Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-mercaptoethanol | - |
Agaricus bisporus | |
2-mercaptoethanol | - |
Solanum tuberosum | |
2-mercaptoethanol | - |
Trametes sanguinea | |
2-mercaptoethanol | - |
Trichoderma reesei | |
benzaldehyde | - |
Agaricus bisporus | |
benzaldehyde | - |
Malus domestica | |
benzaldehyde | - |
Solanum tuberosum | |
benzaldehyde | - |
Trametes sanguinea | |
benzaldehyde | - |
Trichoderma reesei | |
beta-mercaptoethanol | - |
Malus domestica | |
EDTA | - |
Agaricus bisporus | |
EDTA | - |
Malus domestica | |
EDTA | - |
Solanum tuberosum | |
EDTA | - |
Trametes sanguinea | |
EDTA | - |
Trichoderma reesei | |
glutathione | - |
Agaricus bisporus | |
glutathione | - |
Malus domestica | |
glutathione | - |
Solanum tuberosum | |
glutathione | - |
Trametes sanguinea | |
glutathione | - |
Trichoderma reesei | |
kojic acid | - |
Agaricus bisporus | |
kojic acid | - |
Malus domestica | |
kojic acid | - |
Solanum tuberosum | |
kojic acid | - |
Trametes sanguinea | |
kojic acid | - |
Trichoderma reesei | |
NaCl | - |
Agaricus bisporus | |
NaCl | - |
Malus domestica | |
NaCl | - |
Solanum tuberosum | |
NaCl | - |
Trametes sanguinea | |
NaCl | - |
Trichoderma reesei | |
SDS | - |
Agaricus bisporus | |
SDS | - |
Malus domestica | |
SDS | - |
Solanum tuberosum | |
SDS | - |
Trametes sanguinea | |
SDS | - |
Trichoderma reesei | |
Sodium azide | - |
Agaricus bisporus | |
Sodium azide | - |
Malus domestica | |
Sodium azide | - |
Solanum tuberosum | |
Sodium azide | - |
Trametes sanguinea | |
Sodium azide | - |
Trichoderma reesei |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
13400 | - |
2 * 13400 + 2 * 43000, SDS-PAGE | Agaricus bisporus |
43000 | - |
2 * 13400 + 2 * 43000, SDS-PAGE | Agaricus bisporus |
43500 | - |
determined by mass spectrometry | Trichoderma reesei |
45000 | - |
determined by SDS-PAGE | Trametes sanguinea |
45000 | - |
determined by SDS-PAGE | Malus domestica |
45000 | - |
determined by SDS-PAGE | Solanum tuberosum |
112800 | - |
- |
Agaricus bisporus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Agaricus bisporus | O42713 | - |
- |
Malus domestica | - |
- |
- |
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 | - |
Trametes sanguinea | - |
- |
- |
Trichoderma reesei | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Trichoderma reesei |
- |
Trametes sanguinea |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Agaricus bisporus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(+)-catechin hydrate + 1/2 O2 | - |
Trichoderma reesei | ? | - |
? | |
(+)-catechin hydrate + 1/2 O2 | - |
Trametes sanguinea | ? | - |
? | |
(+)-catechin hydrate + 1/2 O2 | - |
Malus domestica | ? | - |
? | |
(+)-catechin hydrate + 1/2 O2 | - |
Agaricus bisporus | ? | - |
? | |
(+)-catechin hydrate + 1/2 O2 | - |
Solanum tuberosum | ? | - |
? | |
(-)-epicatechin + 1/2 O2 | - |
Trichoderma reesei | ? | - |
? | |
(-)-epicatechin + 1/2 O2 | - |
Trametes sanguinea | ? | - |
? | |
(-)-epicatechin + 1/2 O2 | - |
Malus domestica | ? | - |
? | |
(-)-epicatechin + 1/2 O2 | - |
Agaricus bisporus | ? | - |
? | |
(-)-epicatechin + 1/2 O2 | - |
Solanum tuberosum | ? | - |
? | |
caffeic acid + 1/2 O2 | - |
Trichoderma reesei | caffeoyl quinone + H2O | - |
? | |
caffeic acid + 1/2 O2 | - |
Malus domestica | caffeoyl quinone + H2O | - |
? | |
caffeic acid + 1/2 O2 | - |
Agaricus bisporus | caffeoyl quinone + H2O | - |
? | |
caffeic acid + 1/2 O2 | - |
Solanum tuberosum | caffeoyl quinone + H2O | - |
? | |
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 | - |
? | |
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 | - |
? | |
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 | - |
? | |
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 | - |
? | |
D-dopa + 1/2 O2 | tyrosinase oxidizes L- and D-forms with similar rate | Agaricus bisporus | D-dopaquinone + H2O | - |
? | |
D-dopa + 1/2 O2 | tyrosinase oxidizes L- and D-forms with similar rate | Solanum tuberosum | D-dopaquinone + H2O | - |
? | |
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 | - |
? | |
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 | - |
? | |
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 | - |
? | |
D-tyrosine + O2 + AH2 | tyrosinase oxidizes L- and D-forms with similar rate | Agaricus bisporus | D-dopa + H2O + A | - |
? | |
D-tyrosine + O2 + AH2 | tyrosinase oxidizes L- and D-forms with similar rate | Solanum tuberosum | D-dopa + H2O + A | - |
? | |
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 | - |
? | |
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 | - |
? | |
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 | - |
? | |
DL-dopa + 1/2 O2 | tyrosinase oxidizes L- and D-forms with similar rate | Agaricus bisporus | DL-dopaquinone + H2O | - |
? | |
DL-dopa + 1/2 O2 | tyrosinase oxidizes L- and D-forms with similar rate | Solanum tuberosum | DL-dopaquinone + H2O | - |
? | |
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 | - |
? | |
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 | - |
? | |
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 | - |
? | |
DL-tyrosine + O2 + AH2 | tyrosinase oxidizes L- and D-forms with similar rate | Agaricus bisporus | DL-dopa + H2O + A | - |
? | |
DL-tyrosine + O2 + AH2 | tyrosinase oxidizes L- and D-forms with similar rate | Solanum tuberosum | DL-dopa + H2O + A | - |
? | |
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 | - |
? | |
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 | - |
? | |
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 | - |
? | |
L-dopa + 1/2 O2 | tyrosinase oxidizes L- and D-forms with similar rate | Agaricus bisporus | L-dopaquinone + H2O | - |
? | |
L-dopa + 1/2 O2 | tyrosinase oxidizes L- and D-forms with similar rate | Solanum tuberosum | L-dopaquinone + H2O | - |
? | |
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 | - |
? | |
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 | - |
? | |
L-tyrosine + O2 + AH2 | tyrosinase oxidizes L- and D-forms with similar rate | Agaricus bisporus | L-dopa + H2O + A | - |
? | |
L-tyrosine + O2 + AH2 | tyrosinase oxidizes L- and D-forms with similar rate | Solanum tuberosum | L-dopa + H2O + A | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
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 | ? | - |
? | |
p-coumaric acid + O2 + AH2 | p-coumaric acid is rapidly oxidized only by tyrosinase from Trichoderma reesei | Trichoderma reesei | caffeic acid + H2O + A | - |
? | |
p-cresol + O2 | relatively well oxidized | Solanum tuberosum | 4-methylpyrocatechol + H2O | - |
? | |
p-cresol + O2 + AH2 | - |
Trichoderma reesei | 4-methylpyrocatechol + H2O + A | - |
? | |
p-cresol + O2 + AH2 | - |
Trametes sanguinea | 4-methylpyrocatechol + H2O + A | - |
? | |
p-cresol + O2 + AH2 | - |
Agaricus bisporus | 4-methylpyrocatechol + H2O + A | - |
? | |
p-cresol + O2 + AH2 | relatively well oxidized by tyrosinase | Malus domestica | 4-methylpyrocatechol + H2O + A | - |
? | |
p-tyrosol + O2 + AH2 | - |
Trichoderma reesei | 2-(3,4-dihydroxyphenyl)ethanol + H2O + A | - |
? | |
p-tyrosol + O2 + AH2 | - |
Trametes sanguinea | 2-(3,4-dihydroxyphenyl)ethanol + H2O + A | - |
? | |
p-tyrosol + O2 + AH2 | - |
Agaricus bisporus | 2-(3,4-dihydroxyphenyl)ethanol + H2O + A | - |
? | |
p-tyrosol + O2 + AH2 | relatively well oxidized | Solanum tuberosum | 2-(3,4-dihydroxyphenyl)ethanol + H2O + A | - |
? | |
p-tyrosol + O2 + AH2 | relatively well oxidized by tyrosinase | Malus domestica | 2-(3,4-dihydroxyphenyl)ethanol + H2O + A | - |
? | |
phenol + O2 + AH2 | - |
Trichoderma reesei | o-dihydroxybenzene + H2O + A | - |
? | |
phenol + O2 + AH2 | - |
Trametes sanguinea | o-dihydroxybenzene + H2O + A | - |
? | |
phenol + O2 + AH2 | - |
Malus domestica | catechol + H2O + A | - |
? | |
phenol + O2 + AH2 | - |
Agaricus bisporus | catechol + H2O + A | - |
? | |
phenol + O2 + AH2 | - |
Solanum tuberosum | catechol + H2O + A | - |
? | |
pyrocatechol + 1/2 O2 | - |
Trichoderma reesei | 1,2-benzoquinone + H2O | - |
? | |
pyrocatechol + 1/2 O2 | - |
Trametes sanguinea | 1,2-benzoquinone + H2O | - |
? | |
pyrocatechol + 1/2 O2 | - |
Malus domestica | 1,2-benzoquinone + H2O | - |
? | |
pyrocatechol + 1/2 O2 | - |
Agaricus bisporus | 1,2-benzoquinone + H2O | - |
? | |
pyrocatechol + 1/2 O2 | - |
Solanum tuberosum | 1,2-benzoquinone + H2O | - |
? | |
pyrogallol + 1/2 O2 | - |
Trichoderma reesei | ? | - |
? | |
pyrogallol + 1/2 O2 | - |
Trametes sanguinea | ? | - |
? | |
pyrogallol + 1/2 O2 | - |
Malus domestica | ? | - |
? | |
pyrogallol + 1/2 O2 | - |
Agaricus bisporus | ? | - |
? | |
pyrogallol + 1/2 O2 | - |
Solanum tuberosum | ? | - |
? | |
tyramine + O2 | - |
Trichoderma reesei | 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O | - |
? | |
tyramine + O2 | - |
Trametes sanguinea | 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O | - |
? | |
tyramine + O2 | - |
Malus domestica | 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O | - |
? | |
tyramine + O2 | - |
Agaricus bisporus | 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O | - |
? | |
tyramine + O2 | - |
Solanum tuberosum | 4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | 2 * 13400 + 2 * 43000, SDS-PAGE | Agaricus bisporus |
Synonyms | Comment | Organism |
---|---|---|
AbPPO1 | - |
Agaricus bisporus |
monophenol, o-diphenol:oxygen oxidoreductase | - |
Trichoderma reesei |
monophenol, o-diphenol:oxygen oxidoreductase | - |
Trametes sanguinea |
monophenol, o-diphenol:oxygen oxidoreductase | - |
Malus domestica |
monophenol, o-diphenol:oxygen oxidoreductase | - |
Agaricus bisporus |
monophenol, o-diphenol:oxygen oxidoreductase | - |
Solanum tuberosum |
polyphenol oxidase | - |
Trichoderma reesei |
polyphenol oxidase | - |
Trametes sanguinea |
polyphenol oxidase | - |
Malus domestica |
polyphenol oxidase | - |
Agaricus bisporus |
polyphenol oxidase | - |
Solanum tuberosum |
PotPPO | - |
Solanum tuberosum |
tyrosinase | - |
Trichoderma reesei |
tyrosinase | - |
Trametes sanguinea |
tyrosinase | - |
Malus domestica |
tyrosinase | - |
Agaricus bisporus |
tyrosinase | - |
Solanum tuberosum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
enzyme activity assay at | Trichoderma reesei |
25 | - |
enzyme activity assay at | Trametes sanguinea |
25 | - |
enzyme activity assay at | Malus domestica |
25 | - |
enzyme activity assay at | Agaricus bisporus |
25 | - |
enzyme activity assay at | Solanum tuberosum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | 7 | pH-optimum | Agaricus bisporus |
6 | 6.5 | pH-optimum | Malus domestica |
6 | 6.5 | pH-optimum | Solanum tuberosum |
6.5 | 7 | pH-optimum | Trametes sanguinea |
7 | - |
enzyme activity assay at | Trichoderma reesei |
7 | - |
enzyme activity assay at | Trametes sanguinea |
7 | - |
enzyme activity assay at | Malus domestica |
7 | - |
enzyme activity assay at | Agaricus bisporus |
7 | - |
enzyme activity assay at | Solanum tuberosum |
8 | 9.5 | pH-optimum | Trichoderma reesei |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5 | 8 | active at this pH-range | Trametes sanguinea |
5.5 | 8.5 | active at this pH-range | Solanum tuberosum |
5.5 | 8 | active at this pH-range | Malus domestica |
6 | 10 | active at this pH-range | Trichoderma reesei |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Trametes sanguinea | - |
- |
4.55 |
Agaricus bisporus | - |
- |
4.75 |
Trichoderma reesei | - |
- |
9 |