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0.798 - 2.89
(-)-epicatechin
4
(-)-epigallocatechin
Mycelia sterilia
-
-
1.3
(-)-epigallocatechin gallate
Mycelia sterilia
-
-
1 - 2.16
1,2,3-benzenetriol
1.41
1-tert-butyl-catechol
-
pH 7.0
4 - 5.6
2,3,4-trihydroxybenzoic acid
1.16 - 5.1
3,4-Dihydroxyphenyl acetic acid
1.05 - 1.89
3,4-dihydroxyphenyl propionic acid
2.9 - 7.18
3,4-dihydroxyphenylacetic acid
1.31 - 3.69
3-methylcatechol
0.12 - 11.6
4-methylcatechol
4.1
4-tert-butylcatechol
-
-
3.9
4-tertiary butylcatechol
-
28.6
catechin
Mycelia sterilia
-
-
0.56 - 6.2
chlorogenic acid
8
D-2-methyl-3,4-dihydroxyphenylalanine
-
-
4.3
dihydrocaffeic acid
-
-
6.8
L-2-methyl-3,4-dihydroxyphenylalanine
-
-
0.57
L-3,4-dihydroxyphenylalanine methyl ester
-
-
0.0000239
L-adrenaline
-
pH 7.2, 20°C
0.0000194
L-noradrenaline
-
pH 7.2, 20°C
8
Luteolin-7-glycoside
-
-
1.2 - 1.23
tert-butyl-catechol
0.91 - 2.8
tert-butylcatechol
additional information
additional information
-
0.31
(+)-catechin
Ferula sp.
-
pH 6.5, 30°C, stem enzyme
0.554
(+)-catechin
Ferula sp.
-
pH 6.5, 30°C, leaf enzyme
0.99
(+)-catechin
-
pH 4.0, 25°C
0.798
(-)-epicatechin
Ferula sp.
-
pH 6.0, 15°C, leaf enzyme
2.89
(-)-epicatechin
Ferula sp.
-
pH 6.0, 15°C, stem enzyme
1
1,2,3-benzenetriol
-
pH 3.5, 25°C
2.16
1,2,3-benzenetriol
-
-
4
2,3,4-trihydroxybenzoic acid
-
-
5.6
2,3,4-trihydroxybenzoic acid
-
1.16
3,4-Dihydroxyphenyl acetic acid
-
-
4.4
3,4-Dihydroxyphenyl acetic acid
-
-
5.1
3,4-Dihydroxyphenyl acetic acid
-
-
1.05
3,4-dihydroxyphenyl propionic acid
-
-
1.89
3,4-dihydroxyphenyl propionic acid
-
-
2.9
3,4-dihydroxyphenylacetic acid
-
-
6
3,4-dihydroxyphenylacetic acid
-
6.66
3,4-dihydroxyphenylacetic acid
-
for Cucumis melo L. inodorus cv. Amarillo
7.18
3,4-dihydroxyphenylacetic acid
-
for Cucumis melo L. cantalupensis cv. Charentais
1.31
3-methylcatechol
pH 5.6, 25°C, MES buffer
3.69
3-methylcatechol
pH 5.4, 25°C, sodium acetate buffer
0.12
4-methylcatechol
-
pH 7.0
1.2
4-methylcatechol
-
pH 7.0, 25°C
1.25
4-methylcatechol
-
pH 3.5, 25°C
1.809
4-methylcatechol
-
-
2.36
4-methylcatechol
-
-
2.77
4-methylcatechol
-
pH 6.0, 25°C
3.44
4-methylcatechol
-
-
3.88
4-methylcatechol
-
pH 5.0, 20°C
6.58
4-methylcatechol
Ferula sp.
-
pH 6.0, 25°C, leaf enzyme
6.78
4-methylcatechol
Ferula sp.
-
pH 6.0, 25°C, stem enzyme
8
4-methylcatechol
-
pH 6.0, 30°C
8.3
4-methylcatechol
-
pH 6.5, 25°C
9.86
4-methylcatechol
-
-
10
4-methylcatechol
-
pH 7.0, 50°C
11.6
4-methylcatechol
-
-
5
caffeic acid
-
-
9.5
caffeic acid
-
pH 6.5, 25°C
0.1
catechol
-
pH 7.0
0.213
catechol
-
at pH 7.5 and 25°C
0.41
catechol
pH 6.2, 25°C, sodium phosphate buffer
0.414
catechol
-
pH 4.5, 25°C
0.68
catechol
pH 6.0, 25°C, MES buffer
0.87
catechol
pH 5.8, 25°C, sodium phosphate buffer
1.15
catechol
-
at 22°C, pH not specified in the publication
1.25
catechol
pH 5.8, 25°C, MES buffer
1.62
catechol
-
pH 8.0, 25°C
2.34
catechol
Ferula sp.
-
pH 7.0, 12°C, leaf enzyme
2.64
catechol
Ferula sp.
-
pH 7.0, 12°C, stem enzyme
3.48
catechol
-
pH 8.0, 40°C
4.2
catechol
Mycelia sterilia
-
-
4.2
catechol
-
isoenzyme B
5.95
catechol
-
pH 5.0, 25°C
6.3
catechol
-
in 20 mM Tris-HCl buffer at pH 7.1 and 28°C
6.6
catechol
-
isoenzyme A
7.174
catechol
-
SDS-activated hemocyanin
8
catechol
-
pH 7.0, 50°C
21.1
catechol
-
pH 6.5, 25°C
23.52
catechol
-
at pH 7.0 and 37°C
36
catechol
-
isoenzyme D
36.6
catechol
-
pH 6.8, 25°C
44
catechol
-
isozyme PPO 1, in 0.2 M sodium phosphate buffer pH 7.0, 25°C
53.8
catechol
-
pH 6.0, 40°C
69
catechol
-
pH 6.5, 25°C
203.8
catechol
-
pH 5.0, 20°C
326.6
catechol
-
Km of pawpaw fruit PPO is comparable with the Km of PPO from other fruits
0.56
chlorogenic acid
-
pH 5.0, 20°C
0.74
chlorogenic acid
-
-
0.764
chlorogenic acid
Ferula sp.
-
pH 6.0, 20°C, leaf enzyme
0.87
chlorogenic acid
-
pH 7.0
0.88
chlorogenic acid
-
leaf enzyme
1
chlorogenic acid
-
pH 4.5, 25°C, soluble, active enzyme form
1
chlorogenic acid
-
at pH 7.5 and 25°C
1.07
chlorogenic acid
Ferula sp.
-
pH 6.0, 20°C, stem enzyme
1.3 - 1.38
chlorogenic acid
-
pH 4.5, dependent on the assay method
2.27
chlorogenic acid
-
endosperm enzyme
5.7
chlorogenic acid
-
pH 4.5, 25°C, particulate, latent enzyme form
6.2
chlorogenic acid
-
pH 6.5, 25°C
0.47
D-catechin
-
-
1.2
D-catechin
-
pH 6.5, 25°C
0.000219
D-Dopa
-
pH 7.2, 20°C
0.181
dopamine
-
SDS-activated hemocyanin
0.427
dopamine
-
pH 6.5, 25°C
0.6
dopamine
-
pH 6.5, 25°C
1.22
dopamine
-
at substrate concentrations above 4 mM, substrate inhibition is observed and the data are fitted to a simple model for substrate inhibition. KM, kcat and KI are obtained for the inhibitory binding site
1.45
dopamine
-
substrate range 0.3-4 mM
0.000223
L-Dopa
-
pH 7.2, 20°C
0.96
L-Dopa
-
at 22°C, pH not specified in the publication
1.02
L-Dopa
-
pH 6.0, 25°C, soluble enzyme in presence of SDS
1.5
L-Dopa
-
pH 6.8, 30°C
1.6 - 2
L-Dopa
-
at pH 7.0 and 37°C
1.96
L-Dopa
-
pH 6.0, 25°C, membrane enzyme in presence of SDS
2.2
L-Dopa
-
isoenzyme Ib
2.45
L-Dopa
-
pH 6.0, 25°C, soluble enzyme
2.565
L-Dopa
-
SDS-activated hemocyanin
2.69
L-Dopa
-
at pH 7.5 and 25°C
3.1
L-Dopa
-
in 20 mM Tris-HCl buffer at pH 7.1 and 28°C
3.5
L-Dopa
-
isoenzyme II
6.18
L-Dopa
-
pH 6.0, 25°C, membrane enzyme
21.4
L-Dopa
-
pH 3.5, 25°C
56.3
L-Dopa
-
pH 6.5, 25°C
0.79
pyrogallol
pH 6.0, 25°C, MES buffer
0.83
pyrogallol
pH 5.8, 25°C, sodium phosphate buffer
1.26
pyrogallol
pH 5.4, 25°C, MES buffer
1.3
pyrogallol
-
isozyme PPO 1, in 0.2 M sodium phosphate buffer pH 7.0, 25°C
3.42
pyrogallol
-
pH 9.0, 25°C
3.9
pyrogallol
Mycelia sterilia
-
-
7.31
pyrogallol
pH 5.6, 25°C, sodium acetate buffer
19.6
pyrogallol
-
pH 6.8, 25°C
1.2
tert-butyl-catechol
-
pH 4.5, 25°C, soluble, active enzyme form
1.23
tert-butyl-catechol
-
pH 4.5, 25°C, particulate, latent enzyme form
0.91
tert-butylcatechol
-
-
2.8
tert-butylcatechol
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
betanidin degradation steady-state kinetics
-
additional information
additional information
-
detailed kinetics, overview
-
additional information
additional information
-
detailed kinetics, overview
-
additional information
additional information
-
detailed kinetics, overview
-
additional information
additional information
-
general kinetic mechanism, the diphenolase activity is characterized by a lag period, whose duration depends on the substrate concentration, the pH, and the presence of catalytic amounts of o-diphenol, overview
-
additional information
additional information
-
kinetic mechanism, general kinetic model
-
additional information
additional information
-
kinetics and activation energy, dependent on the locality of origin, the growth phase, and the tissue, overview
-
additional information
additional information
-
kinetics of the activation process of latent PPO by trypsin, Michaelis-Menten mechanism with double intermediate
-
additional information
additional information
-
kinetics, tetranuclear carbonato-bridged copper(II) cluster with the macrocyclic ligand, overview
-
additional information
additional information
-
temperature and pH dependencis of the two enzyme forms, in absence or presence of SDS
-
additional information
additional information
-
the enhancement of kcat upon activation is accompanied by a marked shift in the pH optimum for the oxidation of t-butyl catechol from 4.5 to 6.0, an increased sensitivity to tropolone, altered susceptibility to proteolytic degradation and decreased thermostability
-
additional information
additional information
-
thermodynamics and Michaelis-Menten kinetics, modeling in connection with pressure inactivation kinetics, overview
-
additional information
additional information
wild-type isozyme PPO-6 displays a low degree in cooperativity in catalysis. Cooperativity of the C197S mutein is significantly decreased at pH 3.5, under SDS activation at pH 5.0 the degree of cooperativity of the C197S mutein is similar to that of the PPO-6 wild-type enzyme
-
additional information
additional information
-
wild-type isozyme PPO-6 displays a low degree in cooperativity in catalysis. Cooperativity of the C197S mutein is significantly decreased at pH 3.5, under SDS activation at pH 5.0 the degree of cooperativity of the C197S mutein is similar to that of the PPO-6 wild-type enzyme
-
additional information
additional information
Michaelis-Menten kinetics at different pH and in different buffer systems, overview
-
additional information
additional information
-
Michaelis-Menten kinetics at different pH and in different buffer systems, overview
-