BRENDA - Enzyme Database

Purification and characterization of polyphenol oxidase from Ferula sp.

Erat, M.; Sakiroglu, H.; Kufrevioglu, O.I.; Food Chem. 95, 503-508 (2006)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.10.3.1
2-mercaptoethanol
competitive
Ferula sp.
1.10.3.1
L-ascorbic acid
noncompetitive
Ferula sp.
1.10.3.1
L-cysteine chloride
competitive
Ferula sp.
1.10.3.1
Sodium diethyl dithiocarbamate
competitive
Ferula sp.
1.10.3.1
Sodium metabisulfite
competitive
Ferula sp.
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.10.3.1
0.31
-
(+)-catechin
pH 6.5, 30°C, stem enzyme
Ferula sp.
1.10.3.1
0.554
-
(+)-catechin
pH 6.5, 30°C, leaf enzyme
Ferula sp.
1.10.3.1
0.764
-
chlorogenic acid
pH 6.0, 20°C, leaf enzyme
Ferula sp.
1.10.3.1
0.798
-
(-)-epicatechin
pH 6.0, 15°C, leaf enzyme
Ferula sp.
1.10.3.1
1.07
-
chlorogenic acid
pH 6.0, 20°C, stem enzyme
Ferula sp.
1.10.3.1
2.34
-
catechol
pH 7.0, 12°C, leaf enzyme
Ferula sp.
1.10.3.1
2.64
-
catechol
pH 7.0, 12°C, stem enzyme
Ferula sp.
1.10.3.1
2.89
-
(-)-epicatechin
pH 6.0, 15°C, stem enzyme
Ferula sp.
1.10.3.1
6.58
-
4-methylcatechol
pH 6.0, 25°C, leaf enzyme
Ferula sp.
1.10.3.1
6.78
-
4-methylcatechol
pH 6.0, 25°C, stem enzyme
Ferula sp.
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.10.3.1
(+)-catechin + O2
Ferula sp.
-
?
-
-
?
1.10.3.1
(-)-epicatechin + O2
Ferula sp.
-
?
-
-
?
1.10.3.1
4-methylcatechol + O2
Ferula sp.
-
4-methyl-1,2-benzoquinone + H2O
-
-
?
1.10.3.1
catechol + 1/2 O2
Ferula sp.
-
1,2-benzoquinone + H2O
-
-
?
1.10.3.1
chlorogenic acid + O2
Ferula sp.
-
?
-
-
?
1.10.3.1
additional information
Ferula sp.
polyphenol oxidase is a major enzyme responsible for the browning reaction in damaged plant tissues and fruits
?
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.10.3.1
Ferula sp.
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.10.3.1
native enzyme, 25.8fold from stem and 43.3 from leaves, by (NH4)2SO4 precipitation, dialysis, and gel filtration
Ferula sp.
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
1.10.3.1
leaf
-
Ferula sp.
-
1.10.3.1
root
-
Ferula sp.
-
1.10.3.1
stem
-
Ferula sp.
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.10.3.1
additional information
-
substrate specificity, tissue specific activities, overview
Ferula sp.
1.10.3.1
13.15
-
purified stem enzyme
Ferula sp.
1.10.3.1
41.6
-
purified leaf enzyme
Ferula sp.
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.10.3.1
(+)-catechin + O2
-
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
(-)-epicatechin + O2
-
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
(-)-epicatechin + O2
high activity
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
4-methylcatechol + O2
-
673779
Ferula sp.
4-methyl-1,2-benzoquinone + H2O
-
-
-
?
1.10.3.1
catechin + O2
-
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
catechol + 1/2 O2
-
673779
Ferula sp.
1,2-benzoquinone + H2O
-
-
-
?
1.10.3.1
catechol + 1/2 O2
best substrate
673779
Ferula sp.
1,2-benzoquinone + H2O
-
-
-
?
1.10.3.1
chlorogenic acid + O2
-
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
dopamine + O2
low activity
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
gallic acid + O2
low activity
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
L-DOPA + O2
low activity
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
additional information
polyphenol oxidase is a major enzyme responsible for the browning reaction in damaged plant tissues and fruits
673779
Ferula sp.
?
-
-
-
-
1.10.3.1
additional information
substrate specificity, overview, no activity with L-tyrosine
673779
Ferula sp.
?
-
-
-
-
1.10.3.1
pyrogallol + O2
low activity
673779
Ferula sp.
?
-
-
-
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.10.3.1
12
30
dependent on the substrate, overview
Ferula sp.
Temperature Range [°C]
EC Number
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
1.10.3.1
5
70
-
Ferula sp.
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
1.10.3.1
30
-
60 min, purified enzyme, 40% reduced activity
Ferula sp.
1.10.3.1
40
-
60 min, purified enzyme, 65% reduced activity
Ferula sp.
1.10.3.1
50
-
60 min, purified enzyme, complete inactivation
Ferula sp.
1.10.3.1
60
-
40 min, purified enzyme, irreversible denaturation
Ferula sp.
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.10.3.1
6
7
dependent on the substrate, overview
Ferula sp.
pH Range
EC Number
pH Minimum
pH Maximum
Commentary
Organism
1.10.3.1
5
7.5
-
Ferula sp.
pH Stability
EC Number
pH Stability
pH Stability Maximum
Commentary
Organism
1.10.3.1
5
7.5
-
Ferula sp.
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.10.3.1
0.0259
-
Sodium metabisulfite
pH 7.0, stem enzyme
Ferula sp.
1.10.3.1
0.0454
-
Sodium diethyl dithiocarbamate
pH 7.0, stem enzyme
Ferula sp.
1.10.3.1
0.0632
-
2-mercaptoethanol
pH 7.0, stem enzyme
Ferula sp.
1.10.3.1
0.0645
-
Sodium diethyl dithiocarbamate
pH 7.0, leaf enzyme
Ferula sp.
1.10.3.1
0.0718
-
L-ascorbic acid
pH 7.0, stem enzyme
Ferula sp.
1.10.3.1
0.0815
-
L-ascorbic acid
pH 7.0, leaf enzyme
Ferula sp.
1.10.3.1
0.116
-
L-cysteine chloride
pH 7.0, stem enzyme
Ferula sp.
1.10.3.1
0.119
-
Sodium metabisulfite
pH 7.0, leaf enzyme
Ferula sp.
1.10.3.1
0.126
-
L-cysteine chloride
pH 7.0, leaf enzyme
Ferula sp.
1.10.3.1
0.138
-
2-mercaptoethanol
pH 7.0, leaf enzyme
Ferula sp.
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.10.3.1
2-mercaptoethanol
competitive
Ferula sp.
1.10.3.1
L-ascorbic acid
noncompetitive
Ferula sp.
1.10.3.1
L-cysteine chloride
competitive
Ferula sp.
1.10.3.1
Sodium diethyl dithiocarbamate
competitive
Ferula sp.
1.10.3.1
Sodium metabisulfite
competitive
Ferula sp.
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.10.3.1
0.0259
-
Sodium metabisulfite
pH 7.0, stem enzyme
Ferula sp.
1.10.3.1
0.0454
-
Sodium diethyl dithiocarbamate
pH 7.0, stem enzyme
Ferula sp.
1.10.3.1
0.0632
-
2-mercaptoethanol
pH 7.0, stem enzyme
Ferula sp.
1.10.3.1
0.0645
-
Sodium diethyl dithiocarbamate
pH 7.0, leaf enzyme
Ferula sp.
1.10.3.1
0.0718
-
L-ascorbic acid
pH 7.0, stem enzyme
Ferula sp.
1.10.3.1
0.0815
-
L-ascorbic acid
pH 7.0, leaf enzyme
Ferula sp.
1.10.3.1
0.116
-
L-cysteine chloride
pH 7.0, stem enzyme
Ferula sp.
1.10.3.1
0.119
-
Sodium metabisulfite
pH 7.0, leaf enzyme
Ferula sp.
1.10.3.1
0.126
-
L-cysteine chloride
pH 7.0, leaf enzyme
Ferula sp.
1.10.3.1
0.138
-
2-mercaptoethanol
pH 7.0, leaf enzyme
Ferula sp.
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.10.3.1
0.31
-
(+)-catechin
pH 6.5, 30°C, stem enzyme
Ferula sp.
1.10.3.1
0.554
-
(+)-catechin
pH 6.5, 30°C, leaf enzyme
Ferula sp.
1.10.3.1
0.764
-
chlorogenic acid
pH 6.0, 20°C, leaf enzyme
Ferula sp.
1.10.3.1
0.798
-
(-)-epicatechin
pH 6.0, 15°C, leaf enzyme
Ferula sp.
1.10.3.1
1.07
-
chlorogenic acid
pH 6.0, 20°C, stem enzyme
Ferula sp.
1.10.3.1
2.34
-
catechol
pH 7.0, 12°C, leaf enzyme
Ferula sp.
1.10.3.1
2.64
-
catechol
pH 7.0, 12°C, stem enzyme
Ferula sp.
1.10.3.1
2.89
-
(-)-epicatechin
pH 6.0, 15°C, stem enzyme
Ferula sp.
1.10.3.1
6.58
-
4-methylcatechol
pH 6.0, 25°C, leaf enzyme
Ferula sp.
1.10.3.1
6.78
-
4-methylcatechol
pH 6.0, 25°C, stem enzyme
Ferula sp.
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.10.3.1
(+)-catechin + O2
Ferula sp.
-
?
-
-
?
1.10.3.1
(-)-epicatechin + O2
Ferula sp.
-
?
-
-
?
1.10.3.1
4-methylcatechol + O2
Ferula sp.
-
4-methyl-1,2-benzoquinone + H2O
-
-
?
1.10.3.1
catechol + 1/2 O2
Ferula sp.
-
1,2-benzoquinone + H2O
-
-
?
1.10.3.1
chlorogenic acid + O2
Ferula sp.
-
?
-
-
?
1.10.3.1
additional information
Ferula sp.
polyphenol oxidase is a major enzyme responsible for the browning reaction in damaged plant tissues and fruits
?
-
-
-
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.10.3.1
native enzyme, 25.8fold from stem and 43.3 from leaves, by (NH4)2SO4 precipitation, dialysis, and gel filtration
Ferula sp.
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
1.10.3.1
leaf
-
Ferula sp.
-
1.10.3.1
root
-
Ferula sp.
-
1.10.3.1
stem
-
Ferula sp.
-
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
1.10.3.1
additional information
-
substrate specificity, tissue specific activities, overview
Ferula sp.
1.10.3.1
13.15
-
purified stem enzyme
Ferula sp.
1.10.3.1
41.6
-
purified leaf enzyme
Ferula sp.
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.10.3.1
(+)-catechin + O2
-
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
(-)-epicatechin + O2
-
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
(-)-epicatechin + O2
high activity
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
4-methylcatechol + O2
-
673779
Ferula sp.
4-methyl-1,2-benzoquinone + H2O
-
-
-
?
1.10.3.1
catechin + O2
-
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
catechol + 1/2 O2
-
673779
Ferula sp.
1,2-benzoquinone + H2O
-
-
-
?
1.10.3.1
catechol + 1/2 O2
best substrate
673779
Ferula sp.
1,2-benzoquinone + H2O
-
-
-
?
1.10.3.1
chlorogenic acid + O2
-
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
dopamine + O2
low activity
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
gallic acid + O2
low activity
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
L-DOPA + O2
low activity
673779
Ferula sp.
?
-
-
-
?
1.10.3.1
additional information
polyphenol oxidase is a major enzyme responsible for the browning reaction in damaged plant tissues and fruits
673779
Ferula sp.
?
-
-
-
-
1.10.3.1
additional information
substrate specificity, overview, no activity with L-tyrosine
673779
Ferula sp.
?
-
-
-
-
1.10.3.1
pyrogallol + O2
low activity
673779
Ferula sp.
?
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.10.3.1
12
30
dependent on the substrate, overview
Ferula sp.
Temperature Range [°C] (protein specific)
EC Number
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
1.10.3.1
5
70
-
Ferula sp.
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
1.10.3.1
30
-
60 min, purified enzyme, 40% reduced activity
Ferula sp.
1.10.3.1
40
-
60 min, purified enzyme, 65% reduced activity
Ferula sp.
1.10.3.1
50
-
60 min, purified enzyme, complete inactivation
Ferula sp.
1.10.3.1
60
-
40 min, purified enzyme, irreversible denaturation
Ferula sp.
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.10.3.1
6
7
dependent on the substrate, overview
Ferula sp.
pH Range (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
Organism
1.10.3.1
5
7.5
-
Ferula sp.
pH Stability (protein specific)
EC Number
pH Stability
pH Stability Maximum
Commentary
Organism
1.10.3.1
5
7.5
-
Ferula sp.