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Enzyme Nomenclature
Information on EC 1.14.18.1 - tyrosinase
Word Map on EC 1.14.18.1
- 1.14.18.1
- melanoma
- melanin
- melanocyte
-
melanogenesis
- skin
- mushroom
- melanosomes
- copper
- catechols
-
melanogenic
- hair
- hyperpigmentation
-
cosmetic
-
kojic
-
metastatic
- albinism
-
microphthalmia-associated
-
electrode
-
albino
- dopachrome
-
black
-
biosensors
-
polyphenols
-
brown
- eyes
-
tautomerase
- laccase
-
immunotherapy
- vitiligo
-
melanization
-
amelanotic
- hydroquinone
- alpha-msh
- dopamine
-
pigmentary
-
amperometric
- o-quinone
-
melanocortins
-
crest-derived
- food industry
- nutrition
- drug development
- 3,4-dihydroxyphenylalanine
-
hla-a2
- pharmacology
- biotechnology
- agaricus
-
1,1-diphenyl-2-picrylhydrazyl
- agouti
-
decolor
- micrometastases
- hemocyanins
- agriculture
-
copper-binding
-
copper-containing
- bisporus
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
topEC NUMBER 
COMMENTARY 
1.14.18.1
-
RECOMMENDED NAME
GeneOntology No.
tyrosinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 L-dopa + O2 = 2 dopaquinone + 2 H2O
(2)
-
-
-
L-dopa + 1/2 O2 = dopaquinone + H2O
(1b)
-
-
-
L-tyrosine + 1/2 O2 = L-dopa
(1a)
-
-
-
L-tyrosine + O2 = dopaquinone + H2O
(1) overall reaction
-
-
-
L-tyrosine + O2 = dopaquinone + H2O
proposed mechanism of hydroxylation and oxidation of phenols
-
L-tyrosine + O2 = dopaquinone + H2O
proposed interaction of the oxy site effective structure with monophenolic and diphenolic substrates
-
L-tyrosine + O2 = dopaquinone + H2O
2 o-diphenol + O2 = 2 o-quinone + 2 H2O i.e. catecholase activity, proposed mechanism for sequence of hydroxylase and catecholase; monophenol + O2 = o-diphenol + H2O, i.e. cresolase activity, proposed mechanism for sequence of hydroxylase and catecholase
-
L-tyrosine + O2 = dopaquinone + H2O
reaction mechanism of monophenolase and diphenolase activity
-
L-tyrosine + O2 = dopaquinone + H2O
proposed structural reaction mechanism for the monophenolase and diphenolase activity
Mushroom
-
L-tyrosine + O2 = dopaquinone + H2O
catalytic cycle, reaction mechanism, active site structure
-
L-tyrosine + O2 = dopaquinone + H2O
catalytic cycle, reaction mechanism, active site structure
-
L-tyrosine + O2 = dopaquinone + H2O
catalytic cycle, reaction mechanism, active site structure
-
L-tyrosine + O2 = dopaquinone + H2O
catalytic cycle, reaction mechanism, active site structure
-
L-tyrosine + O2 = dopaquinone + H2O
catalytic cycle, reaction mechanism, active site structure
-
L-tyrosine + O2 = dopaquinone + H2O
the active site of the enzyme contains a pair of antiferromagnetically coupled Cu2+ ions in the met form, and during turnover both the reduced and the oxy forms are cyclically produced, the rate-limiting step is associated with cleavage of the peroxide O-O bond, reaction and kinetic mechanism
-
L-tyrosine + O2 = dopaquinone + H2O
catalyzes the hydroxylation of monophenols to o-diphenols (cresolase activity) and the oxidation of o-diphenols to o-quinones (catecholase activity)
-
L-tyrosine + O2 = dopaquinone + H2O
PPO catalyzes the hydroxylation of monophenols to o-diphenols (EC 1.14.18.1) throughout a cresolase/monophenolase activity and a subsequent oxidation of these o-diphenols to the corresponding o-quinones (EC 1.10.3.1) by a catecholase/diphenolase activity
-
L-tyrosine + O2 = dopaquinone + H2O
EC 1.14.18.1, catalyze hydroxylation of monophenols to o-diphenols and their subsequent oxidation to o-quinones
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
SYSTEMATIC NAME
IUBMB Comments
L-tyrosine,L-dopa:oxygen oxidoreductase
A type III copper protein found in a broad variety of bacteria, fungi, plants, insects, crustaceans, and mammals, which is involved in the synthesis of betalains and melanin. The enzyme, which is activated upon binding molecular oxygen, can catalyse both a monophenolase reaction cycle (reaction 1) or a diphenolase reaction cycle (reaction 2). During the monophenolase cycle, one of the bound oxygen atoms is transferred to a monophenol (such as L-tyrosine), generating an o-diphenol intermediate, which is subsequently oxidized to an o-quinone and released, along with a water molecule. The enzyme remains in an inactive deoxy state, and is restored to the active oxy state by the binding of a new oxygen molecule. During the diphenolase cycle the enzyme binds an external diphenol molecule (such as L-dopa) and oxidizes it to an o-quinone that is released along with a water molecule, leaving the enzyme in the intermediate met state. The enzyme then binds a second diphenol molecule and repeats the process, ending in a deoxy state [7].
The second reaction is identical to that catalysed by the related enzyme catechol oxidase (EC 1.10.3.1). However, the latter can not catalyse the hydroxylation or monooxygenation of monophenols.
CAS REGISTRY NUMBER
COMMENTARY
9002-10-2
not distinguished from EC 1.10.3.1
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Ilex argentinus
enzyme is involved in sclerotisation, i.e., the hardening of the chitinous cuticle, and defense
-
-
the Barbados cherry (Malpighia glabra L.) has a very short shelf life under ambient conditions due to skin colour loss and quality deterioration during storage
-
-
Mushroom
strain F6, soil bacterium. The coexistence of this tyrosinase with a laccase in Pseudomonas putida F6 is reported and both activities characterised
-
-
strain MUCL 30555, strain MUCL 29375, strain MUCL 38480, strain MUCL 39533, strain MUCL 38466, strain MUCL 38467, strain I-937, strain ss3
-
-
strain 2-40 isolated from a salt marsh grass, related to Alteromonas
-
-
strain 2-40 isolated from a salt marsh grass, related to Alteromonas
-
-
-
636415, 636423, 636427, 636435, 636436, 672488, 672593, 673001, 674114, 675458, 676133, 684129, 685018, 685452, 685458, 685461, 685462, 685515, 685530, 685604, 685609, 685668, 685671, 685753, 686065, 686532, 687260, 687948, 687996, 688026, 688028, 688030, 688037, 688039, 688041, 688054, 688064, 688592, 689064, 689106, 689118, 689278, 689383, 689413, 689436, 689439, 689440, 689441, 689442, 689702, 695931, 696463, 696563, 696650, 696667, 696694, 696757, 696758, 696844, 697303, 697659, 697741, 697742, 697744, 698040, 698391, 698427, 698442, 699039, 699195, 699239, 699403, 699640, 700322, 700323, 700853, 710912, 711435, 711457, 711476, 712217, 712534, 712597, 713205, 726870, 727168
-
-
white button mushroom, enzyme protects a human lymphoma cell line, Raji cells, against H2O2-induced oxidative damage to cellular DNA
-
-
-
636385, 636401, 636422, 636438, 636444, 672587, 673001, 675298, 684735, 687841, 688569, 689413, 696686, 699403, 700692
-
-
-
636357, 636397, 636398, 636402, 636416, 636417, 636418, 636428, 684270, 685452, 686065, 688041, 688592, 689442, 696686, 700692
-
-
-
-
-
F6 strain wild-type and 2 mutants overproducing melanin, F6-HDO with disrupted homogentisate 1,2-dioxygenase gene and F6-TR with disrupted transcriptional regulator gene
-
-
strain F6, soil bacterium. The coexistence of this tyrosinase with a laccase in Pseudomonas putida F6 is reported and both activities characterised
-
-
var. Naomi, Pizzutello, Rosa Maletto, and PO228, physicochemical properties of the different tomato varieties, overview
-
-
tyrosinases from apple, potato, the white rot fungus Pycnoporus sanguineus, the filamentous fungus Trichoderma reesei and the edible mushroom Agaricus bisporus are compared for their biochemical characteristics
UniProt
strain CBS 357.63, strain CBS 614.73, strain G05, strain W006, strain W 006-2, strain W 3008, strain W28, strain G118, strain G66, strain H2180
-
-
cultivars CA 9632, PH82-2, Nongda 3291, Jing 9428, Nongda 152, Zhongyou 9507, Yumai 70, and Nongda 116
-
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
knockdown of As-pro-PO III expression in pupae using double-stranded RNA results in high pupal mortality and deformed adults that subsequently died following emergence
physiological function
tyrosinases might play a significant role during egg shell formation in Schistosoma japonicum; tyrosinases might play a significant role during egg shell formation in Schistosoma japonicum
physiological function
-
tyrosinases are essential enzymes in melanin biosynthesis and therefore responsible for pigmentation of skin and hair
physiological function
-
tyrosinases are essential enzymes in melanin biosynthesis and therefore responsible for pigmentation of skin and hair
physiological function
-
tyrosinase is a key enzyme in the melanin biosynthesis
physiological function
-
phenoloxidase can serve as a protecting agent against environmental pathogens in Dugesia japonica
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
(1R,3R,4S,5R)-3-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]-1,4,5-trihydroxycyclohexanecarboxylic acid + O2
(1R,3R,4S,5R)-3-[[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy]-1,4,5-trihydroxycyclohexanecarboxylic acid + H2O
-
-
-
-
?
(1S,3R,4S,5R)-4-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]-1,3,5-trihydroxycyclohexanecarboxylic acid + O2
(1S,3R,4S,5R)-4-[[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy]-1,3,5-trihydroxycyclohexanecarboxylic acid + H2O
-
-
-
-
?
(R)-dopaxanthin + dehydroascorbic acid + O2
(R)-dopaxanthin quinone + L-ascorbic acid + H2O
(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-caffeoylisocitric acid + O2
?
-
i.e., E-3-carboxy-2-(3-(3,4-dihydroxyphenyl)prop-2-enoyloxy)pentanedioic acid
-
-
?
2-caffeoylisocitric acid 6-methyl ester + O2
?
-
i.e, E-2-(3-(3,4-dihydroxyphenyl)prop-2-enoyloxy)-3-(methoxycarbonyl)pentanedioic acid
-
-
?
2-hydroxy-1-[[(2E)-3-(4-hydroxy-3-methoxyphenyl)prop-2-enoyl]oxy]propane-1,2,3-tricarboxylic acid + O2
3-C-carboxy-2-deoxy-4-O-[(2E)-3-(3-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]pentaric acid + H2O
-
-
-
-
?
2-O-caffeoylthreonic acid + O2
?
-
i.e., E-2-(3-(3,4-dihydroxyphenyl)prop-2-enoyloxy)-3,4-dihydroxybutanoic acid
-
-
?
2-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]-3,4-dihydroxybutanoic acid + O2
2-[[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy]-3,4-dihydroxybutanoic acid + H2O
-
-
-
-
?
3,4-dihydroxybenzoic acid + 1/2 O2
(3,4-dioxocyclohexa-1,5-dien-1-yl)acetic acid + H2O
-
isoenzymes 1-3, 22%, 13%, and 13% of L-dopa activity respectively
-
?
3,4-dihydroxymandelic acid + O2
?
-
9% of the activity with L-dopa
-
-
?
3,4-dihydroxyphenylacetic acid + 1/2 O2
(3,4-dioxocyclohexa-1,5-dien-1-yl)acetic acid + H2O
-
DHPAA
-
-
?
3,4-dihydroxyphenylpropionic acid + 1/2 O2
3-(3,4-dioxocyclohexa-1,5-dien-1-yl)propanoic acid + H2O
-
DHPPA
-
-
?
3,4-dihydroxyphenylpropionic acid + O2
3-(3,4-dioxocyclohexa-1,5-dien-1-yl)propionic acid
Ilex argentinus
-
-
-
?
3-(3,4-dihydroxyphenyl) propionic acid + 1/2 O2
3-(3,4-dihydroxyphenyl)propionic acid + H2O
-
-
-
?
3-(4-hydroxyphenyl)propionic acid + 1/2 O2
3-(3,4-dihydroxyphenyl)propionic acid + H2O
-
-
-
?
3-chlorophenol + O2
4-chloro-1,2-quinone + H2O
-
20% of 3-chlorophenol is oxidized after 2 h by tyrosinase
4-chloro-1,2-quinone subsequently undergoes a nucleophilic substitution reaction at the chlorine atom by excess phenol to give the corresponding phenol-quinone adduct 4-(3-chlorophenoxy)cyclohexa-3,5-diene-1,2-dione
-
?
3-[2-(3,4-dihydroxyphenyl)ethylaminocarbonyl]-3-methyl-1-(4-acetylphenyl)triazene + O2
(2E)-3-(4-acetylphenyl)-N-[2-(3,4-dioxocyclohexa-1,5-dien-1-yl)ethyl]-1-methyltriaz-2-ene-1-carboxamide + H2O
-
-
-
-
?
3-[2-(3,4-dihydroxyphenyl)ethylaminocarbonyl]-3-methyl-1-(4-ethoxycarbonylphenyl)triazene + O2
ethyl 4-[(1E)-3-[[2-(3,4-dioxocyclohexa-1,5-dien-1-yl)ethyl]carbamoyl]-3-methyltriaz-1-en-1-yl]benzoate + H2O
-
-
-
-
?
3-[2-(3,4-dihydroxyphenyl)ethylaminocarbonyl]-3-methyl-1-(4-tolyl)triazene + O2
(2E)-N-[2-(3,4-dioxocyclohexa-1,5-dien-1-yl)ethyl]-1-methyl-3-(4-methylphenyl)triaz-2-ene-1-carboxamide + H2O
-
-
-
-
?
3-[2-(4-hydroxyphenyl)ethylaminocarbonyl]-3-methyl-1-(4-acetylphenyl)triazene + O2
(2E)-3-(4-acetylphenyl)-1-methyl-N-[2-(4-oxocyclohexa-1,5-dien-1-yl)ethyl]triaz-2-ene-1-carboxamide + H2O
-
-
-
-
?
3-[2-(4-hydroxyphenyl)ethylaminocarbonyl]-3-methyl-1-(4-cyanophenyl)triazene + O2
(2E)-3-(4-cyanophenyl)-1-methyl-N-[2-(4-oxocyclohexa-1,5-dien-1-yl)ethyl]triaz-2-ene-1-carboxamide + H2O
-
-
-
-
?
3-[2-(4-hydroxyphenyl)ethylaminocarbonyl]-3-methyl-1-(4-ethoxycarbonylphenyl)triazene + O2
ethyl 4-[(1E)-3-methyl-3-[[2-(4-oxocyclohexa-1,5-dien-1-yl)ethyl]carbamoyl]triaz-1-en-1-yl]benzoate + H2O
-
-
-
-
?
3-[2-(4-hydroxyphenyl)ethylaminocarbonyl]-3-methyl-1-(4-tolyl)triazene + O2
(2E)-1-methyl-3-(4-methylphenyl)-N-[2-(4-oxocyclohexa-1,5-dien-1-yl)ethyl]triaz-2-ene-1-carboxamide + H2O
-
-
-
-
?
4-chlorocatechol + 1/2 O2
4-chlorocyclohexa-3,5-diene-1,2-dione + H2O
-
-
-
-
?
4-ethylcatechol + 1/2 O2
4-ethylcyclohexa-3,5-diene-1,2-dione + H2O
-
-
-
-
?
4-hydroxybenzaldehyde + 1/2 O2
3,4-dihydroxybenzaldehyde + H2O
-
-
-
?
4-hydroxybenzyl alcohol + O2 + AH2
3,4-dihydroxybenzyl alcohol + H2O + A
-
-
-
?
4-methyl catechol + O2
4-methyl-o-benzoquinone + H2O
-
5% of the activity with L-dopa
-
-
?
4-methylcatechol + O2
?
-
90% activity compared to 3,4-dihydroxyhydrocinnamic acid
-
-
?
4-nitrocatechol + 1/2 O2
4-nitrocyclohexa-3,5-diene-1,2-dione + H2O
-
-
-
-
?
4-t-butylphenol + O2 + AH2
4-t-butyl 1,2-benzoquinone + H2O + A
-
-
-
?
4-tert-butylcatechol + 1/2 O2
4-tert-butylcyclohexa-3,5-diene-1,2-dione + H2O
-
-
-
-
?
4-[(4-methylphenyl)azo]-1,2-benzendiol + 1/2 O2
4-[(E)-(4-methylphenyl)diazenyl]cyclohexa-3,5-diene-1,2-dione + H2O
catechol + 1/2 O2
o-benzoquinone + H2O
-
PPO from butter lettuce shows a higher affinity to 4-methylcatechol than to catechol
-
-
?
DL-DOPA + O2
DL-dopaquinone + H2O
-
78% activity compared to L-DOPA
-
-
?
DL-DOPA + O2
dopaquinone + H2O
-
39% activity at 2.5 mM substrate concentration
-
-
?
esculetin + 1/2 O2
2H-chromene-2,6,7-trione + H2O
-
demonstration, that esculetin is no inhibitor, but a substrate of mushroom polyphenol oxidase (PPO) and horseradish peroxidase (POD)
-
-
?
gallic acid + 1/2 O2
5-hydroxy-3,4-dioxocyclohexa-1,5-diene-1-carboxylic acid + H2O
-
-
-
-
?
gamma-L-glutaminyl-3,4-dihydroxybenzene + O2
gamma-L-glutaminyl-3,4-benzoquinone + H2O
-
-
-
?
gamma-L-glutaminyl-4-hydroxybenzene + O2 + AH2
gamma-L-glutaminyl-3,4-dihydroxybenzene + H2O + A
-
-
-
?
glycyl-glycyl-L-tyrosine + O2
?
-
3.4fold higher activity compared to Tyr
-
-
?
hydroquinone monomethylether + O2
quinone monomethylether
-
-
-
?
L-tyrosine methyl ester + O2
L-DOPA methyl ester + H2O
-
-
-
?
L-tyrosine methyl ester + O2 + AH2
L-dopa methyl ester + H2O + A
-
-
-
-
?
methyl gallate + O2
methyl 5-hydroxy-3,4-dioxocyclohexa-1,5-diene-1-carboxylate + H2O
-
-
-
-
?
N-acetyldopamine quinone + O2
1,2-dehydro-N-acetyldopamine + H2O
-
enzyme has both o-diphenoloxidase and N-acetyldopamine quinone:N-acetyldopamine quinone methide isomerase activity
-
?
N-beta-alanyldopamine + 1/2 O2
N-beta-alanyldopamine quinone + H2O
-
-
-
?
p-hydroxybenzoic acid + O2
?
-
less than 1% activity compared to L-DOPA
-
-
?
phaselic acid + 1/2 O2
(2S)-2-[[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy]butanedioic acid + H2O
-
-
-
-
?
protocatechuic acid + 1/2 O2
3,4-dioxocyclohexa-1,5-diene-1-carboxylic acid + H2O
-
-
-
-
?
protocatechuic aldehyde + 1/2 O2
3,4-dioxocyclohexa-1,5-diene-1-carbaldehyde + H2O
-
-
-
-
?
tert-butylcatechol + 1/2 O2
4-(tert-butyl)benzo-1,2-quinone + H2O
-
hydrophobic substrate
-
-
?
vanillin + O2 + AH2
3,4-dihydroxy-5-methoxybenzaldehyde + H2O + A
-
-
-
-
?
(-)-epicatechin + 1/2 O2
?
-
the major endogenous polyphenol in litchi pericarp
-
-
?
(-)-epicatechin + O2
?
-
119% activity at 2.5 mM substrate concentration
-
-
?
(R)-dopaxanthin + dehydroascorbic acid + O2
(R)-dopaxanthin quinone + L-ascorbic acid + H2O
-
-
-
-
-
(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)-dopaxanthin + dehydroascorbic acid + O2
(R)-dopaxanthin quinone + L-ascorbic acid + H2O
-
-
-
-
-
(RS)-catechin + O2
?
-
isoenzymes 1-3, 96, 104, and 168% of activity with L-dopa respectively
-
-
?
2-O-caffeoylhydroxycitric acid + O2
?
-
i.e., E-3-carboxy-2-(3-(3,4-dihydroxyphenyl)prop-2-enoyloxy)-3-hydroxypentanedioic acid
-
-
?
3,4-dihydroxyphenylacetic acid + O2
?
-
12% of the activity with L-dopa
-
-
?
3,4-dihydroxyphenylacetic acid + O2
?
-
3-methylbenzothyazolinone hydrazone, MBTH, as chromophore coupling agent
-
-
?
4-chlorophenol + O2
4-chloro-1,2-quinone + H2O
-
91% of 4-chlorophenol is oxidized after 2 h by tyrosinase
4-chloro-1,2-quinone subsequently undergoes a nucleophilic substitution reaction at the chlorine atom by excess phenol to give the corresponding phenol-quinone adduct 4-(4-chlorophenoxy)cyclohexa-3,5-diene-1,2-dione
-
?
4-hydroxybenzoic acid + O2 + AH2
3,4-dihydroxybenzoic acid + H2O + A
-
50% of activity with L-dopa
-
?
4-hydroxybenzoic acid + O2 + AH2
3,4-dihydroxybenzoic acid + H2O + A
-
-
-
?
4-hydroxyphenylpropionic acid + O2
?
-
85% activity compared to 3,4-dihydroxyhydrocinnamic acid
-
-
?
4-methoxyphenol + O2
?
-
40% relative activity compared to L-DOPA, weak monophenolase activity
-
-
?
4-methylcatechol + 1/2 O2
4-methyl-1,2-benzoquinone + H2O
-
oxidation of the substrate with NaIO4 in CHCl3, and [P]CHCl3
-
-
?
4-methylcatechol + 1/2 O2
4-methyl-1,2-benzoquinone + H2O
-
diphenolic substrate
-
-
?
4-methylcatechol + 1/2 O2
4-methyl-1,2-benzoquinone + H2O
-
PPO from butter lettuce shows a higher affinity to 4-methylcatechol than to catechol
-
-
?
4-methylcatechol + 1/2 O2
4-methyl-1,2-benzoquinone + H2O
-
efficient diphenolic substrates for cherry PPO
-
-
?
4-methylcatechol + 1/2 O2
4-methyl-1,2-benzoquinone + H2O
-
best substrate
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
good substrate
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
highest activity
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
good substrate
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
good substrate
-
-
?
4-methylcatechol + O2
4-methyl-1,2-benzoquinone + H2O
-
highest activity, 183% activity at 10 mM substrate concentration
-
-
?
4-methylcatechol + O2
4-methyl-o-benzoquinone + H2O
-
-
-
?
4-methylcatechol + O2
4-methyl-o-benzoquinone + H2O
-
-
-
?
4-methylcatechol + O2
4-methyl-o-benzoquinone + H2O
-
catecholase/cresolase activity ratio of 41
-
?
4-methylcatechol + O2
4-methyl-o-benzoquinone + H2O
-
-
-
?
4-methylcatechol + O2
4-methyl-o-benzoquinone + H2O
-
-
-
?
4-tert-butylcatechol + 1/2 O2
4-(tert-butyl)benzo-1,2-quinone + H2O
-
-
-
?
4-[(4-methylphenyl)azo]-1,2-benzendiol + 1/2 O2
4-[(E)-(4-methylphenyl)diazenyl]cyclohexa-3,5-diene-1,2-dione + H2O
-
-
-
-
?
4-[(4-methylphenyl)azo]-1,2-benzendiol + 1/2 O2
4-[(E)-(4-methylphenyl)diazenyl]cyclohexa-3,5-diene-1,2-dione + H2O
-
synthetic substrate
-
-
?
4-[(4-methylphenyl)azo]-phenol + O2 + AH2
4-[(4-methylbenzo)azo]-1,2-benzendiol + H2O + A
-
-
-
-
?
4-[(4-methylphenyl)azo]-phenol + O2 + AH2
4-[(4-methylbenzo)azo]-1,2-benzendiol + H2O + A
-
synthetic substrate
-
-
?
alpha-methyl-DL-tyrosine + O2 + AH2
N-methyl-DL-dopa + H2O + A
-
-
-
-
?
caffeic acid + 1/2 O2
caffeoyl quinone + H2O
-
17% of activity with L-dopa
-
?
caffeic acid + 1/2 O2
caffeoyl quinone + H2O
-
diphenolic caffeic acid is oxidized relatively fast by all tyrosinases, except only moderately by tyrosinase from Pycnoporus sanguineus
-
-
?
caffeic acid + 1/2 O2
caffeoyl quinone + H2O
-
-
-
?
caffeic acid + O2
caffeoyl quinone + H2O
-
60.9% activity compared to L-DOPA
-
-
?
caffeic acid + O2
caffeoyl quinone + H2O
-
50% activity compared to catechol
-
-
?
caffeic acid + O2
caffeoyl quinone + H2O
-
31% activity at 2.5 mM substrate concentration
-
-
?
caffeic acid + O2
caffeoyl quinone + H2O
-
31% activity at 2.5 mM substrate concentration
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
pyrogallol and catechol are best substrates for catalysis and inactivation
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
24% of the activity with L-dopa
-
-
?
catechol + 1/2 O2
1,2-benzoquinone + H2O
-
efficient diphenolic substrates for cherry PPO
-
-
?