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(+)-catechin hydrate + O2
?
-
-
-
-
?
(-)-catechin + O2
?
-
enzyme activity relative to 4-methylcatechol: 0.77%
-
-
?
(-)-epigallocatechin + O2
?
(-)-epigallocatechin gallate + O2
?
(R)-dopaxanthin + dehydroascorbic acid + O2
(R)-dopaxanthin quinone + L-ascorbic acid + H2O
-
(R)-dopaxanthin is a pigment, the reaction rate on the (R)-isomer of dopaxanthin is 1.9fold lower than that for the (S)-isomer
quantitative product analysis
-
?
(R)-tyrosine-betaxanthin + L-DOPA + O2
(R)-dopaxanthin + dopaquinone + H2O
-
i.e. (R)-portulacaxanthin II, the activity of the enzyme is not restricted to betaxanthins derived from (S)-amino acids
( R)-dopaxanthin is a pigment, quantitative product analysis
-
?
1-butylcatechol + O2
?
-
-
-
-
?
1-tert-butyl-catechol + O2
?
-
-
-
-
?
2 3-methylcatechol + O2
2 3-methyl-1,2-benzoquinone + 2 H2O
-
-
-
?
2 4-methylcatechol + O2
2 4-methyl-1,2-benzoquinone
-
-
-
-
?
2 4-methylcatechol + O2
2 4-methyl-1,2-benzoquinone + 2 H2O
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
2 D-isoproterenol + O2
2 4-[(1S)-1-hydroxy-2-[(propan-2-yl)amino]ethyl]cyclohexa-3,5-diene-1,2-dione + 2 H2O
-
-
-
-
r
2 dopamine + O2
2 4-(2-aminoethyl)-1,2-benzoquinone + 2 H2O
2 o-diphenol + O2
2 o-quinone + 2 H2O
2,3,4-trihydroxybenzoic acid + O2
?
2,3-dihydroxybenzoic acid + O2
?
-
-
-
-
?
2-methylhydroquinone + O2
?
-
low activity
-
-
?
3,4,5-trihydroxy-L-phenylalanine + O2
?
3,4,5-trihydroxybenzoic acid + O2
?
3,4-dihydroxyhydrocinnamic acid + O2
?
-
-
-
-
?
3,4-dihydroxyphenyl acetic acid + O2
?
3,4-dihydroxyphenyl propionic acid + O2
?
3,4-dihydroxyphenylacetic acid + O2
(3,4-dioxocyclohexa-1,5-dien-1-yl)acetic acid + H2O
3,4-dihydroxyphenylacetic acid + O2
?
-
-
-
-
?
3,5-di-tert-butyl catechol + O2
3,5-di-tert-butyl-o-quinone
-
-
-
-
?
3,5-di-tert-butylcatechol + O2
3,5-di-tert-butyl-o-benzoquinone + H2O
3-(3,4-dihydroxyphenyl)-L-alanine + O2
?
-
enzyme activity relative to 4-methylcatechol: 1.15%
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
4-methylcatechol + O2
4-methyl-o-benzoquinone
4-O-caffeoylquinic acid + O2
?
-
-
-
-
?
4-tert-butylcatechol + O2
4-tert-butyl-1,2-benzoquinone + H2O
4-tert-butylcatechol + O2
?
4-[(4-methylbenzol)azo]-1,2-benzenediol + O2
?
-
-
-
-
?
5-caffeoyl quinic acid + O2
?
aminophenol + O2
?
-
-
-
-
?
aniline + O2
?
-
enzyme shows also activity after 24 h incubation
-
-
?
betanidin + O2
betanidin-quinone + H2O
-
the structural unit of the violet betacyanins from Lampranthus productus flowers, the reacion is reversible by ascorbic acid addition at pH 5.0 and 4°C
-
-
?
caffeic acid + 1/2 O2
caffeoyl quinone + H2O
caffeic acid + O2
caffeoyl quinone + H2O
catechol + 1/2 O2
1,2-benzoquinone + H2O
catechol + O2
o-benzoquinone + H2O
-
-
-
-
?
cumaric acid + O2
?
-
-
-
-
?
D-2-methyl-3,4-dihydroxyphenylalanine + O2
2-methyldopaquinone + H2O
-
-
-
-
r
D-dopa + 1/2 O2
D-dopaquinone + H2O
D-isoproterenol + O2
?
-
-
-
-
?
dihydrocaffeic acid + O2
?
-
-
-
-
?
dihydroxyphenylalanine + O2
dihydroxyphenylalanine quinone + H2O
-
-
-
-
?
DL-2-methyl-3,4-dihydroxyphenylalanine + O2
2-methyldopaquinone + H2O
-
the L-isomer is preferred
-
-
?
DL-DOPA + O2
dopaquinone + H2O
dopamine + 1/2 O2
dopamine quinone + H2O
-
-
-
-
?
dopamine + O2
4-(2-aminoethyl)-1,2-benzoquinone + 2 H2O
dopamine + O2
dopaminequinone + H2O
-
-
-
-
?
ferulic acid + O2
?
-
-
-
-
?
guaiacol + O2
?
-
-
-
-
?
hydroquinone + O2
?
-
low activity
-
-
?
L-2-methyl-3,4-dihydroxyphenylalanine + O2
2-methyldopaquinone + H2O
-
-
-
-
r
L-3,4-dihydroxyphenylalanine methyl ester + 1/2 O2
L-dopaquinone methyl ester + H2O
-
-
-
-
?
L-3-hydroxytyrosine + L-dopa + O2
?
L-adrenaline + O2
?
-
-
-
-
?
L-catechin + O2
?
-
-
-
-
?
L-dihydroxyphenylalanine + O2
L-dopaquinone + H2O
-
L-dopa
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
L-dopa + O2
dopachrome + H2O
L-DOPA + O2
dopaquinone + H2O
L-Dopa + O2
L-dopaquinone + H2O
L-noradrenaline + O2
?
-
-
-
-
?
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
L-tyrosine + O2
dihydroxyphenylalanine + H2O
-
-
-
-
?
Luteolin-7-glycoside + O2
?
-
-
-
-
?
myricetin + O2
?
-
-
-
-
?
N-acetyldopamine + O2
?
-
NADA
-
-
?
norepinephrine + O2
?
-
-
-
-
?
p-cresol + O2
?
-
enzyme shows also activity after 24 h incubation
-
-
?
phenol + O2
?
-
enzyme shows also activity after 24 h incubation
-
-
?
phloroglucinol + O2
?
-
-
-
-
?
protocatechuate + O2
?
-
-
-
?
protocatechuic acid + O2
?
rosmarinic acid + O2
?
-
-
-
-
?
shikimic acid + O2
?
-
-
-
-
?
tannic acid + O2
?
-
-
-
-
?
tert-butyl-catechol + O2
?
-
2fold faster reaction rate with the particulate, latent enzyme form compared to the soluble active enzyme
-
-
?
tert-butylcatechol + O2
?
tetramethylbenzidine + O2
?
-
enzyme shows low affinity to this substrate
-
-
?
tyrosol + O2
?
-
enzyme shows also activity after 24 h incubation
-
-
?
verbascosid + O2
?
-
-
-
-
?
additional information
?
-
(+)-catechin + O2
?
Ferula sp.
-
-
-
-
?
(+)-catechin + O2
?
-
-
-
-
?
(+)-catechin + O2
?
-
-
-
-
?
(-)-epicatechin + O2
?
Ferula sp.
-
-
-
-
?
(-)-epicatechin + O2
?
Ferula sp.
-
high activity
-
-
?
(-)-epicatechin + O2
?
-
-
-
-
?
(-)-epicatechin + O2
?
-
-
-
-
?
(-)-epigallocatechin + O2
?
-
-
-
-
?
(-)-epigallocatechin + O2
?
Mycelia sterilia
-
-
-
-
?
(-)-epigallocatechin + O2
?
Mycelia sterilia IBR 35219/2
-
-
-
-
?
(-)-epigallocatechin gallate + O2
?
-
-
-
-
?
(-)-epigallocatechin gallate + O2
?
Mycelia sterilia
-
-
-
-
?
(-)-epigallocatechin gallate + O2
?
Mycelia sterilia IBR 35219/2
-
-
-
-
?
2 4-methylcatechol + O2
2 4-methyl-1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 4-methylcatechol + O2
2 4-methyl-1,2-benzoquinone + 2 H2O
-
best substrate
-
-
?
2 4-methylcatechol + O2
2 4-methyl-1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 4-methylcatechol + O2
2 4-methyl-1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 4-methylcatechol + O2
2 4-methyl-1,2-benzoquinone + 2 H2O
Physalis peruviana Colombian ecotype
-
-
-
-
?
2 4-methylcatechol + O2
2 4-methyl-1,2-benzoquinone + 2 H2O
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
the highest oxidase activity is observed against catechol
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
the highest oxidase activity is observed against catechol
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
enzyme shows high affinity to this substrate
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
enzyme shows highest affinity to this substrate
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
the highest oxidase activity is observed against catechol
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
field bean PPO obeys Michaelis-Menten kinetics and exhibits the phenomenon of inhibition by excess substrate for catechol, 4-methylcatechol and 4-tert-butylcatechol
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
Physalis peruviana Colombian ecotype
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
100% activity with 10 mM substrate concentration
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
enzyme activity relative to 4-methylcatechol: 87%
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
best substrate
-
-
?
2 dopamine + O2
2 4-(2-aminoethyl)-1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 dopamine + O2
2 4-(2-aminoethyl)-1,2-benzoquinone + 2 H2O
-
dopamine is the most specific substrate
-
-
?
2 o-diphenol + O2
2 o-quinone + 2 H2O
-
-
-
?
2 o-diphenol + O2
2 o-quinone + 2 H2O
the reaction depends on molecular oxygen, which is reduced by the copper-containing catalytic domain of the enzyme
-
-
?
2,3,4-trihydroxybenzoic acid + O2
?
-
-
-
?
2,3,4-trihydroxybenzoic acid + O2
?
-
-
-
-
?
3,4,5-trihydroxy-L-phenylalanine + O2
?
-
cytotoxicity of TOPA
-
-
?
3,4,5-trihydroxy-L-phenylalanine + O2
?
-
i.e. TOPA
-
-
?
3,4,5-trihydroxybenzoic acid + O2
?
-
trivial name gallic acid
-
-
?
3,4,5-trihydroxybenzoic acid + O2
?
-
isoenzymes A-C
-
-
?
3,4,5-trihydroxybenzoic acid + O2
?
-
trivial name gallic acid
-
-
?
3,4-dihydroxyphenyl acetic acid + O2
?
-
-
-
-
?
3,4-dihydroxyphenyl acetic acid + O2
?
-
-
-
-
?
3,4-dihydroxyphenyl acetic acid + O2
?
-
-
-
-
?
3,4-dihydroxyphenyl propionic acid + O2
?
-
-
-
-
r
3,4-dihydroxyphenyl propionic acid + O2
?
-
-
-
-
?
3,4-dihydroxyphenylacetic acid + O2
(3,4-dioxocyclohexa-1,5-dien-1-yl)acetic acid + H2O
-
-
-
-
?
3,4-dihydroxyphenylacetic acid + O2
(3,4-dioxocyclohexa-1,5-dien-1-yl)acetic acid + H2O
-
-
-
-
?
3,4-dihydroxyphenylacetic acid + O2
(3,4-dioxocyclohexa-1,5-dien-1-yl)acetic acid + H2O
-
-
-
?
3,5-di-tert-butylcatechol + O2
3,5-di-tert-butyl-o-benzoquinone + H2O
-
mechanism, the rate-determining step is found to change with the substrate to complex ratio, I2+ reacts with DTBCH2, while undergoing a one-electron reduction, leading to the formation of mixed-valence CuIICuIsemiquinone species DTSQ
-
-
?
3,5-di-tert-butylcatechol + O2
3,5-di-tert-butyl-o-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone
-
140% of activity with catechol
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone
-
field bean PPO obeys Michaelis-Menten kinetics and exhibits the phenomenon of inhibition by excess substrate for catechol, 4-methylcatechol and 4-tert-butylcatechol
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
Coffea guarini
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
highest level of enzyme activity in cultivar Violetto di Provenza
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
Ferula sp.
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
208% activity with 10 mM substrate concentration compared to catechol
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-methylcatechol + O2
4-methyl-o-benzoquinone
-
-
-
?
4-methylcatechol + O2
4-methyl-o-benzoquinone
-
-
-
-
?
4-methylcatechol + O2
4-methyl-o-benzoquinone
-
isoenzymes A-D
-
?
4-methylcatechol + O2
?
-
highest activity
-
-
?
4-methylcatechol + O2
?
-
enzyme shows high affinity to this substrate
-
-
?
4-methylcatechol + O2
?
-
enzyme shows highest affinity to this substrate
-
-
?
4-methylcatechol + O2
?
-
-
-
-
?
4-methylcatechol + O2
?
-
-
-
-
?
4-methylcatechol + O2
?
-
enzyme shows highest activity with 4-methylcatechol
-
-
?
4-tert-butylcatechol + O2
4-tert-butyl-1,2-benzoquinone + H2O
-
-
-
-
?
4-tert-butylcatechol + O2
4-tert-butyl-1,2-benzoquinone + H2O
-
-
-
?
4-tert-butylcatechol + O2
4-tert-butyl-1,2-benzoquinone + H2O
-
-
-
?
4-tert-butylcatechol + O2
?
-
-
-
-
?
4-tert-butylcatechol + O2
?
-
field bean PPO obeys Michaelis-Menten kinetics and exhibits the phenomenon of inhibition by excess substrate for catechol, 4-methylcatechol and 4-tert-butylcatechol
-
-
?
5-caffeoyl quinic acid + O2
?
-
i.e. chlorogenic acid
-
-
?
5-caffeoyl quinic acid + O2
?
-
i.e. chlorogenic acid
-
-
?
5-caffeoyl quinic acid + O2
?
-
i.e. chlorogenic acid
-
-
?
5-caffeoyl quinic acid + O2
?
-
i.e. chlorogenic acid
-
-
?
5-caffeoyl quinic acid + O2
?
Coffea guarini
-
i.e. chlorogenic acid
-
-
?
5-caffeoyl quinic acid + O2
?
-
i.e. chlorogenic acid
-
-
?
5-caffeoyl quinic acid + O2
?
-
i.e. chlorogenic acid
-
-
?
5-caffeoyl quinic acid + O2
?
-
i.e. chlorogenic acid
-
-
?
5-caffeoyl quinic acid + O2
?
-
i.e. chlorogenic acid
-
-
?
5-caffeoyl quinic acid + O2
?
-
i.e. chlorogenic acid
-
-
?
5-caffeoyl quinic acid + O2
?
-
i.e. chlorogenic acid
-
-
?
5-caffeoyl quinic acid + O2
?
-
i.e. chlorogenic acid
-
-
?
caffeic acid + 1/2 O2
caffeoyl quinone + H2O
-
-
-
?
caffeic acid + 1/2 O2
caffeoyl quinone + H2O
-
-
-
?
caffeic acid + 1/2 O2
caffeoyl quinone + H2O
-
2% of activity with dopamine
-
-
?
caffeic acid + 1/2 O2
caffeoyl quinone + H2O
-
isoenzymes C and D
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
Coffea guarini
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
?
-
-
-
-
?
caffeic acid + O2
caffeoyl quinone + H2O
-
-
-
-
?
caffeic acid + O2
caffeoyl quinone + H2O
-
-
-
-
?
caffeic acid + O2
caffeoyl quinone + H2O
-
-
-
-
?
caffeic acid + O2
caffeoyl quinone + H2O
-
-
-
-
?
catechin + O2
?
-
-
-
-
?
catechin + O2
?
Ferula sp.
-
-
-
-
?
catechin + O2
?
-
enzyme shows moderate affinity to this substrate
-
-
?
catechin + O2
?
-
-
-
-
?
catechin + O2
?
Mycelia sterilia
-
-
-
-
?
catechin + O2
?
Mycelia sterilia IBR 35219/2
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
no activity with phenol, 4-cresol, L-tyrosine and 4-coumaric acid
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
Coffea guarini
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
Ferula sp.
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
Ferula sp.
-
best substrate
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
no activity with tyrosine, 2-methoxyphenol, 4-hydroxy-3-methoxy-cinnamic acid, hydroquinone and rutin
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
low activity
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
peel enzyme, 34% of activity with dopamine
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
pulp enzyme, 54% of activity with dopamine
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
Mycelia sterilia
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
Mycelia sterilia IBR 35219/2
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
no activity with tyrosine, o-methoxyphenol, p-catechol and m-catechol
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
isoenzymes Ia, Ib and II, 90, 43 and 42% of activity with L-dopa respectively, no activity with L-tyrosine, D-tyrosine, hydroquinone and methylhydroquinone
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
isoenzymes A, B, C and D show no phenolase activity
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
preferred substrate
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + O2
?
-
weak substrate
-
-
?
catechol + O2
?
-
weak substrate
-
-
?
catechol + O2
?
-
-
-
-
?
catechol + O2
?
-
best substrate
-
-
?
catechol + O2
?
-
-
-
-
?
chlorogenic acid + O2
?
-
-
-
-
?
chlorogenic acid + O2
?
-
-
-
-
?
chlorogenic acid + O2
?
-
formation of a highly reactive o-quinone intermediate which then could interact with NH2 groups of lysine, SCH3 groups of methionines and indole rings of tryptophan in nucleophilic addition and in polymerization reactions, the so-called browning and greening reactions
-
-
?
chlorogenic acid + O2
?
-
formation of a highly reactive o-quinone intermediate
-
-
?
chlorogenic acid + O2
?
-
best substrate for both leaf and endosperm enzyme
-
-
?
chlorogenic acid + O2
?
-
probably the major substrate in vivo
-
-
?
chlorogenic acid + O2
?
-
highest level of enzyme activity in cultivars Tema 2000 and Violetto di Sicilia
-
-
?
chlorogenic acid + O2
?
Ferula sp.
-
-
-
-
?
chlorogenic acid + O2
?
-
-
-
-
?
chlorogenic acid + O2
?
-
-
-
-
?
chlorogenic acid + O2
?
-
preferred substrate
-
-
?
chlorogenic acid + O2
?
-
-
-
-
?
chlorogenic acid + O2
?
-
peel enzyme, 5.3% of activity with dopamine
-
-
?
chlorogenic acid + O2
?
-
pulp enzyme, 24.5% of activity with dopamine
-
-
?
chlorogenic acid + O2
?
-
-
-
-
?
chlorogenic acid + O2
?
-
50% of activity with catechol
-
-
?
chlorogenic acid + O2
?
-
best substrate
-
-
?
chlorogenic acid + O2
?
Physalis peruviana Colombian ecotype
-
best substrate
-
-
?
chlorogenic acid + O2
?
-
isoenzymes A-D
-
-
?
chlorogenic acid + O2
?
-
preferred substrate, 50fold faster reaction rate with the particulate, latent enzyme form compared to the soluble active enzyme
-
-
?
chlorogenic acid + O2
?
-
-
-
-
?
chlorogenic acid + O2
?
-
enzyme activity relative to 4-methylcatechol: 6.15%
-
-
?
coumaric acid + O2
?
Coffea guarini
-
-
-
-
?
coumaric acid + O2
?
-
-
-
-
?
D-catechin + O2
?
-
-
-
-
?
D-catechin + O2
?
-
-
-
-
?
D-catechin + O2
?
-
best substrate
-
-
?
D-catechin + O2
?
-
pulp enzyme, 35.6% of activity with dopamine
-
-
?
D-catechin + O2
?
-
peel enzyme, 11.5% of activity with dopamine
-
-
?
D-catechin + O2
?
-
isoenzymes A-D
-
-
?
D-dopa + 1/2 O2
D-dopaquinone + H2O
-
-
-
-
?
D-dopa + 1/2 O2
D-dopaquinone + H2O
-
-
-
-
?
D-dopa + 1/2 O2
D-dopaquinone + H2O
-
-
-
-
?
D-dopa + 1/2 O2
D-dopaquinone + H2O
-
isoenzymes Ia, Ib and II, 54, 60 and 48% of activity with L-dopa respectively
-
?
D-dopa + 1/2 O2
D-dopaquinone + H2O
-
-
-
-
?
DL-DOPA + O2
dopaquinone + H2O
-
i.e. DL-3,4-dihydroxyphenylalanine, the L-isomer is preferred
-
-
?
DL-DOPA + O2
dopaquinone + H2O
-
-
-
-
?
DL-DOPA + O2
dopaquinone + H2O
-
i.e. DL-3,4-dihydroxyphenylalanine, the L-isomer is preferred
-
-
?
DL-DOPA + O2
dopaquinone + H2O
-
i.e. DL-3,4-dihydroxyphenylalanine, the L-isomer is preferred
-
-
?
DL-isoproterenol + O2
?
-
the L-isomer is preferred
-
-
?
DL-isoproterenol + O2
?
-
the L-isomer is preferred
-
-
?
dopamine + O2
4-(2-aminoethyl)-1,2-benzoquinone + 2 H2O
-
-
-
?
dopamine + O2
4-(2-aminoethyl)-1,2-benzoquinone + 2 H2O
-
-
-
?
dopamine + O2
4-(2-aminoethyl)-1,2-benzoquinone + 2 H2O
-
-
-
?
dopamine + O2
4-(2-aminoethyl)-1,2-benzoquinone + 2 H2O
-
isoenzymes A-D
-
?
dopamine + O2
?
-
-
-
-
?
dopamine + O2
?
-
-
-
-
?
dopamine + O2
?
Ferula sp.
-
low activity
-
-
?
dopamine + O2
?
-
enzyme shows moderate affinity to this substrate
-
-
?
dopamine + O2
?
-
-
-
-
?
dopamine + O2
?
-
-
-
-
?
dopamine + O2
?
-
-
-
-
?
dopamine + O2
?
-
-
-
-
?
dopamine + O2
?
-
-
-
-
?
epicatechin + O2
?
-
peel enzyme, 9.3% of activity with dopamine
-
-
?
epicatechin + O2
?
-
pulp enzyme, 22.7% of activity with dopamine
-
-
?
epicatechin + O2
?
-
-
-
-
?
epinephrine + O2
?
-
-
-
-
?
epinephrine + O2
?
-
-
-
-
?
gallic acid + O2
?
Ferula sp.
-
low activity
-
-
?
gallic acid + O2
?
-
enzyme shows very low affinity to this substrate
-
-
?
hydroxyquinone + O2
?
Coffea guarini
-
-
-
-
?
hydroxyquinone + O2
?
-
-
-
-
?
L-3-hydroxytyrosine + L-dopa + O2
?
-
-
-
-
?
L-3-hydroxytyrosine + L-dopa + O2
?
-
-
-
-
?
L-3-hydroxytyrosine + L-dopa + O2
?
-
-
-
-
?
L-3-hydroxytyrosine + L-dopa + O2
?
Coffea guarini
-
-
-
-
?
L-3-hydroxytyrosine + L-dopa + O2
?
-
-
-
-
?
L-3-hydroxytyrosine + L-dopa + O2
?
-
-
-
-
?
L-3-hydroxytyrosine + L-dopa + O2
?
-
-
-
-
?
L-3-hydroxytyrosine + L-dopa + O2
?
-
-
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
-
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
-
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
-
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
endosperm enzyme, 3.9% of activity with chlorogenic acid
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
Coffea guarini
-
i.e. L-3,4-dihydroxyphenylalanine
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
i.e. L-3,4-dihydroxyphenylalanine
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
i.e. L-3,4-dihydroxyphenylalanine
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
-
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
22.65 of activity with catechol
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
i.e. L-3,4-dihydroxyphenylalanine, low activity
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
peel enzyme, 8.0% of activity with dopamine
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
pulp enzyme, 12.3% of activity with dopamine
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
-
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
isoenzymes A-D
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
i.e. L-3,4-dihydroxyphenylalanine
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
no activity with tyrosine, p-methoxyphenol and catechol
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
low activity with the D-isomer, 18% of the activity with the L-isomer
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
i.e. L-3,4-dihydroxyphenylalanine
-
-
?
L-DOPA + O2
?
-
-
-
-
?
L-DOPA + O2
?
Ferula sp.
-
low activity
-
-
?
L-dopa + O2
dopachrome + H2O
-
-
-
-
?
L-dopa + O2
dopachrome + H2O
-
-
-
-
?
L-DOPA + O2
dopaquinone + H2O
-
-
-
-
?
L-DOPA + O2
dopaquinone + H2O
-
-
-
-
?
L-Dopa + O2
L-dopaquinone + H2O
-
specific substrate
-
-
?
L-Dopa + O2
L-dopaquinone + H2O
-
-
-
-
?
L-Dopa + O2
L-dopaquinone + H2O
-
-
-
-
?
L-Dopa + O2
L-dopaquinone + H2O
-
-
-
-
?
L-Dopa + O2
L-dopaquinone + H2O
-
-
-
-
?
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
-
-
o-dopaquinone is unstable in aqueous solution and rapidly suffers a non-enzymatic cyclization to leukodopachrome
-
?
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
-
-
o-dopaquinone is unstable in aqueous solution and rapidly suffers a non-enzymatic cyclization to leukodopachrome
-
?
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
-
-
o-dopaquinone is unstable in aqueous solution and rapidly suffers a non-enzymatic cyclization to leukodopachrome
-
?
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
-
pathway of melanin biosynthesis, detailed overview
cytotoxicity of L-DOPA
-
?
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
-
-
-
-
?
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
-
-
o-dopaquinone is unstable in aqueous solution and rapidly suffers a non-enzymatic cyclization to leukodopachrome
-
?
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
-
-
-
-
?
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
-
-
o-dopaquinone is unstable in aqueous solution and rapidly suffers a non-enzymatic cyclization to leukodopachrome
-
?
p-hydroquinone + O2
?
-
-
-
-
?
p-hydroquinone + O2
?
-
-
-
-
?
p-hydroquinone + O2
?
-
-
-
-
?
protocatechuic acid + O2
?
-
isoenzyme C
-
-
?
protocatechuic acid + O2
?
-
-
-
-
?
pyrocatechol + O2
?
-
-
-
-
?
pyrocatechol + O2
?
-
-
-
-
?
pyrocatechol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
Ferula sp.
-
low activity
-
-
?
pyrogallol + O2
?
-
enzyme shows low affinity to this substrate
-
-
?
pyrogallol + O2
?
-
24% of activity with catechol
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
pulp enzyme, 5.5% of activity with dopamine
-
-
?
pyrogallol + O2
?
-
peel enzyme, 1.4% of activity with dopamine
-
-
?
pyrogallol + O2
?
Mycelia sterilia
-
-
-
-
?
pyrogallol + O2
?
Mycelia sterilia IBR 35219/2
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
isoenzymes Ia, Ib and II, 5, 8 and 15% of activity with L-dopa respectively
-
-
?
pyrogallol + O2
?
-
746% activity with 10 mM substrate concentration compared to catechol
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
-
-
-
?
pyrogallol + O2
?
-
low activity
-
-
?
pyrogallol + O2
?
-
enzyme activity relative to 4-methylcatechol: 9.24%
-
-
?
quercetin + O2
?
-
-
-
-
?
quercetin + O2
?
-
-
-
-
?
tert-butylcatechol + O2
?
-
-
-
-
?
tert-butylcatechol + O2
?
-
-
-
-
?
additional information
?
-
-
role of the enzyme in the biosynthetic scheme of betalains, overview
-
-
?
additional information
?
-
-
betanidin is a labile compound, overview
-
-
?
additional information
?
-
-
multifunctional enzyme
-
-
?
additional information
?
-
-
multifunctional enzyme
-
-
?
additional information
?
-
-
stereospecificity, and monophenolase and diphenolase activities and specificities dependent on conditions, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
tyrosinase is a copper-containing enzyme that catalyzes two distinct reactions of melanin synthesis: the hydroxylation of tyrosine by monophenolase action and the oxidation of 3,4-dihydroxyphenylalanine (L-DOPA) to o-dopaquinone by diphenolase action
-
-
?
additional information
?
-
-
the enzyme fails to oxidize hydroquinone, phenol, or tyrosine
-
-
?
additional information
?
-
-
to investigate the substrate specificity of activated hemocyanin, the turnover of several diphenols is compared using an oxygen electrode
-
-
?
additional information
?
-
-
no activity is detected against L-tyrosine and common laccase substrates such as 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) and syringaldazine with the exception of weak activity with p-hydroquinone
-
-
?
additional information
?
-
-
the enzyme catalyses two different reactions, each using molecular oxygen: the hydroxylation of monophenols to o-diphenols, monophenolase activity, and the oxidation of o-diphenols to o-quinones, diphenolase, overview
-
-
?
additional information
?
-
-
tyrosinase is a copper-containing enzyme that catalyzes two distinct reactions of melanin synthesis: the hydroxylation of tyrosine by monophenolase action and the oxidation of 3,4-dihydroxyphenylalanine (L-DOPA) to o-dopaquinone by diphenolase action
-
-
?
additional information
?
-
-
extremely low levels of activity suggest that this protein likely plays no direct metabolic role in the biodegradation of catecholamines
-
-
?
additional information
?
-
-
no activity is detected against L-tyrosine and common laccase substrates such as 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) and syringaldazine with the exception of weak activity with p-hydroquinone
-
-
?
additional information
?
-
-
no activity with L-tyrosine
-
-
?
additional information
?
-
-
protocatechuic acid (3,4-dihydroxybenzoic acid) shows little or no activity as a sole substrate
-
-
?
additional information
?
-
-
no activity with L-tyrosine
-
-
?
additional information
?
-
-
protocatechuic acid (3,4-dihydroxybenzoic acid) shows little or no activity as a sole substrate
-
-
?
additional information
?
-
-
no activity with p-cresol or L-Tyr
-
-
?
additional information
?
-
-
assay method optimization, overview
-
-
?
additional information
?
-
-
the enzyme shows minimal activity toward monophenol compounds such as tyramine, tyrosine and tyrosine methyl ester
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
Coffea guarini
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
Coffea guarini
-
substrate specificity, overview, the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
no activity detected with L-Tyr, resorcinol and p-cresol
-
-
?
additional information
?
-
-
this enzyme is an o-diphenol oxidase, and no cresolase activity has been found
-
-
?
additional information
?
-
-
L-tyrosine and hydroquinone are ineffective as substrates
-
-
?
additional information
?
-
Ferula sp.
-
polyphenol oxidase is a major enzyme responsible for the browning reaction in damaged plant tissues and fruits
-
-
?
additional information
?
-
Ferula sp.
-
substrate specificity, overview, no activity with L-tyrosine
-
-
?
additional information
?
-
-
PPO oxidizes o-diphenolic compounds to the corresponding o-quinones in the presence of oxygen, subsequently the o-quinones polymerize with other o-quinones, proteins, amino acids etc., resulting in the formation of brown complexes, the enzyme is one of the main enzymes responsible for quality loss in strawberry taste due to phenolic degradation
-
-
?
additional information
?
-
-
PPO oxidizes o-diphenolic compounds to the corresponding o-quinones in the presence of oxygen
-
-
?
additional information
?
-
-
PPO shows activity with biphenols, triphenol but not with monophenols
-
-
?
additional information
?
-
-
tyrosinase is known to be a key enzyme in melanin biosynthesis, involved in determining the color of mammalian skin and hair, various dermatological disorders, such as melasma, age spots and sites of actinic damage, arise from the accumulation of an excessive level of epidermal pigmentation
-
-
?
additional information
?
-
-
tyrosinase is a copper-containing enzyme that catalyzes two distinct reactions of melanin synthesis: the hydroxylation of tyrosine by monophenolase action and the oxidation of 3,4-dihydroxyphenylalanine (L-DOPA) to o-dopaquinone by diphenolase action
-
-
?
additional information
?
-
-
no activity is detected against L-tyrosine and common laccase substrates such as 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) and syringaldazine with the exception of weak activity with p-hydroquinone
-
-
?
additional information
?
-
-
reduction of dioxygen to dihydrogen peroxide upon catechol oxidation by copper(II) complexes, overview, dioxygen undergoes a two-electron reduction to dihydrogen peroxide, and a second mechanism in which it is converted into water upon four-electron reduction, catecholase activity of a tetranuclear carbonato-bridged copper(II) cluster with the macrocyclic ligand 9,22-dipropyl-1,4,9,14,17,22,27,28,29,30-decaazapentacyclotriacontane-5,7(28),11(29),12,18,20(30),24(27),25-octaene, ferromagnetic interaction between the two copper ions within one macrocyclic ring, and a weak antiferromagnetic interaction between the two neighboring copper ions of two different macrocyclic units, solution stability, electrochemical properties, and crystal structure of (I)2(CF3SO3)4 - 2CH3CN- 4H2O, detailed overview, mechanisms versus a coordination mode of the substrate
-
-
?
additional information
?
-
pyragallol is not oxidized by ibCO
-
-
?
additional information
?
-
-
the enzyme is considered as defence oxidative enzyme, is vital the physiological defence strategy adapted by plants to insect herbivory and pathogen attack
-
-
?
additional information
?
-
-
the enzyme shows catecholase and cresolase activities, a type III copper protein that catalyses the O-hydroxylation of monophenols and oxidation of O-diphenols using molecular oxygen
-
-
?
additional information
?
-
-
polyphenol oxidase shows no activity with L-tyrosine, digallol, gallic acid, and methyl gallate
-
-
?
additional information
?
-
-
the enzyme catalyzes the oxidation of o-phenolic substrates to o-quinones, which are subsequently polymerized to dark-coloured pigments. Polyphenoloxidase is considered to be the main contributor to browning discolouration and darkening in fruits and vegetables
-
-
?
additional information
?
-
-
substrate specificity of the purified enzyme, overview, highest PPO activity occurs with 4-methylcatechol, followed by catechol, pyrogallol, (-)-epicatechin, caffeic acid, and DL-dopa, little or no activity is detected toward the monophenolic compounds ferulic acid, L-tyrosine, and phenol
-
-
?
additional information
?
-
-
the putative substrate-binding pocket contains six polar or charged amino acids, His191, His221, Trp224, Trp228, Phe227, and Val190. Trp224 and Trp228 form hydrogen bonds with 4-methylcatechol. Molecular docking of optimum substrate of mPPO, 4-methylcatechol, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, no activity with hydroquinic acid, resorcinol, and tyrosine
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
no activity towards the monophenols p-cresol or L-Tyr
-
-
?
additional information
?
-
-
the enzyme plays a role in enzymatic browning, rapid discolouration of leaf, stem and root tissue after injury and strong pigmentation of tissue extracts, PPO and phenolic compounds could be an important part of the plants defence system against pests and diseases, including root parasitic nematodes, e.g. Radopholus similis
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
tyrosinase is a copper-containing enzyme that catalyzes two distinct reactions of melanin synthesis: the hydroxylation of tyrosine by monophenolase action and the oxidation of 3,4-dihydroxyphenylalanine (L-DOPA) to o-dopaquinone by diphenolase action
-
-
?
additional information
?
-
-
PPO II inhibits cultures of Escherichia coli and it accumulates on the wounded sites of tobacco leaves indicating that it may act as a defense role in plat defense system
-
-
?
additional information
?
-
-
no activity with tyrosine, o-methoxyphenol, p-diphenol and m-diphenol
-
-
?
additional information
?
-
-
PPO activity increases in the transition from the vegetative stage to the generative stage
-
-
?
additional information
?
-
-
phenoloxidase activity is not observed when tyramine and tyrosine (monophenols) were used as substrates
-
-
?
additional information
?
-
-
the specificity of PPO toward chlorogenic acid is approximately 7 times greater than that for 4-methylcatechol and 370 times greater than that for catechol. No activity with L-tyrosine. The Cape gooseberry PPO lacks monophenolase (cresolase) activity, EC 1.14.18.1
-
-
?
additional information
?
-
Physalis peruviana Colombian ecotype
-
the specificity of PPO toward chlorogenic acid is approximately 7 times greater than that for 4-methylcatechol and 370 times greater than that for catechol. No activity with L-tyrosine. The Cape gooseberry PPO lacks monophenolase (cresolase) activity, EC 1.14.18.1
-
-
?
additional information
?
-
-
the enzyme shows no activity towards caffeic acid, DL-Dopa, ferulic acid and phenol
-
-
?
additional information
?
-
-
expressionlevels of polyphenol oxidase activity exhibiting enzymes in the organism, overview
-
-
?
additional information
?
-
-
oxidation of this and other o-diphenols to o-quinones
-
-
?
additional information
?
-
-
substrate specificity of the soluble and particulate enzyme forms, overview
-
-
?
additional information
?
-
-
the purified tyrosinase from hemolymph shows both monophenolase, EC 1.14.18.1, and diphenolase, EC 1.10.3.1, activity and therefore it can be defined as a true tyrosinase, the purified hemocynin does not show any tyrosinase activity
-
-
?
additional information
?
-
-
PPO activity is associated with color changes associated with browning and lycopene degradation, the commercial variety Naomi is more susceptible to enzymatic browning than the local varieties Pizzutello, Rosa Maletto and PO228, due to higher PPO activity levels, lycopene is an antioxidant agent that reconstitutes the polyphenols oxidized by the action of PPO
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview
-
-
?
additional information
?
-
-
tyrosinase is a copper-containing enzyme that catalyzes two distinct reactions of melanin synthesis: the hydroxylation of tyrosine by monophenolase action and the oxidation of 3,4-dihydroxyphenylalanine (L-DOPA) to o-dopaquinone by diphenolase action
-
-
?
additional information
?
-
the enzyme catalyzes the oxidation of ortho-diphenols to the corresponding quinones
-
-
?
additional information
?
-
-
the enzyme catalyzes the oxidation of ortho-diphenols to the corresponding quinones
-
-
?
additional information
?
-
-
broad substrate specificity, overview, tyrosinase is a mono-oxygenase and a bifunctional enzyme that catalyzes the o-hydroxylation of monophenols and subsequent oxidation of o-diphenols to quinones, the enzyme thus accepts monophenols and diphenols as substrates, and the monophenolase activity is the initial rate-determining reaction
-
-
?
additional information
?
-
-
substrate specificity, overview, activity with phenolic and diphenolic substrates, also performing the reaction of tyrosinase, a ortho-hydroxylation of monophenols, EC 1.14.18.1, and the oxidation of catechols to ortho-quinones, the diphenolase activity, EC 1.10.3.1, overview
-
-
?
additional information
?
-
tyrosine is not a substrate
-
-
?
additional information
?
-
-
tyrosine is not a substrate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(+)-catechin + O2
?
Ferula sp.
-
-
-
-
?
(-)-epicatechin + O2
?
Ferula sp.
-
-
-
-
?
2 4-methylcatechol + O2
2 4-methyl-1,2-benzoquinone + 2 H2O
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
2 o-diphenol + O2
2 o-quinone + 2 H2O
-
-
-
?
3,4,5-trihydroxy-L-phenylalanine + O2
?
-
cytotoxicity of TOPA
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
Ferula sp.
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
D-catechin + O2
?
-
-
-
-
?
dihydroxyphenylalanine + O2
dihydroxyphenylalanine quinone + H2O
-
-
-
-
?
dopamine + O2
?
-
-
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
L-tyrosine + O2
dihydroxyphenylalanine + H2O
-
-
-
-
?
additional information
?
-
2 4-methylcatechol + O2
2 4-methyl-1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 4-methylcatechol + O2
2 4-methyl-1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 4-methylcatechol + O2
2 4-methyl-1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 4-methylcatechol + O2
2 4-methyl-1,2-benzoquinone + 2 H2O
Physalis peruviana Colombian ecotype
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
Physalis peruviana Colombian ecotype
-
-
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
Ferula sp.
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
-
-
-
?
chlorogenic acid + O2
?
-
formation of a highly reactive o-quinone intermediate which then could interact with NH2 groups of lysine, SCH3 groups of methionines and indole rings of tryptophan in nucleophilic addition and in polymerization reactions, the so-called browning and greening reactions
-
-
?
chlorogenic acid + O2
?
-
probably the major substrate in vivo
-
-
?
chlorogenic acid + O2
?
Ferula sp.
-
-
-
-
?
chlorogenic acid + O2
?
-
best substrate
-
-
?
chlorogenic acid + O2
?
Physalis peruviana Colombian ecotype
-
best substrate
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
-
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
-
-
-
-
?
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
-
-
-
-
?
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
-
-
-
-
?
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
-
pathway of melanin biosynthesis, detailed overview
cytotoxicity of L-DOPA
-
?
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
-
-
-
-
?
L-tyrosine + L-dopa + O2
L-dopa + dopaquinone + H2O
-
-
-
-
?
additional information
?
-
-
role of the enzyme in the biosynthetic scheme of betalains, overview
-
-
?
additional information
?
-
-
extremely low levels of activity suggest that this protein likely plays no direct metabolic role in the biodegradation of catecholamines
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
Coffea guarini
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
-
mechanical damage by Hemileia vastatrix fungus, the causal agent of the leaf orange rust disease, inoculation and Leucoptera coffeella, the coffee leaf miner, infestation caused different responses in PPO activity in different Coffea species, level of damage or resistance, overview
-
-
?
additional information
?
-
Ferula sp.
-
polyphenol oxidase is a major enzyme responsible for the browning reaction in damaged plant tissues and fruits
-
-
?
additional information
?
-
-
PPO oxidizes o-diphenolic compounds to the corresponding o-quinones in the presence of oxygen, subsequently the o-quinones polymerize with other o-quinones, proteins, amino acids etc., resulting in the formation of brown complexes, the enzyme is one of the main enzymes responsible for quality loss in strawberry taste due to phenolic degradation
-
-
?
additional information
?
-
-
tyrosinase is known to be a key enzyme in melanin biosynthesis, involved in determining the color of mammalian skin and hair, various dermatological disorders, such as melasma, age spots and sites of actinic damage, arise from the accumulation of an excessive level of epidermal pigmentation
-
-
?
additional information
?
-
-
the enzyme is considered as defence oxidative enzyme, is vital the physiological defence strategy adapted by plants to insect herbivory and pathogen attack
-
-
?
additional information
?
-
-
the enzyme catalyzes the oxidation of o-phenolic substrates to o-quinones, which are subsequently polymerized to dark-coloured pigments. Polyphenoloxidase is considered to be the main contributor to browning discolouration and darkening in fruits and vegetables
-
-
?
additional information
?
-
-
the enzyme plays a role in enzymatic browning, rapid discolouration of leaf, stem and root tissue after injury and strong pigmentation of tissue extracts, PPO and phenolic compounds could be an important part of the plants defence system against pests and diseases, including root parasitic nematodes, e.g. Radopholus similis
-
-
?
additional information
?
-
-
PPO II inhibits cultures of Escherichia coli and it accumulates on the wounded sites of tobacco leaves indicating that it may act as a defense role in plat defense system
-
-
?
additional information
?
-
-
PPO activity increases in the transition from the vegetative stage to the generative stage
-
-
?
additional information
?
-
-
expressionlevels of polyphenol oxidase activity exhibiting enzymes in the organism, overview
-
-
?
additional information
?
-
-
PPO activity is associated with color changes associated with browning and lycopene degradation, the commercial variety Naomi is more susceptible to enzymatic browning than the local varieties Pizzutello, Rosa Maletto and PO228, due to higher PPO activity levels, lycopene is an antioxidant agent that reconstitutes the polyphenols oxidized by the action of PPO
-
-
?
additional information
?
-
the enzyme catalyzes the oxidation of ortho-diphenols to the corresponding quinones
-
-
?
additional information
?
-
-
the enzyme catalyzes the oxidation of ortho-diphenols to the corresponding quinones
-
-
?
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(-)-epigallocatechin-3-O-gallate
1-ethyl-3-(3-dimethylaminopropyl) carbodiimide
-
irreversible inactivation, second-order rate constants
2,3-Dihydroxybenzoic acid
2,4-dihydroxy-N-(3,4,5-trihydroxybenzyl)benzamide
-
IC50: 0.550 mM
2,4-dihydroxy-N-(4-hydroxybenzyl)benzamide
-
IC50: 1.820 mM
2-hydroxy-2,4,6-cycloheptatrien-1-one
2-mercaptobenzothiazole
-
1 mM, 94% inhibition
2-methyl-4-[(E)-(4-nitrophenyl)methylidene]-1,3-oxazol-5(4H)-one
-
IC50: 0.00351 mM
2-methyl-4-[(E)-2-thienylmethylidene]-1,3-oxazol-5-one
-
IC50: 0.00311 mM
2-methyl-4-[(E,2Z)-3-phenyl-2-propenyliden]-1,3-oxazol-5(4H)-one
-
IC50: 0.00123 mM
3,4,5-trihydroxy-N-(3,4,5-trihydroxybenzyl)benzamide
-
IC50: 0.555 mM
3,4,5-trihydroxy-N-(4-hydroxybenzyl)benzamide
-
IC50: 1.180 mM
3,4,5-Trihydroxybenzoic acid
3,4-dihydroxy-N-(3,4,5-trihydroxybenzyl)benzamide
-
IC50: 0.280 mM
3,4-dihydroxy-N-(4-hydroxybenzyl)benzamide
-
IC50: 2.0 mM
3,4-dihydroxybenzoic acid
3,5-dihydroxy-N-(3,4,5-trihydroxybenzyl)benzamide
-
IC50: 0.705 mM
3,5-dihydroxy-N-(4-hydroxybenzyl)benzamide
-
IC50: 0.710 mM
3-(acetoyloxy)-2-hydroxy-4-[[5-oxo-2-phenyl-1,3-oxazol-4(5H)-ylidene]methyl]phenylacetate
-
IC50: 0.00215 mM
3-aminophenyl-2,2'-methylenebis-(5,5-dimethylcyclohexane-1,3-dione)
-
IC50: 0.0021 mM
3-aminophenyl-2,2'-methylenebis-(cyclohexane-1,3-dione)
-
IC50: 0.00219 mM
3-chlorophenyl-2,2'-methylenebis-(5,5-dimethylcyclohexane-1,3-dione)
-
IC50: 0.0032 mM
4-chloromercuribenzoate
-
1 mM, 96, 94 and 95% inhibition of isoenzymes Ia, Ib and II respectively
4-hydroxybenzoic acid
-
-
4-methylcatechol
-
field bean PPO obeys Michaelis-Menten kinetics and exhibits the phenomenon of inhibition by excess substrate for catechol, 4-methylcatechol and 4-tert-butylcatechol
4-tert-butylcatechol
-
field bean PPO obeys Michaelis-Menten kinetics and exhibits the phenomenon of inhibition by excess substrate for catechol, 4-methylcatechol and 4-tert-butylcatechol
4-[(E)-(4-nitrophenyl)methylidene]-2-phenyl-1,3-oxazol-5(4H)-one
-
IC50: 0.00323 mM
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
Ag+
-
1 mM, 60% inhibition
Al3+
-
1 mM, 89% inhibition
askendoside B
-
IC50 : 0.014 mM
azide
-
typical inhibitors of catecholoxidase, also inhibit the phenoloxidase activity of activated hemocyanin
Ba2+
-
moderately inhibits PPO
citral
-
noncompetitive inhibitor
cucurbitane glycosides
-
isolated from Bryonia, structureactivity relationships, overview
-
cycloartane glycosides
-
isolated from Astragalus sp., structureactivity relationships, overview
-
D-fructose
-
D-fructose at different concentrations, PPO activities are measured at 25°C and pH 7.0 to determine inhibitor effects of sugars on enzymatic activities. PPO activities from both cultivars show a decreasing pattern as sugar concentration in the assay medium increases
D-glucose
-
D-glucose at different concentrations, PPO activities are measured at 25°C and pH 7.0 to determine inhibitor effects of sugars on enzymatic activities. PPO activities from both cultivars show a decreasing pattern as sugar concentration in the assay medium increases
decahydro-2-naphthyl gallate
diethyldithiocarbamic acid
-
-
DL-dithiothreitol
-
competitive with 4-methylcatechol, catechol or pyrogallol. IC50: 0.147 mM in reaction with 4-methylcatechol, IC50: 0.0329 mM in reaction with pyrogallol, IC50: 0.135 mM in reaction with catechol
epigallocatechin-3-O-gallate
-
-
Fe2+
-
88%, 68% and 80% inhibition of isoenzymes Ia, Ib, and II, respectively
FeCl3
-
markedly inhibits PPO
gallocatechin gallate
-
-
geranyl acetate
-
slight inhibition
glycine methyl ester hydrochloride
-
irreversible inactivation, second-order rate constants
GSH
-
increasing the concentration from 0 to 300 mM results in a high inhibitory effect on enzyme activity, mostly due to a drop of pH of the reaction solution to acidic values. Upon heating GSH at 90°C, thermal degradation product formation is responsible for a partial inhibition. GSH-derived Maillard reaction products highly inhibit enzyme activity, inhibition efficiency increasing with heating time, 2-39 h and temperature, 80-100 °C
hexadecyltrimethyl-ammonium bromide
-
-
Hg2+
-
1 mM, 84% inhibition
iodoacetate
-
1 mM; 1 mM: 46%, 39% and 31% inhibition of isoenzymes Ia, Ib, and II, respectively
L-Cys
-
competitive with 4-methylcatechol, catechol or pyrogallol. IC50: 0.125 mM in reaction with 4-methylcatechol, IC50: 0.637 mM in reaction with pyrogallol, IC50: 0.15 mM in reaction with catechol
Maillard reaction products
-
potential natural inhibitors for use with minimally processed fruits
-
meta-bisulfite
complete inhibition at 0.2 mM, 76% inhibition at 0.02 mM
mimosine
-
1 mM, 88%, 79% and 82% inhibition of isoenzymes Ia, Ib, and II, respectively
Mn2+
-
inhibits activity at 0.01 mM
myrcene
-
competitive inhibitor
N,N-diethyldithiocarbamate
-
94.4% inhibition at 0.0293 mM
N-(2,4-dihydroxybenzyl)-2,4-dihydroxybenzamide
-
IC50: 0.029 mM
N-(2,4-dihydroxybenzyl)-3,4,5-trihydroxybenzamide
-
IC50: 0.017 mM
N-(2,4-dihydroxybenzyl)-3,4-dihydroxybenzamide
-
IC50: 0.011 mM
N-(2,4-dihydroxybenzyl)-3,5-dihydroxybenzamide
-
IC50: 0.0022 mM
N-benzyl-2,4-dihydroxybenzamide
-
IC50: 1.660 mM
N-benzyl-3,4,5-trihydroxybenzamide
-
IC50: 0.780 mM
N-benzyl-3,4-dihydroxybenzamide
-
IC50: 2.0 mM
N-benzyl-3,5-dihydroxybenzamide
-
IC50: 0.700 mM
N-benzylamide
-
IC50: 1.990 mM
N-benzylbenzamide derivatives
-
inhibitory potency, structure-activity relationships, overview
-
naphthol
-
strong inhibition of the reaction with catechol
neryl acetate
-
slight inhibition
orcinol
-
strong inhibition of the reaction with catechol
p-aminobenzenesulfonamide
-
-
p-nitrophenol
-
strong inhibition of the reaction with catechol
papain
-
proteolytic inactivation
-
phenyl-2,2'-methylenebis-(5,5-dimethylcyclohexane-1,3-dione)
-
IC50: 0.0026 mM
polyvinylpyrrolidone 40
-
-
-
procyanidin
-
inhibition intensity increases with NAD+. The inhibitory effect of oxidized procyanidins is twice that of native procyanidins
resorcinol
-
10 mM, 40% inhibition
Sabinene
-
slight inhibition
Salicylhydroxamic acid
-
-
salicylic acid
-
uncompetitive
Sn2+
-
1 mM, 99% inhibition
SnCl2
-
markedly inhibits PPO
Sodium bisulfite
-
1 mM, 97% inhibition
Sodium cyanide
-
noncompetitive
Sodium diethyl dithiocarbamate
succinic acid
-
complete inhibition at 1 mM
sulfonamide compounds
-
-
-
tyramine
-
typical inhibitors of catecholoxidase, also inhibit the phenoloxidase activity of activated hemocyanin
Xanthogenate
-
1 mM, 94% inhibition
(-)-epigallocatechin
-
-
(-)-epigallocatechin-3-O-gallate
-
-
(-)-epigallocatechin-3-O-gallate
-
-
(-)-epigallocatechin-3-O-gallate
-
-
(-)-epigallocatechin-3-O-gallate
-
-
(-)-epigallocatechin-3-O-gallate
-
-
(R)-HTCCA
-
-
(S)-HTCCA
-
-
1-Phenyl-2-thiourea
-
-
1-Phenyl-2-thiourea
-
complete inhibition at 5 mM
1-Phenyl-2-thiourea
-
94.4% inhibition at 0.0293 mM
2,3-Dihydroxybenzoic acid
-
2,3-Dihydroxybenzoic acid
-
-
2-hydroxy-2,4,6-cycloheptatrien-1-one
-
trivial name tropolone
2-hydroxy-2,4,6-cycloheptatrien-1-one
-
1 mM, complete inhibition of isoenzymes Ia, Ib and II
2-mercaptoethanol
-
1 mM, 97% inhibition
2-mercaptoethanol
Ferula sp.
-
competitive
2-mercaptoethanol
complete inhibition at 0.02 mM
2-mercaptoethanol
-
competitive
3,4,5-Trihydroxybenzoic acid
-
3,4,5-Trihydroxybenzoic acid
-
-
3,4-dihydroxybenzoic acid
-
3,4-dihydroxybenzoic acid
-
-
4-hexylresorcinol
-
-
aloesin
-
-
Anisaldehyde
-
noncompetitive, IC50: 0.320 mM
Anisaldehyde
-
noncompetitive, IC50: 0.320 mM
Anisaldehyde
-
noncompetitive, IC50: 0.320 mM
Anisaldehyde
-
noncompetitive, IC50: 0.320 mM
Anisaldehyde
-
noncompetitive, IC50: 0.320 mM
ascorbate
complete inhibition at 2 mM, 94% inhibition at 0.2 mM
ascorbic acid
-
endogenous ascorbic acid prevents betanidin oxidation, the effect of ascorbic acid on the tyrosinase-mediated catalysis is the reduction of the o-quinone product of the enzymatic reaction back to the corresponding o-diphenol with the concomitant oxidation of ascorbic acid to dehydroascorbic acid
ascorbic acid
-
70.95% inhibition at 20 mM
ascorbic acid
-
inhibition of tyrosinase-catalyzed enzymatic browning by trapping the dopaquinone intermediate with cysteine or ascorbic acid, overview
ascorbic acid
-
competitive with pyrolallol or catechol, noncompetitive with 4-methylcatechol as substrate. IC50: 0.357 mM in reaction with 4-methylcatechol, IC50: 0.818 mM in reaction with pyrogallol, IC50: 0.33 mM in reaction with catechol
ascorbic acid
-
11% residual activity at 400 mM in cultivar Violetto di Sicilia, 29% residual activity at 200 mM in cultivar Violetto di Provenza, 8% residual activity at 400 mM in cultivar Tema 2000
ascorbic acid
-
markedly inhibits PPO
ascorbic acid
-
nearly complete inhibition at 10 mM
ascorbic acid
-
pulp enzyme, 1 mM, complete inhibition
ascorbic acid
-
peel enzyme, 1 mM, complete inhibition
ascorbic acid
-
one of the most effective inhibitors of isozyme PPO 1, complete inhibition at 0.1 mM
ascorbic acid
-
0.066 mM, 26%, 59% and 96% inhibition of isoenzymes B, C, and D, respectively
azelaic acid
-
-
benzoic acid
-
64.86% inhibition at 10 mM
benzoic acid
56% inhibition at 20 mM, no inhibition at 0.02-2.0 mM
benzoic acid
-
noncompetitive
captopril
-
-
catechol
-
field bean PPO obeys Michaelis-Menten kinetics and exhibits the phenomenon of inhibition by excess substrate for catechol, 4-methylcatechol and 4-tert-butylcatechol
catechol
-
catechol produces substrate inhibition above 16 mM
cinnamaldehyde
-
noncompetitive, 0.980 mM
cinnamaldehyde
-
noncompetitive, 0.980 mM
cinnamaldehyde
-
noncompetitive, 0.980 mM
cinnamaldehyde
-
noncompetitive, 0.980 mM
cinnamaldehyde
-
noncompetitive, 0.980 mM
Citric acid
-
68.92% inhibition at 20 mM
Citric acid
-
37% residual activity at 400 mM in cultivar Violetto di Sicilia, 59% residual activity at 200 mM in cultivar Violetto di Provenza, 18% residual activity at 400 mM in cultivar Tema 2000
Citric acid
-
32% residual activity at 10 mM
Citric acid
complete inhibition at 20 mM, 47% inhibition at 2 mM
Citric acid
-
slight inhibition
Citric acid
-
weak inhibition
CN-
-
1 mM, 82% inhibition
CN-
-
pulp enzyme, 1 mM, 80% inhibition
CN-
-
peel enzyme, 1 mM, 89% inhibition
CN-
-
0.165 mM, 84%, 70%, 100% and 40% inhibition of isoenzymes A, B, C and D, respectively
Co2+
-
35% residual activity at 10 mM
Cu2+
-
91.45% inhibition at 20 mM
Cu2+
-
moderately inhibits PPO
Cu2+
-
33% residual activity at 10 mM
cuminaldehyde
-
noncompetitive, IC50: 0.050 mM
cuminaldehyde
-
noncompetitive, IC50: 0.050 mM
cuminaldehyde
-
noncompetitive, IC50: 0.050 mM
cuminaldehyde
-
noncompetitive, IC50: 0.050 mM
cuminaldehyde
-
noncompetitive, IC50: 0.050 mM
Cupferron
-
-
cysteine
-
1 mM, 92% inhibition
cysteine
-
inhibition of tyrosinase-catalyzed enzymatic browning by trapping the dopaquinone intermediate with cysteine or ascorbic acid, overview
cysteine
-
pulp enzyme, 1 mM, complete inhibition
cysteine
-
peel enzyme, 1 mM, complete inhibition
davanol
-
-
decahydro-2-naphthyl gallate
-
-
decahydro-2-naphthyl gallate
-
-
decahydro-2-naphthyl gallate
-
-
decahydro-2-naphthyl gallate
-
-
decahydro-2-naphthyl gallate
-
-
diethyldithiocarbamate
-
-
diethyldithiocarbamate
-
72.37% inhibition at 20 mM, the diethyldithiocarbamate-inhibited phenoloxidase-like activity can be perfectly restored by 10 mM Cu2+ while Zn2+ has no recovery effect
diethyldithiocarbamate
-
pulp enzyme, 1 mM, complete inhibition
diethyldithiocarbamate
-
peel enzyme, 1 mM, complete inhibition
diethyldithiocarbamate
-
0.066 mM, 31%, 40%, 36% and 84% inhibition of isoenzymes A, B, C, and D, respectively
dithiothreitol
-
markedly inhibits PPO
dithiothreitol
-
complete inhibition at 0.150 mM of the root enzyme
dopamine
-
at high dopamine concentration, a decrease in activity is observed, indicating substrate inhibition
dopamine
-
dopamine produces substrate inhibition above 2 mM
dopastin
-
-
EDTA
-
75% inhibition at 10 mM
EDTA
-
88.8% inhibition at 3.75 mM
EDTA
73% inhibition at 2 mM, 31% inhibition at 0.2 mM
EDTA
-
inhibits the root enzyme, while the pulp enzyme is only poorly inhiibited
EDTA
-
5% residual activity at 0.1 mM
EDTA
-
100 mM, 33%, 60%, 81% and 35% inhibition of isoenzymes A, B, C and D, respectively
EDTA
-
10 mM, 15% inhibition
EDTA
-
22.2% inhibition at 2 mM
geranyl gallate
-
-
glabrene
-
mixed-type, IC50: 7.600 mM
glabrene
-
mixed-type, IC50: 7.600 mM
glabrene
-
mixed-type, IC50: 7.600 mM
glabrene
-
mixed-type, IC50: 7.600 mM
glabrene
-
mixed-type, IC50: 7.600 mM
glabridin
-
noncompetitive, IC50: 0.004 mM
glabridin
-
noncompetitive, IC50: 0.004 mM
glabridin
-
noncompetitive, IC50: 0.004 mM
glabridin
-
noncompetitive, IC50: 0.004 mM
glabridin
-
noncompetitive, IC50: 0.004 mM
glutathione
-
mixed type inhibition with 4-methylcatechol as substrate, noncompetitive with pyrogallol or catechol as substrates. IC50: 0.174 mM in reaction with 4-methylcatechol, IC50: 0.335 mM in reaction with pyrogallol, IC50: 0.323 mM in reaction with catechol
glutathione
complete inhibition at 2 mM, 94% inhibition at 0.2 mM
glutathione
-
1 mM, 98%, 95% and 96% inhibition of isoenzymes Ia, Ib, and II, respectively
glutathione
-
0.066 mM, 2%, 22% and 84% inhibition of isoenzymes B, C, and D, respectively
glutathione
-
competitive
isoascorbic acid
-
1 mM, 99% inhibition
isoascorbic acid
-
1 mM, complete inhibition of isoenzymes Ia, Ib and II
isoliquiritigenin
-
mixed-type, IC50: 0.047
isoliquiritigenin
-
mixed-type, IC50: 0.047
isoliquiritigenin
-
mixed-type, IC50: 0.047
isoliquiritigenin
-
mixed-type, IC50: 0.047
isoliquiritigenin
-
mixed-type, IC50: 0.047
kaempferol
-
-
kojic acid
-
IC50: 0.016.67 mM
kojic acid
-
IC50: 0.0163 mM
kojic acid
-
mixed-type, IC50: 0.014 mM
kojic acid
-
mixed inhibition
kojic acid
-
typical inhibitors of catecholoxidase, also inhibit the phenoloxidase activity of activated hemocyanin
kojic acid
-
mixed-type, IC50: 0.014 mM
kojic acid
-
mixed-type, IC50: 0.014 mM
kojic acid
-
11% residual activity at 10 mM
kojic acid
96% inhibition at 2 mM, 60% inhibition at 0.2 mM
kojic acid
-
mixed-type, IC50: 0.014 mM
kojic acid
-
1 mM complete inhibition of isoenzymes Ia, Ib and II
kojic acid
-
43% residual activity at 1 mM
kojic acid
-
99% inhibition of diphenolase activity at 1 mM
kojic acid
-
mixed-type, IC50: 0.014 mM
L-ascorbic acid
Ferula sp.
-
noncompetitive
L-ascorbic acid
-
complete inhibition at 0.90 mM of the root enzyme, and at 1 mM of the pulp enzyme
L-ascorbic acid
-
competitive
L-cysteine
-
43.24% inhibition at 20 mM
L-cysteine
-
complete inhibition at 0.973 mM of the root enzyme, and at 1 mM of the pulp enzyme
L-cysteine chloride
Ferula sp.
-
competitive
L-cysteine chloride
-
competitive
L-mimosine
-
IC50: 0.00368 mM
L-mimosine
-
typical inhibitors of catecholoxidase, also inhibit the phenoloxidase activity of activated hemocyanin
luteolin
-
noncompetitive, IC50: 0.190 mM
luteolin
-
noncompetitive, IC50: 0.190 mM
luteolin
-
noncompetitive, IC50: 0.190 mM
luteolin
-
noncompetitive, IC50: 0.190 mM
luteolin
-
noncompetitive, IC50: 0.190 mM
luteolin 7-O-glucoside
-
noncompetitive, IC50: 0.500 mM
luteolin 7-O-glucoside
-
noncompetitive, IC50: 0.500 mM
luteolin 7-O-glucoside
-
noncompetitive, IC50: 0.500 mM
luteolin 7-O-glucoside
-
noncompetitive, IC50: 0.500 mM
luteolin 7-O-glucoside
-
noncompetitive, IC50: 0.500 mM
m-hydroxybenzoic acid
-
m-hydroxybenzoic acid
-
-
Metabisulfite
-
1 mM, 95% inhibition
Methimazole
-
-
Mg2+
-
inhibits activity at 0.01 mM
morin
-
-
morin
-
competitive, IC50: 2.320 mM
NaCl
54% inhibition at 2 mM, 19% inhibition at 0.2 mM
NaCl
-
29% residual activity at 0.1 mM
NaCl
-
800 mM, 48%, 47%, 55% and 93% inhibition of isoenzymes A, B, C, and D, respectively
NaHSO3
-
-
NaHSO3
-
0.066 mM, 64%, 50% and 27% inhibition of isoenzymes B, C, and D, respectively
o-hydroxybenzoic acid
-
o-hydroxybenzoic acid
-
-
p-hydroxybenzoic acid
-
p-hydroxybenzoic acid
-
-
Phenylthiourea
-
typical inhibitors of catecholoxidase, also inhibit the phenoloxidase activity of activated hemocyanin
quercetin
-
-
quercetin
-
competitive, IC50: 0.2 mM
SDS
-
-
SDS
-
12.2% inhibition at 2 mM
Sodium azide
-
-
Sodium azide
-
competitive with 4-methylcatechol or pyrogallol, noncompetitive with catechol as substrate. IC50: 1.31 mM in reaction with 4-methylcatechol, IC50: 10.3 mM in reaction with pyrogallol, IC50: 4.32 mM in reaction with catechol
Sodium azide
complete inhibition at 2 mM, 99% inhibition at 0.2 mM
Sodium azide
-
noncompetitive
Sodium azide
-
10 mM, 100% inhibition
Sodium azide
-
26.6% inhibition at 2 mM
Sodium diethyl dithiocarbamate
Ferula sp.
-
competitive
Sodium diethyl dithiocarbamate
-
-
Sodium diethyl dithiocarbamate
-
cstrong competitive inhibitor
Sodium metabisulfite
Ferula sp.
-
competitive
Sodium metabisulfite
-
markedly inhibits PPO
Sodium metabisulfite
-
27% residual activity at 10 mM
Sodium metabisulfite
-
complete inhibition at 0.109 mM of the root enzyme, and at 1 mM of the pulp enzyme
Sodium metabisulfite
-
one of the most effective inhibitors of isozyme PPO 1, complete inhibition at 0.1 mM
Sodium metabisulfite
-
competitive
sodium sulfite
-
complete inhibition at 10 mM
tartaric acid
-
2% residual activity at 400 mM in cultivar Violetto di Sicilia, 18% residual activity at 400 mM in cultivar Violetto di Provenza, 29% residual activity at 400 mM in cultivar Tema 2000
Thiourea
-
1 mM, 59% inhibition
Thiourea
-
84.46% inhibition at 10 mM
Thiourea
-
strong inhibition of the reaction with catechol
tropolone
-
-
tropolone
-
competitive with pyrolallol or catechol, noncompetitive with 4-methylcatechol. IC50: 0.0109 mM in reaction with 4-methylcatechol, IC50: 0.0539 mM in reaction with pyrogallol, IC50: 0.0297 mM in reaction with catechol
tropolone
-
pseudo first-order rate constants for inactivation
tropolone
-
34% residual activity at 10 mM
tropolone
-
68% residual activity at 0.1 mM
tropolone
-
97% inhibition of diphenolase activity at 1 mM
tropolone
-
most powerful specific PPO inhibitor. It reduces the PPO activity by 50%, when used at a low 0.01 mM concentration
Zn2+
-
45.39% inhibition at 20 mM
Zn2+
-
moderately inhibits PPO
additional information
-
synthesis and evaluation of several tetraketones with variable substituents at C-7, IC50 values, overview
-
additional information
-
synthesis and inhibitory potential of seventeen synthesized oxazolone derivatives, structure-activity relationships, overview
-
additional information
-
no inhibition by cycloalpioside D, cycloorbicoside A, askendoside G, and cucurbitacin L
-
additional information
-
structure, application and importance of inhibitors, overview
-
additional information
-
volatile flavor constituents of Yuzu, Mochiyuzu, Kabosu, Daidai, Naoshichi, Kiyookadaidai, Lisbon lemon, and Eureka lemon essential oils act as inhibitors of diphenolase activity
-
additional information
-
no inhibition by Ca2+ and Mg2+
-
additional information
-
structure, application and importance of inhibitors, overview
-
additional information
-
no inhibition by EDTA, 4-aminobenzoate, salicylic acid, gallic acid and benzoic acid
-
additional information
-
kinetics of enzyme inactivation by temperature and pressure
-
additional information
-
melanin plays a crucial protective role against skin photocarcinogenesis, however, the production of abnormal melanin pigmentation is a serious esthetic problem in humans, melanin biosynthesis can be inhibited by avoiding UV exposure, the inhibition of tyrosinase, the inhibition of melanocyte metabolism and proliferation, or the removal of melanin with corneal ablation, overview, structure, application and importance of inhibitors, overview
-
additional information
-
not inhibited by SDS
-
additional information
-
inhibition by high concentrations of the substrates caffeic acid, dihydrocaffeic acid, chlorogenic acid and rosmarinic acid
-
additional information
-
inhibition by oxidation product from coffeoylquinic acid, oxidation product from (-)-epicatechin, oxidation product from (-)-epicatechin and caffeoylquinic acid, procyanidins from Avrolles cultivar, procyanidines from Kermerrien cultivar, procyanidins from Jeanne renard cultivar and oxidized procyanidins from Jeanne renard cultivar
-
additional information
-
PPO activity is more effectively inhibited in an acid than in an alkaline pH
-
additional information
-
not inhibited by 10 mM EDTA, Cu2+, Mn2+, Zn2+, and Ba2+
-
additional information
-
structure, application and importance of inhibitors, overview
-
additional information
-
no inhibition by amentoflavone, BHT, and morelloflavone
-
additional information
-
not inhibited by 2,2'-dipyridyl, 1,10-phenanthroline and EDTA
-
additional information
-
sensitivity to inhibitors of the soluble and particulate enzyme forms, overview
-
additional information
-
structure, application and importance of inhibitors, overview
-
additional information
-
no inhibition by kojic acid and 2-mercaptoethanol
-
additional information
-
inactivation of the enzyme in freshly prepared grape must under high hydrostatic pressure of 100-800 MPa, combined with moderate temperature (20-70°C), or atmospheric pressure conditions in a temperature range of 55-70°C, pressure and temperature act synergistically, except in the hightemperature-low-pressure region where an antagonistic effect is found, kinetics of thermal inactivation, overview
-
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3.7
2,3-Dihydroxybenzoic acid
Lablab purpureus
-
-
0.55
2,4-dihydroxy-N-(3,4,5-trihydroxybenzyl)benzamide
Agaricus bisporus
-
IC50: 0.550 mM
1.82
2,4-dihydroxy-N-(4-hydroxybenzyl)benzamide
Agaricus bisporus
-
IC50: 1.820 mM
0.00351
2-methyl-4-[(E)-(4-nitrophenyl)methylidene]-1,3-oxazol-5(4H)-one
Agaricus bisporus
-
IC50: 0.00351 mM
0.00311
2-methyl-4-[(E)-2-thienylmethylidene]-1,3-oxazol-5-one
Agaricus bisporus
-
IC50: 0.00311 mM
0.00123
2-methyl-4-[(E,2Z)-3-phenyl-2-propenyliden]-1,3-oxazol-5(4H)-one
Agaricus bisporus
-
IC50: 0.00123 mM
0.555
3,4,5-trihydroxy-N-(3,4,5-trihydroxybenzyl)benzamide
Agaricus bisporus
-
IC50: 0.555 mM
1.18
3,4,5-trihydroxy-N-(4-hydroxybenzyl)benzamide
Agaricus bisporus
-
IC50: 1.180 mM
3.8
3,4,5-Trihydroxybenzoic acid
Lablab purpureus
-
-
0.28
3,4-dihydroxy-N-(3,4,5-trihydroxybenzyl)benzamide
Agaricus bisporus
-
IC50: 0.280 mM
2
3,4-dihydroxy-N-(4-hydroxybenzyl)benzamide
Agaricus bisporus
-
IC50: 2.0 mM
2.8
3,4-dihydroxybenzoic acid
Lablab purpureus
-
-
0.705
3,5-dihydroxy-N-(3,4,5-trihydroxybenzyl)benzamide
Agaricus bisporus
-
IC50: 0.705 mM
0.71
3,5-dihydroxy-N-(4-hydroxybenzyl)benzamide
Agaricus bisporus
-
IC50: 0.710 mM
0.00215
3-(acetoyloxy)-2-hydroxy-4-[[5-oxo-2-phenyl-1,3-oxazol-4(5H)-ylidene]methyl]phenylacetate
Agaricus bisporus
-
IC50: 0.00215 mM
0.0021
3-aminophenyl-2,2'-methylenebis-(5,5-dimethylcyclohexane-1,3-dione)
Agaricus bisporus
-
IC50: 0.0021 mM
0.00219
3-aminophenyl-2,2'-methylenebis-(cyclohexane-1,3-dione)
Agaricus bisporus
-
IC50: 0.00219 mM
0.0032
3-chlorophenyl-2,2'-methylenebis-(5,5-dimethylcyclohexane-1,3-dione)
Agaricus bisporus
-
IC50: 0.0032 mM
0.00323
4-[(E)-(4-nitrophenyl)methylidene]-2-phenyl-1,3-oxazol-5(4H)-one
Agaricus bisporus
-
IC50: 0.00323 mM
0.33
ascorbic acid
Cynara cardunculus var. scolymus
-
competitive with pyrolallol or catechol, noncompetitive with 4-methylcatechol as substrate. IC50: 0.357 mM in reaction with 4-methylcatechol, IC50: 0.818 mM in reaction with pyrogallol, IC50: 0.33 mM in reaction with catechol
0.014
askendoside B
Agaricus bisporus
-
IC50 : 0.014 mM
1.2
benzoic acid
Lablab purpureus
-
-
0.49
beta-mercaptoethanol
Lactarius salmonicolor
-
-
0.135
DL-dithiothreitol
Cynara cardunculus var. scolymus
-
competitive with 4-methylcatechol, catechol or pyrogallol. IC50: 0.147 mM in reaction with 4-methylcatechol, IC50: 0.0329 mM in reaction with pyrogallol, IC50: 0.135 mM in reaction with catechol
0.044 - 0.563
hydroquinone
0.014 - 0.0163
kojic acid
0.15
L-Cys
Cynara cardunculus var. scolymus
-
competitive with 4-methylcatechol, catechol or pyrogallol. IC50: 0.125 mM in reaction with 4-methylcatechol, IC50: 0.637 mM in reaction with pyrogallol, IC50: 0.15 mM in reaction with catechol
0.00368
L-mimosine
Agaricus bisporus
-
IC50: 0.00368 mM
0.00038
L-tyrosine
Lactarius salmonicolor
-
-
0.5
luteolin 7-O-glucoside
1.1
m-hydroxybenzoic acid
Lablab purpureus
-
-
2.32
morin
Beta vulgaris
-
competitive, IC50: 2.320 mM
0.029
N-(2,4-dihydroxybenzyl)-2,4-dihydroxybenzamide
Agaricus bisporus
-
IC50: 0.029 mM
0.017
N-(2,4-dihydroxybenzyl)-3,4,5-trihydroxybenzamide
Agaricus bisporus
-
IC50: 0.017 mM
0.011
N-(2,4-dihydroxybenzyl)-3,4-dihydroxybenzamide
Agaricus bisporus
-
IC50: 0.011 mM
0.0022
N-(2,4-dihydroxybenzyl)-3,5-dihydroxybenzamide
Agaricus bisporus
-
IC50: 0.0022 mM
1.66
N-benzyl-2,4-dihydroxybenzamide
Agaricus bisporus
-
IC50: 1.660 mM
0.78
N-benzyl-3,4,5-trihydroxybenzamide
Agaricus bisporus
-
IC50: 0.780 mM
2
N-benzyl-3,4-dihydroxybenzamide
Agaricus bisporus
-
IC50: 2.0 mM
0.7
N-benzyl-3,5-dihydroxybenzamide
Agaricus bisporus
-
IC50: 0.700 mM
1.99
N-benzylamide
Agaricus bisporus
-
IC50: 1.990 mM
3.6
o-hydroxybenzoic acid
Lablab purpureus
-
-
0.12
oxalic acid
Lactarius salmonicolor
-
-
0.23
p-aminobenzenesulfonamide
Lactarius salmonicolor
-
-
1.3
p-hydroxybenzoic acid
Lablab purpureus
-
-
0.0026
phenyl-2,2'-methylenebis-(5,5-dimethylcyclohexane-1,3-dione)
Agaricus bisporus
-
IC50: 0.0026 mM
0.043 - 0.07
Phenylthiourea
4.32
Sodium azide
Cynara cardunculus var. scolymus
-
competitive with 4-methylcatechol or pyrogallol, noncompetitive with catechol as substrate. IC50: 1.31 mM in reaction with 4-methylcatechol, IC50: 10.3 mM in reaction with pyrogallol, IC50: 4.32 mM in reaction with catechol
0.15 - 0.157
sodium sulfite
0.4
syringic acid
Lactarius salmonicolor
-
-
0.062 - 0.372
Tannic acid
0.0297
tropolone
Cynara cardunculus var. scolymus
-
competitive with pyrolallol or catechol, noncompetitive with 4-methylcatechol. IC50: 0.0109 mM in reaction with 4-methylcatechol, IC50: 0.0539 mM in reaction with pyrogallol, IC50: 0.0297 mM in reaction with catechol
0.32
Anisaldehyde
Beta vulgaris
-
noncompetitive, IC50: 0.320 mM
0.32
Anisaldehyde
Homo sapiens
-
noncompetitive, IC50: 0.320 mM
0.32
Anisaldehyde
Neurospora crassa
-
noncompetitive, IC50: 0.320 mM
0.32
Anisaldehyde
Agaricus bisporus
-
noncompetitive, IC50: 0.320 mM
0.32
Anisaldehyde
Streptomyces glaucescens
-
noncompetitive, IC50: 0.320 mM
0.045
ascorbate
Physalis peruviana
-
pH 5.5, 25°C, with 4-methylcatechol
0.06
ascorbate
Physalis peruviana
-
pH 5.5, 25°C, with chlorogenic acid
3.56
CaCl2
Physalis peruviana
-
pH 5.5, 25°C, with chlorogenic acid
30.96
CaCl2
Physalis peruviana
-
pH 5.5, 25°C, with 4-methylcatechol
0.05
cuminaldehyde
Beta vulgaris
-
noncompetitive, IC50: 0.050 mM
0.05
cuminaldehyde
Homo sapiens
-
noncompetitive, IC50: 0.050 mM
0.05
cuminaldehyde
Neurospora crassa
-
noncompetitive, IC50: 0.050 mM
0.05
cuminaldehyde
Agaricus bisporus
-
noncompetitive, IC50: 0.050 mM
0.05
cuminaldehyde
Streptomyces glaucescens
-
noncompetitive, IC50: 0.050 mM
0.536
fukugiside
Physalis peruviana
-
pH 5.5, 25°C, with chlorogenic acid
0.632
fukugiside
Physalis peruviana
-
pH 5.5, 25°C, with 4-methylcatechol
7.6
glabrene
Beta vulgaris
-
mixed-type, IC50: 7.600 mM
7.6
glabrene
Homo sapiens
-
mixed-type, IC50: 7.600 mM
7.6
glabrene
Neurospora crassa
-
mixed-type, IC50: 7.600 mM
7.6
glabrene
Agaricus bisporus
-
mixed-type, IC50: 7.600 mM
7.6
glabrene
Streptomyces glaucescens
-
mixed-type, IC50: 7.600 mM
0.004
glabridin
Beta vulgaris
-
noncompetitive, IC50: 0.004 mM
0.004
glabridin
Homo sapiens
-
noncompetitive, IC50: 0.004 mM
0.004
glabridin
Neurospora crassa
-
noncompetitive, IC50: 0.004 mM
0.004
glabridin
Agaricus bisporus
-
noncompetitive, IC50: 0.004 mM
0.004
glabridin
Streptomyces glaucescens
-
noncompetitive, IC50: 0.004 mM
0.323
glutathione
Cynara cardunculus var. scolymus
-
mixed type inhibition with 4-methylcatechol as substrate, noncompetitive with pyrogallol or catechol as substrates. IC50: 0.174 mM in reaction with 4-methylcatechol, IC50: 0.335 mM in reaction with pyrogallol, IC50: 0.323 mM in reaction with catechol
0.91
glutathione
Lactarius salmonicolor
-
-
0.044
hydroquinone
Physalis peruviana
-
pH 5.5, 25°C, with chlorogenic acid
0.563
hydroquinone
Physalis peruviana
-
pH 5.5, 25°C, with 4-methylcatechol
0.047
isoliquiritigenin
Beta vulgaris
-
mixed-type, IC50: 0.047 mM
0.047
isoliquiritigenin
Neurospora crassa
-
mixed-type, IC50: 0.047 mM
0.047
isoliquiritigenin
Agaricus bisporus
-
mixed-type, IC50: 0.047 mM
0.047
isoliquiritigenin
Streptomyces glaucescens
-
mixed-type, IC50: 0.047 mM
0.014
kojic acid
Beta vulgaris
-
mixed-type, IC50: 0.014 mM
0.014
kojic acid
Homo sapiens
-
mixed-type, IC50: 0.014 mM
0.014
kojic acid
Neurospora crassa
-
mixed-type, IC50: 0.014 mM
0.014
kojic acid
Agaricus bisporus
-
mixed-type, IC50: 0.014 mM
0.014
kojic acid
Streptomyces glaucescens
-
mixed-type, IC50: 0.014 mM
0.016
kojic acid
Agaricus bisporus
-
IC50: 0.016.67 mM
0.0163
kojic acid
Agaricus bisporus
-
IC50: 0.0163 mM
0.044
L-cysteine
Physalis peruviana
-
pH 5.5, 25°C, with chlorogenic acid
0.052
L-cysteine
Physalis peruviana
-
pH 5.5, 25°C, with 4-methylcatechol
0.15
L-cysteine
Lactarius salmonicolor
-
-
0.19
luteolin
Beta vulgaris
-
noncompetitive, IC50: 0.190 mM
0.19
luteolin
Homo sapiens
-
noncompetitive, IC50: 0.190 mM
0.19
luteolin
Neurospora crassa
-
noncompetitive, IC50: 0.190 mM
0.19
luteolin
Agaricus bisporus
-
noncompetitive, IC50: 0.190 mM
0.19
luteolin
Streptomyces glaucescens
-
noncompetitive, IC50: 0.190 mM
0.5
luteolin 7-O-glucoside
Beta vulgaris
-
noncompetitive, IC50: 0.500 mM
0.5
luteolin 7-O-glucoside
Homo sapiens
-
noncompetitive, IC50: 0.500 mM
0.5
luteolin 7-O-glucoside
Neurospora crassa
-
noncompetitive, IC50: 0.500 mM
0.5
luteolin 7-O-glucoside
Agaricus bisporus
-
noncompetitive, IC50: 0.500 mM
0.5
luteolin 7-O-glucoside
Streptomyces glaucescens
-
noncompetitive, IC50: 0.500 mM
5.01
NaCl
Physalis peruviana
-
pH 5.5, 25°C, with chlorogenic acid
39.54
NaCl
Physalis peruviana
-
pH 5.5, 25°C, with 4-methylcatechol
0.043
Phenylthiourea
Ipomoea batatas
-
0.07
Phenylthiourea
Lablab purpureus
-
-
0.002
quercetin
Physalis peruviana
-
pH 5.5, 25°C, with chlorogenic acid
0.049
quercetin
Physalis peruviana
-
pH 5.5, 25°C, with 4-methylcatechol
0.2
quercetin
Sarcophaga bullata
-
competitive, IC50: 0.2 mM
0.15
sodium sulfite
Physalis peruviana
-
pH 5.5, 25°C, with 4-methylcatechol
0.157
sodium sulfite
Physalis peruviana
-
pH 5.5, 25°C, with chlorogenic acid
0.062
Tannic acid
Physalis peruviana
-
pH 5.5, 25°C, with chlorogenic acid
0.372
Tannic acid
Physalis peruviana
-
pH 5.5, 25°C, with 4-methylcatechol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00018
-
substrate caffeic acid or catechol, leaf enzyme extract
0.00054
-
substrate 3-hydroxytyrosine, leaf enzyme extract
0.00084
-
substrate 3-hydroxytyrosine, leaf enzyme extract
0.0009
-
substrate 3-hydroxytyrosine, leaf enzyme extract
0.0012
-
substrate catechol, leaf enzyme extract
0.0022
-
substrate catechol, leaf enzyme extract
0.0045
-
substrate catechol, leaf enzyme extract
0.0063
-
substrate catechol, leaf enzyme extract
0.0065
-
substrate catechol, leaf enzyme extract
0.007
-
substrate 5-caffeoyl quinic acid or 4-methylcatechol, leaf enzyme extract
0.01
-
substrate catechol, leaf enzyme extract
0.011
-
substrate 5-caffeoyl quinic acid, leaf enzyme extract
0.0124
-
substrate 5-caffeoyl quinic acid, leaf enzyme extract
0.014
Coffea guarini
-
substrate caffeic acid, leaf enzyme extract
0.016
-
substrate 5-caffeoyl quinic acid, leaf enzyme extract
0.017
-
substrate 5-caffeoyl quinic acid, leaf enzyme extract
0.018
-
substrate 4-methylcatechol, leaf enzyme extract
0.019
-
substrate 4-methylcatechol, leaf enzyme extract
0.02
-
substrate 4-methylcatechol, leaf enzyme extract
0.026
-
substrate 5-caffeoyl quinic acid, leaf enzyme extract
0.03
-
substrate 4-methylcatechol, leaf enzyme extract
0.036
-
substrate catechol, leaf enzyme extract
0.04
-
substrate 4-methylcatechol, leaf enzyme extract
0.045
Coffea guarini
-
substrate catechol, leaf enzyme extract
0.073
Coffea guarini
-
substrate 4-methylcatechol, leaf enzyme extract
0.09
Coffea guarini
-
substrate 5-caffeoyl quinic acid, leaf enzyme extract
0.145
-
using L-DOPA as substrate, crude enzyme, at pH 7.5 and 25°C
1
-
reaction with catechol
1.32
-
crude extract, at pH 7.0, 25°C
10
Mycelia sterilia
-
reaction with (-)-epigallocatechin
13.15
Ferula sp.
-
purified stem enzyme
18.18
-
purified recombinant enzyme
18.7
-
partially purified soluble, active enzyme form, substrate tert-butyl-catechol
2.2
Mycelia sterilia
-
reaction with catechol
204.69
-
purified enzyme, substrate chlorogenic acid, pH 5.0, 20°C
227700
-
highly purified enzyme, substrate catechol
24.1
-
solubilized, crude enzyme
241.5
-
isozyme PPO 2 after 183fold purification, at pH 7.0, 25°C
4.458
-
using L-DOPA as substrate, after 30.76fold purification, at pH 7.5 and 25°C
4.5
-
reaction with pyrogallol
41.6
Ferula sp.
-
purified leaf enzyme
5.5
-
reaction with (-)-epigallocatechin gallate
5.7
Mycelia sterilia
-
reaction with pyrogallol
7.3
-
reaction with (-)-epigallocatechin
788.3
-
partially purified enzyme
8.7
Mycelia sterilia
-
reaction with (-)-epigallocatechin gallate
8.76
-
isozyme PPO 1 after 6.6fold purification, at pH 7.0, 25°C
9.8
-
pH 6.0, 40°C, enzyme extract
91.5
-
purified particulate, latent enzyme form, substrate tert-butyl-catechol
0.00042
-
substrate caffeic acid, leaf enzyme extract
0.00042
-
substrate coumaric acid, leaf enzyme extract
0.0006
-
substrate 3-hydroxytyrosine, leaf enzyme extract
0.0006
Coffea guarini
-
substrate coumaric acid, leaf enzyme extract
0.0006
-
substrate coumaric acid, leaf enzyme extract
0.0014
-
substrate caffeic acid, leaf enzyme extract
0.0014
-
substrate caffeic acid, leaf enzyme extract
0.002
-
substrate caffeic acid, leaf enzyme extract
0.002
-
substrate 3-hydroxytyrosine, leaf enzyme extract
0.002
-
substrate 4-methylcatechol, leaf enzyme extract
0.002
-
substrate 3-hydroxytyrosine, leaf enzyme extract
0.003
-
substrate 4-methylcatechol, leaf enzyme extract
0.003
Coffea guarini
-
substrate 3-hydroxytyrosine, leaf enzyme extract
0.004
-
substrate caffeic acid, leaf enzyme extract
0.004
-
substrate 3-hydroxytyrosine, leaf enzyme extract
0.004
-
substrate 5-caffeoyl quinic acid, leaf enzyme extract
0.004
-
substrate caffeic acid, leaf enzyme extract
0.005
-
substrate caffeic acid, leaf enzyme extract
0.005
-
substrate 5-caffeoyl quinic acid, leaf enzyme extract
0.006
-
substrate catechol, leaf enzyme extract
0.006
-
substrate caffeic acid, leaf enzyme extract
0.006
-
substrate caffeic acid, leaf enzyme extract
0.008
-
substrate catechol, leaf enzyme extract
0.008
-
substrate 5-caffeoyl quinic acid, leaf enzyme extract
0.008
-
substrate caffeic acid, leaf enzyme extract
0.0083
-
substrate 4-methylcatechol, leaf enzyme extract
0.0083
-
substrate 4-methylcatechol, leaf enzyme extract
0.023
-
substrate 4-methylcatechol, leaf enzyme extract
0.023
-
substrate catechol, leaf enzyme extract
0.051
-
substrate 5-caffeoyl quinic acid, leaf enzyme extract
0.051
-
substrate 5-caffeoyl quinic acid, leaf enzyme extract
additional information
-
-
additional information
-
-
additional information
-
46000 units/mg, 1 unit is defined as absorbance change at 420 nm of 0.001 per min
additional information
-
the specific activity of the crude enzyme is 3.72 units/mg, the specific activity of the 28.24fold purified enzyme is 105 units/mg, one unit is defined as an increase in the rate of absorbance of 0.001 per min, using L-dopa as substrate, at pH 7.1 and 28°C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
Coffea guarini
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
assay optimization
additional information
-
-
additional information
Ferula sp.
-
substrate specificity, tissue specific activities, overview
additional information
-
compared to PPO from R405-2000, a nonembryogenic cultivar, PPO from coker 312 (embryogenic cultivar) shows a higher PPO activity increasing markedly form primary culture to third subculture
additional information
-
68077.0 units/mg, 1 unit is defined as absorbance change of 0.001 per min at 25°C
additional information
-
370004 U/mg for the purified native enzyme. One unit of enzyme activity is defined as a 0.001-unit change in absorbance per min per ml
additional information
-
-
additional information
-
-
additional information
-
13160.0 units/mg, 1 unit is defined as absorbance change at 420 nm of 0.1 per min
additional information
-
10512.0 units/mg, 1 unit is defined as absorbance change at 420 nm of 0.1 per min and per ml enzyme solution
additional information
-
-
additional information
-
-
additional information
-
4500 units/mg, 1 unit is defined as absorbance change at 420 nm of 0.01 per min
additional information
-
isoenzyme Ia, 123 units/mg, isoenzyme Ib, 113 units/mg, isoenzyme II, 242 units/mg, 1 unit is defined as absorbance change at 420 nm of 0.1 per min
additional information
-
isoenzyme A, 0.0016 units, isoenzyme B, 0.011 units, isoenzyme C, 0.0013 units/mg, isoenzyme D, 0.0028 units, 1 unit is defined as absorbance change at 420 nm of 0.001 per min
additional information
-
analysis of browning parameters
additional information
-
-
additional information
-
-
additional information
-
polyphenol oxidases are induced in cowpea plants by wounding. The highest activity levels are detected 48 h after this stimulus in both wounded and neighbor-to-wounded unifoliates of cowpea seedlings. The increase of activity is in the order of 13 to 15fold, respectively, in comparison to control unifoliates
additional information
-
2612.06 U/mg, one enzyme unit is defined as the amount of enzyme that produces a rise of 0.001 absorbance in one minute at 420 nm
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Wong, T.C.; Luh, B.S.; Whitaker, J.R.
Isolation and characterization of polyphenol oxidase isozymes of clingstone peach
Plant Physiol.
48
19-23
1971
Prunus persica
brenda
Motoda, S.
Properties of polyphenol oxidase from Alternaria tenuis
J. Ferment. Technol.
57
79-85
1979
Alternaria alternata
-
brenda
Motoda, S.
Purification and some properties of polyphenol oxidase from Alternaria tenuis
J. Ferment. Technol.
57
71-78
1979
Alternaria alternata, Alternaria alternata A-2
brenda
Palmieri, G.; Giardina, P.; Marzullo, L.; Desiderio, B.; Nitti, G.; Cannio, R.; Sannia, G.
Stability and activity of a phenol oxidase from the ligninolytic fungus Pleurotus ostreatus
Appl. Microbiol. Biotechnol.
39
632-636
1993
Pleurotus ostreatus
brenda
Dry, I.B.; Robinson, S.P.
Molecular cloning and characterisation of grape berry polyphenol oxidase
Plant Mol. Biol.
26
495-502
1994
Vitis vinifera (P43311), Vitis vinifera
brenda
Klabunde, T.; Eicken, C.; Sacchettini, J.C.; Krebs, B.
Crystal structure of a plant catechol oxidase containing a dicopper center
Nat. Struct. Biol.
5
1084-1090
1998
Ipomoea batatas
brenda
Rompel, A.; Fischer, H.; Meiwes, D.; Buldt-Karentzopoulos, K.; Magrini, A.; Eicken, C.; Gerdemann, C.; Krebs, B.
Substrate specificity of catechol oxidase from Lycopus europaeus and characterization of the bioproducts of enzymic caffeic acid oxidation
FEBS Lett.
445
103-110
1999
Lycopus europaeus
brenda
Yang, C.P.; Fujita, S.; Ashrafuzzaman, M.; Nakamura, N.; Hayashi, N.
Purification and characterization of polyphenol oxidase from banana (Musa sapientum L.) pulp
J. Agric. Food Chem.
48
2732-2735
2000
Musa x paradisiaca
brenda
Paul, B.; Gowda, L.R.
Purification and characterization of a polyphenol oxidase from the seeds of field bean (Dolichos lablab)
J. Agric. Food Chem.
48
3839-3846
2000
Lablab purpureus
brenda
Gentschev, P.; Moller, N.; Krebs, B.
New functional models for catechol oxidases
Inorg. Chim. Acta
300-302
442-452
2000
Ipomoea batatas
-
brenda
Mazzafera, P.; Robinson, S.P.
Characterization of polyphenol oxidase in coffee
Phytochemistry
55
285-296
2000
Coffea arabica
brenda
Yang, C.P.; Fujita, S.; Kohno, K.; Kusubayashi, A.; Ashrafuzzaman, M.; Hayashi, N.
Partial purification and characterization of polyphenol oxidase from banana (Musa sapientum L.) peel
J. Agric. Food Chem.
49
1446-1449
2001
Musa x paradisiaca
brenda
Shi, C.; Dai, Y.; Xu, X.; Xie, Y.; Liu, Q.
The purification of polyphenol oxidase from tobacco
Protein Expr. Purif.
24
51-55
2002
Nicotiana tabacum
brenda
Haase, W.; Ostrovsky, S.
Catecholase activity of a series of dicopper(II) complexes with variable Cu-OH(phenol) moieties
Inorg. Chem.
41
1788-1794
2002
Ipomoea batatas
brenda
Gerdemann, C.; Eicken, C.; Krebs, B.
The crystal structure of catechol oxidase: New insight into the function of type-3 copper proteins
Acc. Chem. Res.
35
183-191
2002
Embryophyta
brenda
Yamamoto, K.; Yoshitama, K.; Teramoto, S.
Purification and characterization of polyphenol oxidase from callus cultures of Portulaca grandiflora
Plant Biotechnol.
19
95-101
2002
Portulaca grandiflora
-
brenda
Endo, K.; Hosono, K.; Beppu, T.; Ueda, K.
A novel extracytoplasmic phenol oxidase of Streptomyces: its possible involvement in the onset of morphogenesis
Microbiology
148
1767-1776
2002
Streptomyces griseus
brenda
Senior, S.Z.; Mans, L.L.; VanGuilder, H.D.; Kelly, K.A.; Hendrich, M.P.; Elgren, T.E.
Catecholase activity associated with copper-S100B
Biochemistry
42
4392-4397
2003
Bos taurus
brenda
Wang, Q.; Chen, Q.X.; Huang, X.H.; Ke, L.N.; Shi, Y.; Wang, J.
Enzymatic characterization and functional groups of polyphenol oxidase from the pupae of blowfly (Sarcophaga bullata)
Biochemistry (Moscow)
69
918-920
2004
Sarcophaga bullata
brenda
Billaud, C.; Brun-Merimee, S.; Louarme, L.; Nicolas, J.
Effect of glutathione and Maillard reaction products prepared from glucose or fructose with glutathione on polyphenoloxidase from apple-I: Enzymatic browning and enzyme activity inhibition
Food Chem.
84
223-233
2003
Malus domestica
-
brenda
Arslan, O.; Erzengin, M.; Sinan, S.; Ozensoy, O.
Purification of mulberry (Morus alba L.) polyphenol oxidase by affinity chromatography and investigation of its kinetic and electrophoretic properties
Food Chem.
88
479-484
2004
Morus alba
brenda
Pruidze, G.N.; McHedlishvili, N.I.; Omiadze, N.T.; Gulua, L.K.; Pruidze, N.G.
Multiple forms of phenol oxidase from Kolkhida tea leaves (Camelia sinensis L.) and Mycelia sterilia IBR 35219/2 and their role in tea production
Food Res. Int.
36
587-595
2003
Camellia sinensis, Mycelia sterilia, Mycelia sterilia IBR 35219/2
brenda
Jiang, H.; Shi, C.; Xie, Y.; Xu, X.; Liu, Q.
Activation of tobacco leaf polyphenol oxidase by sodium dodecyl sulfate
Indian J. Biochem. Biophys.
40
350-353
2003
Nicotiana tabacum
brenda
Goswami, A.P.; Amarapurkar, S.V.
Purification of catecholase from Solanum melangena (brinjal)
Indian J. Biochem. Biophys.
40
442-446
2003
Solanum melongena
brenda
Yemenicioglu, A.; Cemeroglu, B.
Consistency of polyphenol oxidase (PPO) thermostability in ripening apricots (Prunus armeniaca L.): evidence for the presence of thermostable PPO forming and destabilizing mechanisms in apricots
J. Agric. Food Chem.
51
2371-2379
2003
Prunus armeniaca
brenda
Le Bourvellec, C.; Le Quere, J.M.; Sanoner, P.; Drilleau, J.F.; Guyot, S.
Inhibition of apple polyphenol oxidase activity by procyanidins and polyphenol oxidation products
J. Agric. Food Chem.
52
122-130
2004
Malus domestica
brenda
Gandia-Herrero, F.; Garcia-Carmona, F.; Escribano, J.
Purification and characterization of a latent polyphenol oxidase from beet root (Beta vulgaris L.)
J. Agric. Food Chem.
52
609-615
2004
Beta vulgaris
brenda
Dogan, S.; Turan, Y.; Erturk, H.; Arslan, O.
Characterization and purification of polyphenol oxidase from artichoke (Cynara scolymus L.)
J. Agric. Food Chem.
53
776-785
2005
Cynara cardunculus var. scolymus
brenda
Xu, J.; Zheng, T.; Meguro, S.; Kawachi, S.
Purification and characterization of polyphenol oxidase from Henry chestnuts (Castanea henryi)
J. Wood Sci.
50
260-265
2004
Castanea henryi
-
brenda
Hernandez-Romero, D.; Solano, F.; Sanchez-Amat, A.
Polyphenol oxidase activity expression in Ralstonia solanacearum
Appl. Environ. Microbiol.
71
6808-6815
2005
Ralstonia solanacearum
brenda
Selles-Marchart, S.; Casado-Vela, J.; Bru-Martinez, R.
Isolation of a latent polyphenol oxidase from loquat fruit (Eriobotrya japonica Lindl.): kinetic characterization and comparison with the active form
Arch. Biochem. Biophys.
446
175-185
2006
Rhaphiolepis bibas
brenda
Kanade, S.R.; Paul, B.; Rao, A.G.A.; Gowda, L.R.
The conformational state of polyphenol oxidase from field bean (Dolichos lablab) upon SDS and acid-pH activation
Biochem. J.
395
551-562
2006
Lablab purpureus
brenda
Khan, K.M.; Maharvi, G.M.; Khan, M.T.H.; Shaikh, A.J.; Perveen, S.; Begum, S.; Choudhary, M.I.
Tetraketones: a new class of tyrosinase inhibitors
Bioorg. Med. Chem.
14
344-351
2006
Agaricus bisporus
brenda
Khan, K.M.; Mughal, U.R.; Khan, M.T.H.; Perveen, Z.U.S.; Choudhary, M.I.
Oxazolones: new tyrosinase inhibitors; synthesis and their structure-activity relationships
Bioorg. Med. Chem.
14
6027-6033
2006
Agaricus bisporus
brenda
Khan, M.T.H.; Choudhary, I.; Rahman, A.U.; Mamedova, R.P.; Agzamova, M.A.; Sultankhodzhaev, M.N.; Isaev, M.I.
Tyrosinase inhibition studies of cycloartane and cucurbitane glycosides and their structureactivity relationships
Bioorg. Med. Chem.
14
6085-6088
2006
Agaricus bisporus
brenda
Cho, S.J.; Roh, J.S.; Sun, W.S.; Kim, S.H.; Park, K.D.
N-Benzylbenzamides: A new class of potent tyrosinase inhibitors
Bioorg. Med. Chem. Lett.
16
2682-2684
2006
Agaricus bisporus
brenda
Kim, Y.J.; Uyama, H.
Tyrosinase inhibitors from natural and synthetic sources: structure, inhibition mechanism and perspective for the future
Cell. Mol. Life Sci.
62
1707-1723
2005
Agaricus bisporus, Beta vulgaris, Homo sapiens, Neurospora crassa, Streptomyces glaucescens
brenda
Koval,I.A.; Selmeczi, K.; Belle, C.; Philouze, C.; Saint-Aman, E.; Gautier-Luneau, I.; Schuitema, A.M.; van Vliet, M.; Gamez, P.; Roubeau, O.; Lueken, M.; Krebs, B.; Lutz, M.; Spek, A.L.; Pierre, J.L.; Reedijk, J.
Catecholase activity of a copper(II) complex with a macrocyclic ligand: unraveling catalytic mechanisms
Chem. Eur. J.
12
6138 - 6150
2006
Ipomoea batatas
brenda
Selinheimo, E.; Saloheimo, M.; Ahola2, E.; Westerholm-Parvinen, A.; Kalkkinen, N.; Buchert, J.; Kruus, K.
Production and characterization of a secreted, C-terminally processed tyrosinase from the filamentous fungus Trichoderma reesei
FEBS J.
273
4322-4335
2006
Trichoderma reesei
brenda
Dogan, S.; Arslan, O.; zen, F.
Polyphenol oxidase activity of oregano at different stages
Food Chem.
91
341-345
2005
Origanum vulgare subsp. hirtum
brenda
Erat, M.; Sakiroglu, H.; Kufrevioglu, O.I.
Purification and characterization of polyphenol oxidase from Ferula sp.
Food Chem.
95
503-508
2006
Ferula sp.
brenda
Jang, J.; Shin, J.; Song, K.
Characterization of polyphenol oxidase from Solanum tuberosum Jasim
Food Sci. Biotechnol.
14
117-122
2005
Solanum tuberosum
-
brenda
Lim, J.; Jeong, M.; Moon, K.
Purification and characterization of polyphenol oxidase in the flesh of the Fuji apple
Food Sci. Biotechnol.
15
177-182
2006
Malus sp.
-
brenda
Dog An, S.; Turan, P.; Dog An, M.; Arslan, O.; Alkan, M.
Purification and characterization of Ocimum basilicum L. polyphenol oxidase
J. Agric. Food Chem.
53
10224-10230
2005
Ocimum basilicum
brenda
Orenes-Pinero, E.; Garcia-Carmona, F.; Sanchez-Ferrer, A.
A kinetic study of p-cresol oxidation by quince fruit polyphenol oxidase
J. Agric. Food Chem.
53
1196-1200
2005
Cydonia oblonga
brenda
Spagna, G.; Barbagallo, R.N.; Chisari, M.; Branca, F.
Characterization of a tomato polyphenol oxidase and its role in browning and lycopene content
J. Agric. Food Chem.
53
2032-2038
2005
Solanum lycopersicum
brenda
Rapeanu, G.; Van Loey, A.; Smout, C.; Hendrichx, M.
Thermal and high-pressure inactivation kinetics of polyphenol oxidase in victoria grape must
J. Agric. Food Chem.
53
2988-2994
2005
Vitis vinifera
brenda
Gandia-Herrero, F.; Nez-Atieanzar, M.J.; Cabanes, J.; Garcia-Carmona, F.; Escribano, J.
Differential activation of a latent polyphenol oxidase mediated by sodium dodecyl sulfate
J. Agric. Food Chem.
53
6825-6830
2005
Beta vulgaris
brenda
Gandia-Herrero, F.; Escribano, J.; Garcia-Carmona, F.
Characterization of the activity of tyrosinase on betaxanthins derived from (R)-amino acids
J. Agric. Food Chem.
53
9207-9212
2005
Agaricus bisporus
brenda
Matsuura, R.; Ukeda, H.; Sawamura, M.
Tyrosinase inhibitory activity of citrus essential oils
J. Agric. Food Chem.
54
2309-2313
2006
Agaricus bisporus
brenda
Gandia-Herrero, F.; Escribano, J.; Garcia-Carmona, F.
Characterization of the activity of tyrosinase on betanidin
J. Agric. Food Chem.
55
1546-1551
2007
Agaricus bisporus
brenda
Munoz, J.; Garcia-Molina, F.; Varon, R.; Rodriguez-Lopez, J.N.; Garcia-Ruiz, P.A.; Garcia-Casanovas, F.; Tudela, J.
Kinetic characterization of the oxidation of chlorogenic acid by polyphenol oxidase and peroxidase. Characteristics of the o-quinone
J. Agric. Food Chem.
55
920-928
2007
Agaricus bisporus
brenda
Matoba, Y.; Kumagai, T.; Yamamoto, A.; Yoshitsu, H.; Sugiyama, M.
Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis
J. Biol. Chem.
281
8981-8990
2006
Beta vulgaris
brenda
Olianas, A.; Sanjust, E.; Pellegrini, M.; Rescigno, A.
Tyrosinase activity and hemocyanin in the hemolymph of the slipper lobster Scyllarides latus
J. Comp. Physiol. B
175
405-411
2005
Scyllarides latus
brenda
Guelcin, I.; Kuefrevioglu, O.I.; Oktay, M.
Purification and characterization of polyphenol oxidase from nettle (Urtica dioica L.) and inhibitory effects of some chemicals on enzyme activity
J. Enzyme Inhib. Med. Chem.
20
297-302
2005
Urtica dioica
brenda
Dalmadi, I.; Rapeanu, G.; Van Loey, A.; Smout, C.; Hendrickx, M.
Characterization and inactivation by thermal and pressure processing of strawberry (Fragaria ananassa) polyphenol oxidase: a kinetic study
J. Food Biochem.
30
56-76
2006
Fragaria x ananassa
-
brenda
Ni Eidhinn, D.M.; Murphy, E.; O'Beirne, D.
Polyphenol oxidase from apple (Malus domestica Borkh. cv Bramleys seedling): purification strategies and characterization
J. Food Sci.
71
C51-C58
2006
Malus domestica
brenda
Garcia-Molina, F.; Penalver, M.J.; Fenoll, L.G.; Rodriguez-Lopez, J.N.; Varon, R.; Gracia-Canovas, F.; Tudela, J.
Kinetic study of monophenol and o-diphenol binding to oxytyrosinase
J. Mol. Catal. B
32
185-192
2005
Agaricus bisporus, Neurospora crassa, Streptomyces glaucescens
-
brenda
Aclecio Melo, G.; Massao Shimizu, M.; Mazzafera, P.
Polyphenoloxidase activity in coffee leaves and its role in resistance against the coffee leaf miner and coffee leaf rust
Phytochemistry
67
277-285
2006
Coffea arabica, Coffea brevipes, Coffea canephora, Coffea eugenioides, Coffea guarini, Coffea kapakata, Coffea liberica, Coffea liberica var. dewevrei, Coffea racemosa, Coffea salvatrix, Coffea stenophylla
brenda
Wuyts, N.; De Waele, D.; Swennen, R.
Extraction and partial characterization of polyphenol oxidase from banana (Musa acuminata Grande naine) roots
Plant Physiol. Biochem.
44
308-314
2006
Musa acuminata
brenda
Sutay Kocabas, D.; Bakir, U.; Phillips, S.E.; McPherson, M.J.; Ogel, Z.B.
Purification, characterization, and identification of a novel bifunctional catalase-phenol oxidase from Scytalidium thermophilum
Appl. Microbiol. Biotechnol.
79
407-415
2008
Aspergillus niger, Bos taurus, Homo sapiens
brenda
Campello, S.; Beltramini, M.; Giordano, G.; Di Muro, P.; Marino, S.M.; Bubacco, L.
Role of the tertiary structure in the diphenol oxidase activity of Octopus vulgaris hemocyanin
Arch. Biochem. Biophys.
471
159-167
2008
Octopus vulgaris
brenda
Kanade, S.R.; Suhas, V.L.; Chandra, N.; Gowda, L.R.
Functional interaction of diphenols with polyphenol oxidase. Molecular determinants of substrate/inhibitor specificity
FEBS J.
274
4177-4187
2007
Lablab purpureus, Ipomoea batatas (Q9ZP19)
brenda
Jaenicke, E.; Decker, H.
Kinetic properties of catecholoxidase activity of tarantula hemocyanin
FEBS J.
275
1518-1528
2008
Aphonopelma californicum (nom. dub.)
brenda
Chisari, M.; Barbagallo, R.N.; Spagna, G.
Characterization and role of polyphenol oxidase and peroxidase in browning of fresh-cut melon
J. Agric. Food Chem.
56
132-138
2008
Cucumis melo
brenda
Fang, C.; Wang, C.; Xiong, Y.L.; Pomper, K.W.
Extraction and characterization of polyphenol oxidase in pawpaw (Asimina triloba) fruit
J. Food Biochem.
31
603-620
2007
Asimina triloba
brenda
Perdomo-Morales, R.; Montero-Alejo, V.; Perera, E.; Pardo-Ruiz, Z.; Alonso-Jimenez, E.
Hemocyanin-derived phenoloxidase activity in the spiny lobster Panulirus argus (Latreille, 1804)
Biochim. Biophys. Acta
1780
652-658
2008
Panulirus argus
brenda
Dedeoglu, N.; Guler, O.O.
Differential in vitro inhibition of polyphenoloxidase from a wild edible mushroom Lactarius salmonicolor
J. Enzyme Inhib. Med. Chem.
24
464-470
2009
Lactarius salmonicolor
brenda
Kouakou, T.H.; Kouadio, Y.J.; Kouame, P.; Waffo-Teguo, P.; Decendit, A.; Merillon, J.M.
Purification and biochemical characterization of polyphenol oxidases from embryogenic and nonembryogenic cotton (Gossypium hirsutum L.) cells
Appl. Biochem. Biotechnol.
158
285-301
2009
Gossypium hirsutum
brenda
Gasparetti, C.; Faccio, G.; Arvas, M.; Buchert, J.; Saloheimo, M.; Kruus, K.
Discovery of a new tyrosinase-like enzyme family lacking a C-terminally processed domain: production and characterization of an Aspergillus oryzae catechol oxidase
Appl. Microbiol. Biotechnol.
86
213-226
2009
Aspergillus oryzae
brenda
Gheibi, N.; Saboury, A.A.; Haghbeen, K.; Rajaei, F.; Pahlevan, A.A.
Dual effects of aliphatic carboxylic acids on cresolase and catecholase reactions of mushroom tyrosinase
J. Enzyme Inhib. Med. Chem.
24
1076-1081
2009
Agaricus bisporus
brenda
Pinto, M.S.; Siqueira, F.P.; Oliveira, A.E.; Fernandes, K.V.
A wounding-induced PPO from cowpea (Vigna unguiculata) seedlings
Phytochemistry
69
2297-2302
2008
Vigna unguiculata
brenda
Fan, T.; Li, M.; Wang, J.; Yang, L.; Cong, R.
Purification and characterization of phenoloxidase from Octopus ocellatus
Acta Biochim. Biophys. Sin.
41
865-872
2009
Amphioctopus fangsiao
brenda
Holzapfel, C.; Shahrokh, P.; Kafkewitz, D.
Polyphenol oxidase activity in the roots of seedlings of Bromus (Poaceae) and other grass genera
Am. J. Bot.
97
1195-1199
2010
Bromus inermis, Bromus rubens
brenda
Kim, S.G.; Jung, B.W.; Kim, H.
Hemocyanin-derived phenoloxidase activity with broad temperature stability extending into the cold environment in hemocytes of the hair crab Erimacrus isenbeckii
Comp. Biochem. Physiol. B
159
103-108
2011
Erimacrus isenbeckii
brenda
Virador, V.M.; Reyes Grajeda, J.P.; Blanco-Labra, A.; Mendiola-Olaya, E.; Smith, G.M.; Moreno, A.; Whitaker, J.R.
Cloning, sequencing, purification, and crystal structure of Grenache (Vitis vinifera) polyphenol oxidase
J. Agric. Food Chem.
58
1189-1201
2010
Vitis vinifera (P93622), Vitis vinifera
brenda
Todaro, A.; Peluso, O.; Catalano, A.E.; Mauromicale, G.; Spagna, G.
Polyphenol oxidase activity from three sicilian artichoke [Cynara cardunculus L. var. scolymus L. (Fiori)] cultivars: studies and technological application on minimally processed production
J. Agric. Food Chem.
58
1714-1718
2010
Cynara cardunculus var. scolymus
brenda
Wu, Y.; Pan, L.; Yu, S.; Li, H.
Cloning, microbial expression and structure-activity relationship of polyphenol oxidases from Camellia sinensis
J. Biotechnol.
145
66-72
2010
Camellia sinensis (A6N8J4), Camellia sinensis (A6NAA0), Camellia sinensis (A6YS04), Camellia sinensis (A6YS05), Camellia sinensis (C5MLZ1), Camellia sinensis
brenda
Liu, J.W.; Huang, Y.Y.; Ding, J.; Liu, C.; Xiao, X.D.; Ni, D.J.
Prokaryotic expression and purification of Camellia sinensis polyphenol oxidase
J. Sci. Food Agric.
90
2490-2494
2010
Camellia sinensis
brenda
Palma-Orozco, G.; Ortiz-Moreno, A.; Dorantes-Alvarez, L.; Sampedro, J.G.; Najera, H.
Purification and partial biochemical characterization of polyphenol oxidase from mamey (Pouteria sapota)
Phytochemistry
72
82-88
2011
Pouteria sapota
brenda
Diwakar, S.K.; Mishra, S.K.
Purification and biochemical characterization of ionically unbound polyphenol oxidase from Musa paradisiaca leaf
Prep. Biochem. Biotechnol.
41
187-200
2011
Musa x paradisiaca
brenda
Hakulinen, N.; Gasparetti, C.; Kaljunen, H.; Kruus, K.; Rouvinen, J.
The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae
J. Biol. Inorg. Chem.
18
917-929
2013
Aspergillus oryzae (Q2UNF9), Aspergillus oryzae
brenda
Dirks-Hofmeister, M.E.; Inlow, J.K.; Moerschbacher, B.M.
Site-directed mutagenesis of a tetrameric dandelion polyphenol oxidase (PPO-6) reveals the site of subunit interaction
Plant Mol. Biol.
80
203-217
2012
Taraxacum officinale (I7HUF2), Taraxacum officinale
brenda
Liu, N.N.; Liu, W.; Wang, D.J.; Zhou, Y.B.; Lin, X.J.; Wang, X.; Li, S.B.
Purification and partial characterization of polyphenol oxidase from the flower buds of Lonicera japonica Thunb
Food Chem.
138
478-483
2013
Lonicera japonica
brenda
Bae, Y.A.; Cai, G.B.; Kim, S.H.; Sohn, W.M.; Kong, Y.
Expression pattern and substrate specificity of Clonorchis sinensis tyrosinases
Int. J. Parasitol.
43
891-900
2013
Clonorchis sinensis
brenda
Cheng, X.; Huang, X.; Liu, S.; Tang, M.; Hu, W.; Pan, S.
Characterization of germin-like protein with polyphenol oxidase activity from Satsuma mandarine
Biochem. Biophys. Res. Commun.
449
313-318
2014
Citrus unshiu
brenda
Gul Guven, R.; Aslan, N.; Guven, K.; Matpan Bekler, F.; Acer, O.
Purification and characterization of polyphenol oxidase from corn tassel
Cell. Mol. Biol.
62
6-11
2016
Zea mays
brenda
Cheema, S.; Sommerhalter, M.
Characterization of polyphenol oxidase activity in Ataulfo mango
Food Chem.
171
382-387
2015
Mangifera indica (D2XZ13), Mangifera indica
brenda
Liu, F.; Zhao, J.H.; Wen, X.; Ni, Y.Y.
Purification and structural analysis of membrane-bound polyphenol oxidase from Fuji apple
Food Chem.
183
72-77
2015
Malus domestica
brenda
Bravo, K.; Osorio, E.
Characterization of polyphenol oxidase from Cape gooseberry (Physalis peruviana L.) fruit
Food Chem.
197
185-190
2016
Physalis peruviana, Physalis peruviana Colombian ecotype
brenda
de Oliveira Carvalho, J.; Orlanda, J.F.F.
Heat stability and effect of pH on enzyme activity of polyphenol oxidase in buriti (Mauritia flexuosa Linnaeus f.) fruit extract
Food Chem.
233
159-163
2017
Mauritia flexuosa
brenda
Hua, Y.; Shen, G.; Liu, D.
Characterization of polyphenol oxidase extracted from white radish
Mod. Food Sci. Technol.
30
69-73
2014
Raphanus sativus
-
brenda
Mandal, L.; Mandal, S.; Mohanta, S.
Syntheses, crystal structures, magnetochemistry and catechol oxidase activity of a tetracopper(II) compound and a new type of dicopper(II)-based 1D coordination polymer
New J. Chem.
41
4689-4701
2017
synthetic construct
-
brenda
Sarkar, N.; Harms, K.; Frontera, A.; Chattopadhyay, S.
Importance of C-H...pi interactions in stabilizing the syn/anti arrangement of pendant alkoxy side arms in two manganese(IV) Schiff base complexes Exploration of catechol oxidase and phenoxazinone synthase like actIVities
New J. Chem.
41
8053-8065
2017
synthetic construct
-
brenda