
-
1.14.18.1 Trichoderma reesei
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.18.1
-
Trichoderma reesei
1.14.18.1
-
Trametes sanguinea

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 (+)-catechin hydrate + 1/2 O2
-
Trichoderma reesei ?
-
?
1.14.18.1 (+)-catechin hydrate + 1/2 O2
-
Trametes sanguinea ?
-
?
1.14.18.1 (+)-catechin hydrate + 1/2 O2
-
Malus domestica ?
-
?
1.14.18.1 (+)-catechin hydrate + 1/2 O2
-
Agaricus bisporus ?
-
?
1.14.18.1 (+)-catechin hydrate + 1/2 O2
-
Solanum tuberosum ?
-
?
1.14.18.1 (-)-epicatechin + 1/2 O2
-
Trichoderma reesei ?
-
?
1.14.18.1 (-)-epicatechin + 1/2 O2
-
Trametes sanguinea ?
-
?
1.14.18.1 (-)-epicatechin + 1/2 O2
-
Malus domestica ?
-
?
1.14.18.1 (-)-epicatechin + 1/2 O2
-
Agaricus bisporus ?
-
?
1.14.18.1 (-)-epicatechin + 1/2 O2
-
Solanum tuberosum ?
-
?
1.14.18.1 caffeic acid + 1/2 O2
-
Trichoderma reesei caffeoyl quinone + H2O
-
?
1.14.18.1 caffeic acid + 1/2 O2
-
Malus domestica caffeoyl quinone + H2O
-
?
1.14.18.1 caffeic acid + 1/2 O2
-
Agaricus bisporus caffeoyl quinone + H2O
-
?
1.14.18.1 caffeic acid + 1/2 O2
-
Solanum tuberosum caffeoyl quinone + H2O
-
?
1.14.18.1 caffeic acid + 1/2 O2 diphenolic caffeic acid is oxidized relatively fast by all tyrosinases, except only moderately by tyrosinase from Pycnoporus sanguineus Trametes sanguinea caffeoyl quinone + H2O
-
?
1.14.18.1 D-dopa + 1/2 O2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms Trichoderma reesei D-dopaquinone + H2O
-
?
1.14.18.1 D-dopa + 1/2 O2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms Trametes sanguinea D-dopaquinone + H2O
-
?
1.14.18.1 D-dopa + 1/2 O2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms. Because the activity of the tyrosinase on tyrosine is practically nondetectable, no significant differences between the oxidation rates on the D-, DL- and D-forms of tyrosine can be measured for tyrosinase Malus domestica D-dopaquinone + H2O
-
?
1.14.18.1 D-dopa + 1/2 O2 tyrosinase oxidizes L- and D-forms with similar rate Agaricus bisporus D-dopaquinone + H2O
-
?
1.14.18.1 D-dopa + 1/2 O2 tyrosinase oxidizes L- and D-forms with similar rate Solanum tuberosum D-dopaquinone + H2O
-
?
1.14.18.1 D-tyrosine + O2 + AH2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms Trichoderma reesei D-dopa + H2O + A
-
?
1.14.18.1 D-tyrosine + O2 + AH2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms Trametes sanguinea D-dopa + H2O + A
-
?
1.14.18.1 D-tyrosine + O2 + AH2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms. Because the activity of the tyrosinase on tyrosine is practically nondetectable, no significant differences between the oxidation rates on the D-, DL- and D-forms of tyrosine can be measured for tyrosinase Malus domestica D-dopa + H2O + A
-
?
1.14.18.1 D-tyrosine + O2 + AH2 tyrosinase oxidizes L- and D-forms with similar rate Agaricus bisporus D-dopa + H2O + A
-
?
1.14.18.1 D-tyrosine + O2 + AH2 tyrosinase oxidizes L- and D-forms with similar rate Solanum tuberosum D-dopa + H2O + A
-
?
1.14.18.1 DL-dopa + 1/2 O2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms Trichoderma reesei DL-dopaquinone + H2O
-
?
1.14.18.1 DL-dopa + 1/2 O2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms Trametes sanguinea DL-dopaquinone + H2O
-
?
1.14.18.1 DL-dopa + 1/2 O2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms. Because the activity of the tyrosinase on tyrosine is practically nondetectable, no significant differences between the oxidation rates on the D-, DL- and D-forms of tyrosine can be measured for tyrosinase Malus domestica DL-dopaquinone + H2O
-
?
1.14.18.1 DL-dopa + 1/2 O2 tyrosinase oxidizes L- and D-forms with similar rate Agaricus bisporus DL-dopaquinone + H2O
-
?
1.14.18.1 DL-dopa + 1/2 O2 tyrosinase oxidizes L- and D-forms with similar rate Solanum tuberosum DL-dopaquinone + H2O
-
?
1.14.18.1 DL-tyrosine + O2 + AH2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms Trichoderma reesei DL-dopa + H2O + A
-
?
1.14.18.1 DL-tyrosine + O2 + AH2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms Trametes sanguinea DL-dopa + H2O + A
-
?
1.14.18.1 DL-tyrosine + O2 + AH2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms. Because the activity of the tyrosinase on tyrosine is practically nondetectable, no significant differences between the oxidation rates on the D-, DL- and D-forms of tyrosine can be measured for tyrosinase Malus domestica DL-dopa + H2O + A
-
?
1.14.18.1 DL-tyrosine + O2 + AH2 tyrosinase oxidizes L- and D-forms with similar rate Agaricus bisporus DL-dopa + H2O + A
-
?
1.14.18.1 DL-tyrosine + O2 + AH2 tyrosinase oxidizes L- and D-forms with similar rate Solanum tuberosum DL-dopa + H2O + A
-
?
1.14.18.1 L-dopa + 1/2 O2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms Trichoderma reesei L-dopaquinone + H2O
-
?
1.14.18.1 L-dopa + 1/2 O2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms Trametes sanguinea L-dopaquinone + H2O
-
?
1.14.18.1 L-dopa + 1/2 O2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms. Because the activity of the tyrosinase on tyrosine is practically nondetectable, no significant differences between the oxidation rates on the D-, DL- and D-forms of tyrosine can be measured for tyrosinase Malus domestica L-dopaquinone + H2O
-
?
1.14.18.1 L-dopa + 1/2 O2 tyrosinase oxidizes L- and D-forms with similar rate Agaricus bisporus L-dopaquinone + H2O
-
?
1.14.18.1 L-dopa + 1/2 O2 tyrosinase oxidizes L- and D-forms with similar rate Solanum tuberosum L-dopaquinone + H2O
-
?
1.14.18.1 L-tyrosine + O2 + AH2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms Trichoderma reesei L-dopa + H2O + A
-
?
1.14.18.1 L-tyrosine + O2 + AH2 L-forms of dopa and tyrosine are much better substrates than the corresponding D-forms Trametes sanguinea L-dopa + H2O + A
-
?
1.14.18.1 L-tyrosine + O2 + AH2 tyrosinase oxidizes L- and D-forms with similar rate Agaricus bisporus L-dopa + H2O + A
-
?
1.14.18.1 L-tyrosine + O2 + AH2 tyrosinase oxidizes L- and D-forms with similar rate Solanum tuberosum L-dopa + H2O + A
-
?
1.14.18.1 additional information accepts both mono- and diphenols as substrates. The hydroxylation ability of the enzyme is also referred to cresolase or monophenolase activity (EC 1.14.18.1), and the oxidation ability to catecholase or diphenolase activity (EC 1.10.3.1). The tyrosinases generally have noticeably lower activity on monophenols than on di- or triphenols, the activity of tyrosinase from Pycnoporus sanguineus on tyrosine is particularly low. Ferulic acid is not a substrate to any of the tyrosinases. The substrate p-coumaric acid is rapidly oxidized only by tyrosinase from Trichoderma reesei Trametes sanguinea ?
-
?
1.14.18.1 additional information accepts both mono- and diphenols as substrates. The hydroxylation ability of the enzyme is also referred to cresolase or monophenolase activity (EC 1.14.18.1), and the oxidation ability to catecholase or diphenolase activity (EC 1.10.3.1). The tyrosinases generally have noticeably lower activity on monophenols than on di- or triphenols. Ferulic acid is not a substrate to any of the tyrosinases. The substrate p-coumaric acid is rapidly oxidized only by tyrosinase from Trichoderma reesei Agaricus bisporus ?
-
?
1.14.18.1 additional information accepts both mono- and diphenols as substrates. The hydroxylation ability of the enzyme is also referred to cresolase or monophenolase activity (EC 1.14.18.1), and the oxidation ability to catecholase or diphenolase activity (EC 1.10.3.1). The tyrosinases generally have noticeably lower activity on monophenols than on di- or triphenols. Ferulic acid is not a substrate to any of the tyrosinases. The substrate p-coumaric acid is rapidly oxidized only by tyrosinase from Trichoderma reesei Solanum tuberosum ?
-
?
1.14.18.1 additional information accepts both mono- and diphenols as substrates. The hydroxylation ability of the enzyme is also referred to cresolase or monophenolase activity (EC 1.14.18.1), and the oxidation ability to catecholase or diphenolase activity (EC 1.10.3.1). The tyrosinases generally have noticeably lower activity on monophenols than on di- or triphenols. The activity of tyrosinase on tyrosine is particularly low. Ferulic acid is not a substrate to any of the tyrosinases. The substrate p-coumaric acid is rapidly oxidized only by tyrosinase from Trichoderma reesei Malus domestica ?
-
?
1.14.18.1 additional information accepts both mono- and diphenols as substrates. The hydroxylation ability of the enzyme is also referred to cresolase or monophenolase activity (EC 1.14.18.1), and the oxidation ability to catecholase or diphenolase activity (EC 1.10.3.1). The tyrosinases generally have noticeably lower activity on monophenols than on di- or triphenols. Tyrosinase from Trichoderma reesei shows the best ability to crosslink alpha-casein. Tyrosinase from Trichoderma reesei also has the highest activity on most of the tested monophenols, and shows noticeable short lag periods prior to the oxidation. Ferulic acid is not a substrate to any of the tyrosinases Trichoderma reesei ?
-
?
1.14.18.1 p-coumaric acid + O2 + AH2 p-coumaric acid is rapidly oxidized only by tyrosinase from Trichoderma reesei Trichoderma reesei caffeic acid + H2O + A
-
?
1.14.18.1 p-cresol + O2 relatively well oxidized Solanum tuberosum 4-methylpyrocatechol + H2O
-
?
1.14.18.1 p-cresol + O2 + AH2
-
Trichoderma reesei 4-methylpyrocatechol + H2O + A
-
?
1.14.18.1 p-cresol + O2 + AH2
-
Trametes sanguinea 4-methylpyrocatechol + H2O + A
-
?
1.14.18.1 p-cresol + O2 + AH2
-
Agaricus bisporus 4-methylpyrocatechol + H2O + A
-
?
1.14.18.1 p-cresol + O2 + AH2 relatively well oxidized by tyrosinase Malus domestica 4-methylpyrocatechol + H2O + A
-
?
1.14.18.1 p-tyrosol + O2 + AH2
-
Trichoderma reesei 2-(3,4-dihydroxyphenyl)ethanol + H2O + A
-
?
1.14.18.1 p-tyrosol + O2 + AH2
-
Trametes sanguinea 2-(3,4-dihydroxyphenyl)ethanol + H2O + A
-
?
1.14.18.1 p-tyrosol + O2 + AH2
-
Agaricus bisporus 2-(3,4-dihydroxyphenyl)ethanol + H2O + A
-
?
1.14.18.1 p-tyrosol + O2 + AH2 relatively well oxidized Solanum tuberosum 2-(3,4-dihydroxyphenyl)ethanol + H2O + A
-
?
1.14.18.1 p-tyrosol + O2 + AH2 relatively well oxidized by tyrosinase Malus domestica 2-(3,4-dihydroxyphenyl)ethanol + H2O + A
-
?
1.14.18.1 phenol + O2 + AH2
-
Trichoderma reesei o-dihydroxybenzene + H2O + A
-
?
1.14.18.1 phenol + O2 + AH2
-
Trametes sanguinea o-dihydroxybenzene + H2O + A
-
?
1.14.18.1 phenol + O2 + AH2
-
Malus domestica catechol + H2O + A
-
?
1.14.18.1 phenol + O2 + AH2
-
Agaricus bisporus catechol + H2O + A
-
?
1.14.18.1 phenol + O2 + AH2
-
Solanum tuberosum catechol + H2O + A
-
?
1.14.18.1 pyrocatechol + 1/2 O2
-
Trichoderma reesei 1,2-benzoquinone + H2O
-
?
1.14.18.1 pyrocatechol + 1/2 O2
-
Trametes sanguinea 1,2-benzoquinone + H2O
-
?
1.14.18.1 pyrocatechol + 1/2 O2
-
Malus domestica 1,2-benzoquinone + H2O
-
?
1.14.18.1 pyrocatechol + 1/2 O2
-
Agaricus bisporus 1,2-benzoquinone + H2O
-
?
1.14.18.1 pyrocatechol + 1/2 O2
-
Solanum tuberosum 1,2-benzoquinone + H2O
-
?
1.14.18.1 pyrogallol + 1/2 O2
-
Trichoderma reesei ?
-
?
1.14.18.1 pyrogallol + 1/2 O2
-
Trametes sanguinea ?
-
?
1.14.18.1 pyrogallol + 1/2 O2
-
Malus domestica ?
-
?
1.14.18.1 pyrogallol + 1/2 O2
-
Agaricus bisporus ?
-
?
1.14.18.1 pyrogallol + 1/2 O2
-
Solanum tuberosum ?
-
?
1.14.18.1 tyramine + O2
-
Trichoderma reesei 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O
-
?
1.14.18.1 tyramine + O2
-
Trametes sanguinea 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O
-
?
1.14.18.1 tyramine + O2
-
Malus domestica 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O
-
?
1.14.18.1 tyramine + O2
-
Agaricus bisporus 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O
-
?
1.14.18.1 tyramine + O2
-
Solanum tuberosum 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O
-
?

Subunits

EC Number Subunits Comment Organism
1.14.18.1 tetramer 2 * 13400 + 2 * 43000, SDS-PAGE Agaricus bisporus

Synonyms

EC Number Synonyms Comment Organism
1.14.18.1 AbPPO1
-
Agaricus bisporus
1.14.18.1 monophenol, o-diphenol:oxygen oxidoreductase
-
Trichoderma reesei
1.14.18.1 monophenol, o-diphenol:oxygen oxidoreductase
-
Trametes sanguinea
1.14.18.1 monophenol, o-diphenol:oxygen oxidoreductase
-
Malus domestica
1.14.18.1 monophenol, o-diphenol:oxygen oxidoreductase
-
Agaricus bisporus
1.14.18.1 monophenol, o-diphenol:oxygen oxidoreductase
-
Solanum tuberosum
1.14.18.1 polyphenol oxidase
-
Trichoderma reesei
1.14.18.1 polyphenol oxidase
-
Trametes sanguinea
1.14.18.1 polyphenol oxidase
-
Malus domestica
1.14.18.1 polyphenol oxidase
-
Agaricus bisporus
1.14.18.1 polyphenol oxidase
-
Solanum tuberosum
1.14.18.1 PotPPO
-
Solanum tuberosum
1.14.18.1 tyrosinase
-
Trichoderma reesei
1.14.18.1 tyrosinase
-
Trametes sanguinea
1.14.18.1 tyrosinase
-
Malus domestica
1.14.18.1 tyrosinase
-
Agaricus bisporus
1.14.18.1 tyrosinase
-
Solanum tuberosum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.18.1 25
-
enzyme activity assay at Trichoderma reesei
1.14.18.1 25
-
enzyme activity assay at Trametes sanguinea
1.14.18.1 25
-
enzyme activity assay at Malus domestica
1.14.18.1 25
-
enzyme activity assay at Agaricus bisporus
1.14.18.1 25
-
enzyme activity assay at Solanum tuberosum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.18.1 6 7 pH-optimum Agaricus bisporus
1.14.18.1 6 6.5 pH-optimum Malus domestica
1.14.18.1 6 6.5 pH-optimum Solanum tuberosum
1.14.18.1 6.5 7 pH-optimum Trametes sanguinea
1.14.18.1 7
-
enzyme activity assay at Trichoderma reesei
1.14.18.1 7
-
enzyme activity assay at Trametes sanguinea
1.14.18.1 7
-
enzyme activity assay at Malus domestica
1.14.18.1 7
-
enzyme activity assay at Agaricus bisporus
1.14.18.1 7
-
enzyme activity assay at Solanum tuberosum
1.14.18.1 8 9.5 pH-optimum Trichoderma reesei

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.14.18.1 5 8 active at this pH-range Trametes sanguinea
1.14.18.1 5.5 8.5 active at this pH-range Solanum tuberosum
1.14.18.1 5.5 8 active at this pH-range Malus domestica
1.14.18.1 6 10 active at this pH-range Trichoderma reesei

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.14.18.1 Trametes sanguinea
-
-
4.55
1.14.18.1 Agaricus bisporus
-
-
4.75
1.14.18.1 Trichoderma reesei
-
-
9