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Literature summary for 1.14.18.1 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

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 [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

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 (Commentary)

Purification (Comment) Organism
-
Trichoderma reesei
-
Trametes sanguinea

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Agaricus bisporus
-

Substrates and Products (Substrate)

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

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

Synonyms

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 [°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

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 Range

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

pI Value

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