1.10.3.1: catechol oxidase
This is an abbreviated version!
For detailed information about catechol oxidase, go to the full flat file.
Word Map on EC 1.10.3.1
-
1.10.3.1
-
limpet
-
keyhole
-
brown
-
catalase
-
lymphocyte
-
dismutase
-
hemolymph
-
igm
-
humoral
-
larvae
-
shrimp
-
mushroom
-
haptens
-
vannamei
-
sod
-
antigen-specific
-
melanization
-
arthropod
-
haemocyte
-
melanin
-
crab
-
litopenaeus
-
idiotype
-
o-quinones
-
crustacean
-
hepatopancreas
-
chlorogenic
-
delayed-type
-
ammonia-lyase
-
l-dopa
-
postharvest
-
laccase
-
shelf
-
molluscan
-
anti-idiotypic
-
dinuclear
-
gastropod
-
crayfish
-
nutrition
-
pyrogallol
-
agriculture
-
drug development
-
lobster
-
alginolyticus
-
entomopathogenic
-
copper-binding
-
antiferromagnetic
-
penaeus
-
kojic
-
copper-containing
-
pomatia
-
food industry
-
toxoid
-
limulus
- 1.10.3.1
-
limpet
-
keyhole
- brown
- catalase
- lymphocyte
- dismutase
- hemolymph
- igm
-
humoral
- larvae
- shrimp
- mushroom
-
haptens
- vannamei
- sod
-
antigen-specific
-
melanization
-
arthropod
- haemocyte
- melanin
- crab
- litopenaeus
-
idiotype
- o-quinones
-
crustacean
- hepatopancreas
-
chlorogenic
-
delayed-type
-
ammonia-lyase
- l-dopa
-
postharvest
- laccase
-
shelf
-
molluscan
-
anti-idiotypic
-
dinuclear
-
gastropod
- crayfish
- nutrition
- pyrogallol
- agriculture
- drug development
- lobster
- alginolyticus
-
entomopathogenic
-
copper-binding
-
antiferromagnetic
- penaeus
-
kojic
-
copper-containing
- pomatia
- food industry
- toxoid
- limulus
Reaction
2 catechol
+
Synonyms
1,2-benzene: oxygen oxidoreductase, 1,2-benzenediol:oxygen oxidoreductase, AoCO4, catalase-phenol oxidase, catechol oxidase, catecholase, catecholoxidase, CATPO, CO, copper-S100B, cresolase, dihydroxy-L-phenylalanine:oxygen oxidoreductase, Diphenol oxidase, diphenolase, dopa oxidase, germin-like protein, GLP, hemocyanin, ibCO, LsPPO, mettyrosinase, monophenol, o-diphenol: oxygen oxidoreductase, monophenol, o-diphenol:oxygen oxidoreductase, More, MppO, o-diphenol oxidoreductase, o-diphenol: dioxygen oxidoreductase, dehydrogenating, o-diphenol:oxygen oxidoreductase, o-diphenolase, o-diphenoloxidase, oxytyrosinase, phenol oxidase, phenolase, phenoloxidase, polyphenol oxidase, polyphenoloxidase, PPO, PPO 1, PPO 2, PPO II, PPO-6, pyrocatechol oxidase, TYR3, tyrosinase
ECTree
1.10.3.1 catechol oxidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.10.3.1 - catechol oxidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(-)-catechin + O2
?
-
enzyme activity relative to 4-methylcatechol: 0.77%
-
-
?
(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
-
?
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
3-(3,4-dihydroxyphenyl)-L-alanine + O2
?
-
enzyme activity relative to 4-methylcatechol: 1.15%
-
-
?
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
-
-
?
D-2-methyl-3,4-dihydroxyphenylalanine + O2
2-methyldopaquinone + H2O
-
-
-
-
r
dihydroxyphenylalanine + O2
dihydroxyphenylalanine quinone + H2O
-
-
-
-
?
DL-2-methyl-3,4-dihydroxyphenylalanine + O2
2-methyldopaquinone + H2O
-
the L-isomer is preferred
-
-
?
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-dihydroxyphenylalanine + O2
L-dopaquinone + H2O
-
L-dopa
-
-
?
tert-butyl-catechol + O2
?
-
2fold faster reaction rate with the particulate, latent enzyme form compared to the soluble active enzyme
-
-
?
tetramethylbenzidine + O2
?
-
enzyme shows low affinity to this substrate
-
-
?
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
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
-
the highest oxidase activity is observed against catechol
-
-
?
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
-
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
-
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
-
100% activity with 10 mM substrate concentration
-
-
?
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
-
enzyme activity relative to 4-methylcatechol: 87%
-
-
?
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
the reaction depends on molecular oxygen, which is reduced by the copper-containing catalytic domain of the enzyme
-
-
?
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
-
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
-
highest level of enzyme activity in cultivar Violetto di Provenza
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
208% activity with 10 mM substrate concentration compared to catechol
-
-
?
4-methylcatechol + O2
?
-
enzyme shows high affinity to this substrate
-
-
?
4-methylcatechol + O2
?
-
enzyme shows highest affinity to this substrate
-
-
?
4-methylcatechol + O2
?
-
enzyme shows highest activity with 4-methylcatechol
-
-
?
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
-
-
?
caffeic acid + 1/2 O2
caffeoyl quinone + H2O
-
2% of activity with dopamine
-
-
?
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
-
no activity with tyrosine, 2-methoxyphenol, 4-hydroxy-3-methoxy-cinnamic acid, hydroquinone and rutin
-
?
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
-
no activity with tyrosine, o-methoxyphenol, p-catechol and m-catechol
-
?
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
-
?
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
?
-
highest level of enzyme activity in cultivars Tema 2000 and Violetto di Sicilia
-
-
?
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
?
-
preferred substrate, 50fold faster reaction rate with the particulate, latent enzyme form compared to the soluble active enzyme
-
-
?
chlorogenic acid + O2
?
-
enzyme activity relative to 4-methylcatechol: 6.15%
-
-
?
D-dopa + 1/2 O2
D-dopaquinone + H2O
-
isoenzymes Ia, Ib and II, 54, 60 and 48% of activity with L-dopa respectively
-
?
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-DOPA + O2
dopaquinone + H2O
-
i.e. DL-3,4-dihydroxyphenylalanine, the L-isomer is preferred
-
-
?
dopamine + O2
4-(2-aminoethyl)-1,2-benzoquinone + 2 H2O
-
isoenzymes A-D
-
?
gallic acid + O2
?
-
enzyme shows very low affinity to this substrate
-
-
?
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
-
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
-
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
-
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-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
-
-
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
-
?
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
?
-
enzyme activity relative to 4-methylcatechol: 9.24%
-
-
?
additional information
?
-
-
role of the enzyme in the biosynthetic scheme of betalains, overview
-
-
?
additional information
?
-
-
betanidin is a labile compound, overview
-
-
?
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
?
-
-
protocatechuic acid (3,4-dihydroxybenzoic acid) shows little or no activity as a sole substrate
-
-
?
additional information
?
-
-
protocatechuic acid (3,4-dihydroxybenzoic acid) shows little or no activity as a sole substrate
-
-
?
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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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no activity detected with L-Tyr, resorcinol and p-cresol
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additional information
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this enzyme is an o-diphenol oxidase, and no cresolase activity has been found
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additional information
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L-tyrosine and hydroquinone are ineffective as substrates
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additional information
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Ferula sp.
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polyphenol oxidase is a major enzyme responsible for the browning reaction in damaged plant tissues and fruits
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additional information
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Ferula sp.
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substrate specificity, overview, no activity with L-tyrosine
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additional information
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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
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additional information
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PPO oxidizes o-diphenolic compounds to the corresponding o-quinones in the presence of oxygen
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additional information
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PPO shows activity with biphenols, triphenol but not with monophenols
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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the enzyme is considered as defence oxidative enzyme, is vital the physiological defence strategy adapted by plants to insect herbivory and pathogen attack
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additional information
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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
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additional information
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polyphenol oxidase shows no activity with L-tyrosine, digallol, gallic acid, and methyl gallate
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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substrate specificity, overview, no activity with hydroquinic acid, resorcinol, and tyrosine
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additional information
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no activity towards the monophenols p-cresol or L-Tyr
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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no activity with tyrosine, o-methoxyphenol, p-diphenol and m-diphenol
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additional information
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PPO activity increases in the transition from the vegetative stage to the generative stage
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additional information
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phenoloxidase activity is not observed when tyramine and tyrosine (monophenols) were used as substrates
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additional information
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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
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additional information
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Physalis peruviana Colombian ecotype
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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
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additional information
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the enzyme shows no activity towards caffeic acid, DL-Dopa, ferulic acid and phenol
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additional information
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expressionlevels of polyphenol oxidase activity exhibiting enzymes in the organism, overview
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additional information
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oxidation of this and other o-diphenols to o-quinones
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additional information
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substrate specificity of the soluble and particulate enzyme forms, overview
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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the enzyme catalyzes the oxidation of ortho-diphenols to the corresponding quinones
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additional information
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the enzyme catalyzes the oxidation of ortho-diphenols to the corresponding quinones
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additional information
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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
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additional information
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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
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