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Information on EC 1.14.18.1 - tyrosinase and Organism(s) Mus musculus and UniProt Accession P11344
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1.14.18.1 tyrosinaseIUBMB Comments
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 . 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.
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Word Map
- 1.14.18.1
- melanin
- melanoma
- melanocyte
-
melanogenesis
- melanosomes
-
cosmetic
-
microphthalmia-associated
- hyperpigmentation
-
melanogenic
- catechols
- polyphenols
-
kojic
- copper
- albinism
-
whitening
- hair
-
keratinocytes
-
albino
- flavonoid
-
biosensors
- o-quinone
-
amperometric
-
phytochemical
-
pigmentary
- vitiligo
-
tautomerase
- laccase
- abts
- alpha-msh
-
melanization
-
depigmentation
- hydroquinone
-
electrode
-
melanocortins
-
2,2-diphenyl-1-picrylhydrazyl
-
copper-binding
- polyphenoloxidase
-
frap
- biotechnology
- agriculture
- pharmacology
-
hla-a2
- nutrition
-
1,1-diphenyl-2-picrylhydrazyl
- food industry
- hemocyanins
- environmental protection
- l-3,4-dihydroxyphenylalanine
-
crest-derived
- drug development
- microphthalmia
- medicine
- agaricus
- butyrylcholinesterase
-
melanoma-associated
-
copper-containing
-
decolor
- bisporus
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
tyrosinase, monophenolase, oxygen oxidoreductase, phenol oxidases, murine tyrosinase, melc2, o-diphenol oxidase, monophenol oxidase, met-tyrosinase, jrppo1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
catechol oxidase
-
-
-
-
catecholase
-
-
-
-
chlorogenic acid oxidase
-
-
-
-
chlorogenic oxidase
-
-
-
-
cresolase
-
-
-
-
Diphenol oxidase
-
-
-
-
dopa oxidase
monophenol dihydroxyphenylalanine:oxygen oxidoreductase
-
-
-
-
monophenol monooxidase
-
-
-
-
monophenol oxidase
-
-
-
-
monophenol, dihydroxy-L-phenylalanine oxygen oxidoreductase
-
-
-
-
monophenolase
-
-
-
-
N-acetyl-6-hydroxytryptophan oxidase
-
-
-
-
o-diphenol oxidase
-
-
-
-
o-diphenol oxidoreductase
-
-
-
-
o-diphenol:O2 oxidoreductase
-
-
-
-
o-diphenol:oxygen oxidoreductase
-
-
-
-
o-diphenolase
-
-
-
-
phenol oxidase
-
-
-
-
phenolase
-
-
-
-
polyaromatic oxidase
-
-
-
-
polyphenol oxidase
-
-
-
-
polyphenolase
-
-
-
-
pyrocatechol oxidase
-
-
-
-
tyrosinase
tyrosine-dopa oxidase
-
-
-
-
dopa oxidase
-
-
-
-
tyrosinase
-
-
-
-
tyrosinase
-
this enzyme is able to catalyse two different reactions: the hydroxylation of monophenols to o-diphenols (monophenolase or cresolase activity, EC 1.14.18.1), and the oxidation of o-diphenols to o-quinones (diphenolase or catechol oxidase activity, EC 1.10.3.1)
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -
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
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
L-tyrosine + O2 + AH2
L-dopa + H2O + A
radioactive substrate L-[3,5-3H]-tyrosine, specific activity 50 Ci/mmol
-
-
?
3,4-dihydroxyphenylethanol + O2
2-(3,4-dioxocyclohexa-1,5-dien-1-yl)ethanol + H2O
-
-
-
-
r
3,4-dihydroxyphenylglycol + O2
2-(3,4-dioxocyclohexa-1,5-dien-1-yl)glycol + H2O
-
-
-
-
r
L-3,4-dihydroxyphenylalanine + 1/2 O2
L-dopaquinone + H2O
-
-
-
-
?
additional information
?
-
-
catalyzing the rate-limiting step for melanin biosynthesis
-
-
?
L-tyrosine + O2 + AH2
L-3,4-dihydroxyphenylalanine + H2O + A
-
rate-limiting enzyme in melanin biosynthesis
-
-
?
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
catalyzing the rate-limiting step for melanin biosynthesis
-
-
?
L-tyrosine + O2 + AH2
L-3,4-dihydroxyphenylalanine + H2O + A
-
rate-limiting enzyme in melanin biosynthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
the active site of the tyrosinase model shows the same structural conformation as in sTyr and ibCO, where two copper ions are coordinated by three histidines each, forming a binuclear type 3 copper site similar to that of the template structure
copper
-
copper transporter ATP7A localizes to melanosomes in wildtype melanocytes. Copper restores in vitro tyrosinase activity in melanosomes of BLOC-1-deficient melanocytes, immunofluorescence microscopy
Cu2+
-
tyrosinases is a copper-containing enzyme belonging to the type 3 copper protein family
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(2,4-dihydroxyphenyl)-3-(2,4-dimethoxy-3-methylphenyl)propane
-
tyrosinase inhibitor with strong depigmenting effects, found in the medicinal plant Dianella ensifolia. 22times more potent than kojic acid
gallic acid
-
significantly inhibited tyrosinase. Isolated from Radix polygoni multiflori, a herb used effectively to prevent graying and to treat skin depigmentation diseases in traditional Chinese medicine
p-hydroxybenzyl alcohol
-
p-hydroxybenzyl alcohol, inhibitory effect on tyrosinase activity and melanogenesis. p-hydroxybenzyl alcohol exhibits an inhibitory effect on melanogenesis in mouse melanocytes at noncytotoxic concentrations. The results indicate that no significant difference is observed in tyrosinase gene expression between the p-hydroxybenzyl alcohol-treated and non-treated cells. Thus, it is concluded that no repression of tyrosinase gene is induced by p-hydroxybenzyl alcohol
paeonol
-
effects of paeonol on cell growth of B16F10 melanoma cells are shown. The effect of a high dose of paeonol (200 microM) is better than that of 2 microM hydroquinone (HQ), which acts as a positive agent. Paeonol down-regulates tyrosinase expression at mRNA and protein level. And paeonol inhibits MITF mRNA expression in B16F10 melanoma cells und the phosphorylation of CREB
terrein
-
examines the effects of a combination of 2-butyl-5-hydroxyphenyl 3-(3,4-dihydroxyphenyl)propanoate with terrein, an agent that down-regulates microphthalmia-associated transcription factor. Cells co-treated with 2-butyl-5-hydroxyphenyl 3-(3,4-dihydroxyphenyl)propanoate and terrein show much less pigmentation than cells treated with 2-butyl-5-hydroxyphenyl 3-(3,4-dihydroxyphenyl)propanoate or terrein alone
(2E)-3-(3,4-dihydroxyphenyl)-N-[2-(1H-indol-3-yl)ethyl]prop-2-enamide
-
14% inhibition at 0.1 mM
(2E)-3-(3,4-dihydroxyphenyl)-N-[2-(1H-indol-3-yl)ethyl]prop-2-enamide
-
2% inhibition at 0.1 mM
(2E)-3-(3,4-dihydroxyphenyl)-N-[2-(4-hydroxyphenyl)ethyl]prop-2-enamide
-
30% inhibition at 0.1 mM
(2E)-3-(3,4-dihydroxyphenyl)-N-[2-(4-hydroxyphenyl)ethyl]prop-2-enamide
-
15% inhibition at 0.1 mM
(2E)-3-(3,4-dihydroxyphenyl)-N-[2-(5-hydroxy-1H-indol-3-yl)ethyl]prop-2-enamide
-
73% inhibition at 0.1 mM
(2E)-3-(3,4-dihydroxyphenyl)-N-[2-(5-hydroxy-1H-indol-3-yl)ethyl]prop-2-enamide
-
55% inhibition at 0.1 mM
(2E)-3-(3,4-dihydroxyphenyl)-N-[2-(5-methoxy-1H-indol-3-yl)ethyl]prop-2-enamide
-
4% inhibition at 0.1 mM
(2E)-3-(3,4-dihydroxyphenyl)-N-[2-(5-methoxy-1H-indol-3-yl)ethyl]prop-2-enamide
-
1% inhibition at 0.1 mM
(2E)-3-(4-hydroxy-3-methoxyphenyl)-N-[2-(1H-indol-3-yl)ethyl]prop-2-enamide
-
4% inhibition at 0.1 mM
(2E)-3-(4-hydroxy-3-methoxyphenyl)-N-[2-(1H-indol-3-yl)ethyl]prop-2-enamide
-
13% inhibition at 0.1 mM
(2E)-N-[2-(5-hydroxy-1H-indol-3-yl)ethyl]-3-(4-hydroxy-3-methoxyphenyl)prop-2-enamide
-
29% inhibition at 0.1 mM
(2E)-N-[2-(5-hydroxy-1H-indol-3-yl)ethyl]-3-(4-hydroxy-3-methoxyphenyl)prop-2-enamide
-
48% inhibition at 0.1 mM
2,4-dihydroxy-N-[2-(5-hydroxy-1H-indol-3-yl)ethyl]benzamide
-
50% inhibition at 0.1 mM
2,4-dihydroxy-N-[2-(5-hydroxy-1H-indol-3-yl)ethyl]benzamide
-
39% inhibition at 0.1 mM
3,4-dihydroxy-N-[2-(5-hydroxy-1H-indol-3-yl)ethyl]benzamide
-
43% inhibition at 0.1 mM
3,4-dihydroxy-N-[2-(5-hydroxy-1H-indol-3-yl)ethyl]benzamide
-
48% inhibition at 0.1 mM
4-hydroxy-N-[2-(5-hydroxy-1H-indol-3-yl)ethyl]-3-methoxybenzamide
-
16% inhibition at 0.1 mM
4-hydroxy-N-[2-(5-hydroxy-1H-indol-3-yl)ethyl]-3-methoxybenzamide
-
32% inhibition at 0.1 mM
4-hydroxy-N-[2-(5-hydroxy-1H-indol-3-yl)ethyl]benzamide
-
9% inhibition at 0.1 mM
4-hydroxy-N-[2-(5-hydroxy-1H-indol-3-yl)ethyl]benzamide
-
31% inhibition at 0.1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Aloe-emodin
-
isolated from Radix polygoni multiflori, a herb used effectively to prevent graying and to treat skin depigmentation diseases in traditional Chinese medicine. Shows slightly melanogenesis stimulation activities
2,3,5,4'-tetrahydroxystilbene-2-O-beta-D-glucoside
-
THSG, one of six compounds isolated from Radix polygoni multiflori, a herb used effectively to prevent graying and to treat skin depigmentation diseases in traditional Chinese medicine. Shows significant melanogenesis stimulation activities and significant activation effects on B16 cell tyrosinase. THSG is a potent activator of tyrosinase
2,3,5,4'-tetrahydroxystilbene-2-O-beta-D-glucoside
-
THSG, tyrosinase activator isolated from Radix Polygoni multiflori. It significantly increases the activity of murine tyrosinase and stimulates melanin biosynthesis in B16 melanoma cells. THSG is found to be non-cytotoxic to B16 melanoma cells at a concentration of 0.1-12.5 microg/ml
chrysophanol
-
isolated from Radix polygoni multiflori, a herb used effectively to prevent graying and to treat skin depigmentation diseases in traditional Chinese medicine. Shows significant melanogenesis stimulation activities
emodin
-
isolated from Radix polygoni multiflori, a herb used effectively to prevent graying and to treat skin depigmentation diseases in traditional Chinese medicine. Shows significant melanogenesis stimulation activities
L-Dopa
-
low-mobility enzyme form shows an absolute requirement of L-dopa for tyrosine hydroxylation in contrast to high-mobility enzyme form
physcion
-
isolated from Radix polygoni multiflori, a herb used effectively to prevent graying and to treat skin depigmentation diseases in traditional Chinese medicine. Shows slightly melanogenesis stimulation activities
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.028
(2E)-3-(3,4-dihydroxyphenyl)-N-[2-(5-hydroxy-1H-indol-3-yl)ethyl]prop-2-enamide
Mus musculus
-
-
0.216
(2E)-N-[2-(5-hydroxy-1H-indol-3-yl)ethyl]-3-(4-hydroxy-3-methoxyphenyl)prop-2-enamide
Mus musculus
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
tryrosinase is present but inactive in BLOC-1-deficient melanocytes
-
-
to catalyse melanin synthesis, tyrosinase is subsequently reloaded with copper within specialized organelles called melanosomes, immunofluorescence microscopy
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
tyrosinases are essential enzymes in melanin biosynthesis and therefore responsible for pigmentation of skin and hair
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TYRO_MOUSE
533
1
60606
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58000
corresponds to the fully deglycosylated protein backbone. Western blot analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
additional information
-
isoenzymes with molecular weights of 58000 Da and 68000 Da are highly resistant to proteinase K digestion
glycoprotein
-
isoenzymes are most probably due to post-translational glycosylation, isoenzymes are immunological similar and possess the same amino acid content, 6 potential glycosylation sites in cDNA
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
M374G
potential to delete the enzymatic activity of Tyr. Major effect on the active site: the packing density of this normally rigid environment is significantly lowered when the original amino acid is mutated to the smaller glycine because the missing side chain of G374 can neither anchor the loop nor orient the side chain of H367
M374G/S375G
Tyr-GG double mutant, potential to delete the enzymatic activity of Tyr. The M374G/S375G mutation, designated Tyr-GG, replaces two residues present in mTyr by the equivalent residues in mTyrp1 and could potentially modify the enzymatic properties of the protein, when compared with wild-type Tyr. Analysis of the behaviour of the individual mutants M374G and S374G indicates that loss of enzymatic activity in Tyr-GG is mostly because of the M374G mutation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
high-mobility tyrosinase form, ammonium sulfate, hydroxyapatite, gel filtration, low-mobility tyrosinase form, DEAE-Sephadex, partial purification
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the wild-type Tyr and mutant constructs are transiently expressed in human embryonic kidney (HEK) 293T cells for functional analysis
in vitro transcription translation of 2 different cDNA clones encoding tyrosinase 1 and 2
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
pharmacology
-
results of low cytotoxicity, high inhibition of melanin synthesis and lack of effect on gene expression suggest that p-hydroxybenzyl alcohol can be a potential agent for skin lightening to be used in cosmetic products
drug development
-
activators of tyrosinase with stimulatory effects on melanogenesis are beneficial for the treatment of hypopigmentation diseases. 2,3,5,4'-tetrahydroxystilbene-2-O-beta-D-glucoside is a potent tyrosinase activator and stimulator of melanogenesis with potential for the treatment of hypopigmentation disease
drug development
-
the suppression of tyrosinase activity by 2-butyl-5-hydroxyphenyl 3-(3,4-dihydroxyphenyl)propanoate and the inhibition of tyrosinase production by terrein appear to be an optimal combination for skin whitening
drug development
-
tyrosinase is a key enzyme involved in melanin biosynthesis and of particular interest in repigmentation research
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Terao, M.; Tabe, L.; Garattini, E.; Sartori, D.; Studer, M.; Mintz, B.
Isolation and characterization of variant cDNAs encoding mouse tyrosinase
Biochem. Biophys. Res. Commun.
159
848-853
1989
Mus musculus
Yurkow, E.J.; Laskin, J.D.
Purification of tyrosinase to homogeneity based on its resistance to sodium dodecyl sulfate-proteinase K digestion
Arch. Biochem. Biophys.
275
122-129
1989
Mus musculus
Jimenez, M.; Maloy, W.L.; Hearing, V.J.
Specific identification of an authentic clone for mammalian tyrosinase
J. Biol. Chem.
264
3397-3403
1989
Mus musculus
Takeuchi, S.; Yamamoto, H.; Takeuchi, T.
Expression of tyrosinase gene in amelanotic mutant mice
Biochem. Biophys. Res. Commun.
155
470-475
1988
Mus musculus
Hearing, V.J.
Mammalian monophenol monooxygenase (tyrosinase): purification, properties, and reactions catalyzed
Methods Enzymol.
142
154-165
1987
Mammalia, Mus musculus
Menon, I.A.; Haberman, H.F.
Activation of tyrosinase in microsomes and melanosomes from B16 and Harding-Passey melanomas
Arch. Biochem. Biophys.
137
231-242
1970
Mus musculus
Yamamoto, H.; Takeuchi, S.; Kudo, T.; Makino, K.; Nakata, A.; Shinoda, T.; Takeuchi, T.
Cloning and sequencing of mouse tyrosinase cDNA
Jpn. J. Genet.
62
271-274
1987
Mus musculus
-
Hearing, V.J.; Ekel, T.M.; Montague, P.M.; Hearing, E.D.; Nicholson, J.M.
Mammalian tyrosinase: isolation by a simple new procedure and characterization of its steric requirements for cofactor activity
Arch. Biochem. Biophys.
185
407-418
1978
Mus musculus
Kwon, B.S.; Walkulchik, M.; Haq, A.K.; Halaban, R.; Kestler, D.
Sequence analysis of mouse tyrosinase cDNA and the effect of melanotropin on its gene expression
Biochem. Biophys. Res. Commun.
153
1301-1309
1988
Mus musculus
Muller, G.; Ruppert, S.; Schmid, E.; Schutz, G.
Functional analysis of alternatively spliced tyrosinase gene transcripts
EMBO J.
7
2723-2730
1988
Mus musculus
Fuller, B.B.; Lundsford, J.B.; Iman, D.S.
alpha-Melanocyte-stimulating hormone regulation of tyrosinase in Cloudman S-91 mouse melanoma cell cultures
J. Biol. Chem.
262
4024-4033
1987
Mus musculus
Jimenez-Cervantes, C.; Garcia-Borron, J.C.; Valverde, P.; Solano, F.; Lozano, J.A.
Tyrosinase isoenzymes in mammalian melanocytes. 1. Biochemical characterization of two melanosomal tyrosinases from B16 mouse melanoma
Eur. J. Biochem.
217
549-556
1993
Mus musculus
Jimenez-Cervantes, C.; Garcia-Borron, J.C.; Lozano, J.A.; Solano, F.
Effect of detergents and endogenous lipids on the activity and properties of tyrosinase and its related proteins
Biochim. Biophys. Acta
1243
421-430
1995
Mus musculus
Bu, J.; Ma, P.C.; Chen, Z.Q.; Zhou, W.Q.; Fu, Y.J.; Li, L.J.; Li, C.R.
Inhibition of MITF and tyrosinase by paeonol-stimulated JNK/SAPK to reduction of phosphorylated CREB
Am. J. Chin. Med.
36
245-263
2008
Mus musculus
Liu, S.H.; Pan, I.H.; Chu, I.M.
Inhibitory effect of p-hydroxybenzyl alcohol on tyrosinase activity and melanogenesis
Biol. Pharm. Bull.
30
1135-1139
2007
Agaricus bisporus, Mus musculus
Nesterov, A.; Zhao, J.; Minter, D.; Hertel, C.; Ma, W.; Abeysinghe, P.; Hong, M.; Jia, Q.
1-(2,4-dihydroxyphenyl)-3-(2,4-dimethoxy-3-methylphenyl)propane, a novel tyrosinase inhibitor with strong depigmenting effects
Chem. Pharm. Bull.
56
1292-1296
2008
Agaricus bisporus, Mus musculus
Guan, S.; Su, W.; Wang, N.; Li, P.; Wang, Y.
Effects of radix polygoni multiflori components on tyrosinase activity and melanogenesis
J. Enzyme Inhib. Med. Chem.
23
252-255
2008
Agaricus bisporus, Mus musculus
Kim, D.S.; Lee, S.; Lee, H.K.; Park, S.H.; Ryoo, I.J.; Yoo, I.D.; Kwon, S.B.; Baek, K.J.; Na, J.I.; Park, K.C.
The hypopigmentary action of KI-063 (a new tyrosinase inhibitor) combined with terrein
J. Pharm. Pharmacol.
60
343-348
2008
Agaricus bisporus, Mus musculus
Setty, S.R.; Tenza, D.; Sviderskaya, E.V.; Bennett, D.C.; Raposo, G.; Marks, M.S.
Cell-specific ATP7A transport sustains copper-dependent tyrosinase activity in melanosomes
Nature
454
1142-1146
2008
Mus musculus
Guan, S.; Su, W.; Wang, N.; Li, P.; Wang, Y.
A potent tyrosinase activator from Radix Polygoni multiflori and its melanogenesis stimulatory effect in B16 melanoma cells
Phytother. Res.
22
660-663
2008
Agaricus bisporus, Mus musculus
Schweikardt, T.; Olivares, C.; Solano, F.; Jaenicke, E.; Garcia-Borron, J.C.; Decker, H.
A three-dimensional model of mammalian tyrosinase active site accounting for loss of function mutations
Pigment Cell Res.
20
394-401
2007
Mus musculus (P11344), Mus musculus
Yamazaki, Y.; Kawano, Y.; Yamanaka, A.; Maruyama, S.
N-[(dihydroxyphenyl)acyl]serotonins as potent inhibitors of tyrosinase from mouse and human melanoma cells
Bioorg. Med. Chem. Lett.
19
4178-4182
2009
Homo sapiens, Mus musculus
EXTERNAL LINKS (specific for EC-Number 1.14.18.1)
Transporter Classification Database (TCDB): 9.B.423.1.1
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