1.14.18.1: tyrosinase
This is an abbreviated version!
For detailed information about tyrosinase, go to the full flat file.
Word Map on EC 1.14.18.1
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1.14.18.1
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melanin
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melanoma
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melanocyte
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melanogenesis
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melanosomes
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cosmetic
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microphthalmia-associated
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hyperpigmentation
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melanogenic
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catechols
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polyphenols
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kojic
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copper
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albinism
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whitening
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hair
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keratinocytes
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albino
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flavonoid
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biosensors
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o-quinone
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amperometric
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phytochemical
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pigmentary
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vitiligo
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tautomerase
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laccase
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abts
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alpha-msh
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melanization
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depigmentation
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hydroquinone
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electrode
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melanocortins
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2,2-diphenyl-1-picrylhydrazyl
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copper-binding
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polyphenoloxidase
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frap
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biotechnology
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agriculture
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pharmacology
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hla-a2
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nutrition
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1,1-diphenyl-2-picrylhydrazyl
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food industry
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hemocyanins
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environmental protection
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l-3,4-dihydroxyphenylalanine
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crest-derived
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drug development
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microphthalmia
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medicine
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agaricus
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butyrylcholinesterase
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melanoma-associated
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copper-containing
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decolor
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bisporus
- 1.14.18.1
- melanin
- melanoma
- melanocyte
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melanogenesis
- melanosomes
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cosmetic
-
microphthalmia-associated
- hyperpigmentation
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melanogenic
- catechols
- polyphenols
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kojic
- copper
- albinism
-
whitening
- hair
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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
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copper-binding
- polyphenoloxidase
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frap
- biotechnology
- agriculture
- pharmacology
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hla-a2
- nutrition
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1,1-diphenyl-2-picrylhydrazyl
- food industry
- hemocyanins
- environmental protection
- l-3,4-dihydroxyphenylalanine
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crest-derived
- drug development
- microphthalmia
- medicine
- agaricus
- butyrylcholinesterase
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melanoma-associated
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copper-containing
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decolor
- bisporus
Reaction
2 L-dopa
+
Synonyms
AbPPO1, AbPPO4, AbTYR, aurone synthase, catalase-phenol oxidase, catechol oxidase, catecholase, CATPO, chlorogenic acid oxidase, chlorogenic oxidase, cresolase, cresolase/monophenolase, CsPPO, CZA14Tyr, deoxy-tyrosinase, dihydroxy-L-phenylalanine:oxygen oxidoreductase, Diphenol oxidase, diphenolase, dopa oxidase, EC 1.10.3.1, EC 1.14.17.2, Hc-derived phenoloxidase, Hc-phenoloxidase, HcPO, HdPO, hemocyanin-derived phenoloxidase, jrPPO1, jrTYR, L-DOPA monophenolase, L-DOPA oxidase, L-DOPA:oxygen oxidoreductase, L-tyrosine hydroxylase, MdPPO1, melC2, MelC2 tyrosinase, met-tyrosinase, monophenol dihydroxyphenylalanine:oxygen oxidoreductase, monophenol monooxidase, monophenol monooxygenase, monophenol monoxygenase, monophenol oxidase, monophenol oxygen oxidoreductase, monophenol, 3,4-dihydroxy L-phenylalanine (L-DOPA):oxygen oxidoreductase, monophenol, dihydroxy-L-phenylalanine oxygen oxidoreductase, monophenol, dihydroxy-L-phenylalanine:oxygen oxidoreductase, monophenol, dihydroxyphenylalanine:oxygen oxidoreductase, monophenol, L-Dopa: oxidoreductase, monophenol, L-DOPA: oxygen oxidoreductase, monophenol, o-diphenol: oxygen oxidoreductase, monophenol, o-diphenol:O2 oxidoreductase, monophenol, o-diphenol:oxygen oxido-reductase, monophenol, o-diphenol:oxygen oxidoreductase, monophenol, polyphenol oxidase, monophenol: dioxygen oxidoreductases, hydroxylating, monophenolase, monphenol mono-oxygenase, More, mTyr, murine tyrosinase, mushroom tyrosinase, mushroom tyrosine, N-acetyl-6-hydroxytryptophan oxidase, o-diphenol oxidase, o-diphenol oxidoreductase, o-diphenol oxygen oxidoreductase, o-diphenol: O2 oxidoreductase, o-diphenol: oxidoreductase, o-diphenol:O2 oxidoreductase, o-diphenol:oxygen oxidoreductase, o-diphenolase, OCA1, Orf13, oxygen oxidoreductase, phenol oxidase, phenol oxidases, phenolase, phenoloxidase, PO, polyaromatic oxidase, polyphenol oxidase, polyphenol oxidase 3, polyphenol oxidase 4, polyphenol oxidase B, polyphenolase, polyphenoloxidase, PotPPO, PPO, PPO 3, PPO B, PPO1, PPO2, PPO3, pro-PO III, prophenoloxidase III, pyrocatechol oxidase, SPRTyr, ST94, ST94t, tryosinase, tryrosinase, TY, tyr, TYR1, TYR2, tyrA, TyrBm, tyrosinase, tyrosinase 2, tyrosinase 4, tyrosinase diphenolase, tyrosine-dopa oxidase
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1.14.18.1 tyrosinaseAdvanced search results
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Metals Ions on EC 1.14.18.1 - tyrosinase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
boron
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boron in an essential micronutrient required for growth and development of plants. Boron treatments: Germination of maize seeds is not effected by boron concentrations up to 10 mM but decreased by 20 mM boron. Excess boron lowers the PPO activity in seed tissues during germination of maize. Time course of PPO activities in embryo and endosperm of maize seeds treated with boron during and following germination is shown
Ca2+
Co2+
copper
Cu2+
Fe3+
H2O2
K+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
copper
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copper containing enzyme. Bathochromic shift of selected phenylethanoid glycosides (0.01 mM) in the presence of CuSO4 (0.05 mM)
copper
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0.22% copper, probably 4 copper atoms per enzyme molecule
copper
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inhibitors such as sodium diethyl dithiocarbamate and thiourea, which combine with the copper moiety in the enzyme, are generally potent inhibitors of PPO. The inhibitors are copper-chelating agents and they suppress browning activities in which copper is directly involved in the oxidation of phenolic compounds
copper
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copper transporter ATP7A localizes to melanosomes in wildtype melanocytes. Copper restores in vitro tyrosinase activity in melanosomes of BLOC-1-deficient melanocytes, immunofluorescence microscopy
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
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enzyme contains a binuclear copper complex at the active site which is responsible for the interaction with phenolic substrates and the binding and activation of molecular O2, depending on the oxidation state of the copper, 3 different forms are known: Met-, oxy-, and deoxytyrosinase
copper
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1H-NMR spectra, each copper atom is coordinated by the Nepsilon atoms of 3 histidine residues
copper
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first presention of a complete quantitative analysis of the XANES part of the XAS spectrum of a binuclear copper site
copper
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the activator protein ORF378 may facilitate the incorporation of Cu(II) into apotyrosinase
copper
correct copper concentration in the growth medium is critical for the expression of this copper containing enzyme. Optimization of the copper concentration and the expression conditions lead to a 10fold increase in the expression level of processed active histidine tagged TYR2
Cu2+
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a copper-containing enzyme
Cu2+
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bound to the enzyme, the central domain contains two copper binding sites, mettyrosinase, the resting form of tyrosinase, contains two tetragonal Cu(II) ions antiferromagnetically coupled through an endogenous bridge, although hydroxide exogenous ligands other than peroxide are bound to the copper site, the exogenous oxygen molecule is bound as peroxide and bridges the two copper centers
Cu2+
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a binuclear copper enzyme. In the catalytic site of TYR, the bivalent copper ions are chelated by three individual histidine residues, overview
Cu2+
a copper-containing enzyme, the catalytic centre of tyrosinase has two copper atoms each coordinated with three histidine residues. These copper atoms have different oxidation and coordination modes, depending on the enzymatic form: Cu2+Cu2+ in Em (metatyrosinase), Cu1+Cu1+ in Ed (deoxytyrosinase), and Cu2+Cu2+O22- in Eox (oxytyrosinase)
Cu2+
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binding of dioxygen to the two copper atoms (usually identified as CuA and CuB) located in the active site, inuclear copper-binding site of Agaricus bisporus tyrosinase, overview
Cu2+
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the enzyme's catalytic site contains two divalent copper cations chelated by His61, His85, His94, His259, His263 and His294 catalytic amino acid residue
Cu2+
required, activates, copper is an essential constituent of tyrosinase active site. Tyrosinase is a type-3 copper protein with two putative conserved copper-binding sites comprising of six histidines, tyrosinase has a di-copper active site
Cu2+
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bound to the enzyme, the central domain contains two copper binding sites, mettyrosinase, the resting form of tyrosinase, contains two tetragonal Cu(II) ions antiferromagnetically coupled through an endogenous bridge, although hydroxide exogenous ligands other than peroxide are bound to the copper site, the exogenous oxygen molecule is bound as peroxide and bridges the two copper centers
Cu2+
a copper-containing enzyme, copper content of 0.880 atom/molecule of protein in recombinant refolded enzyme
Cu2+
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tyrosinases is a copper-containing enzyme belonging to the type 3 copper protein family
Cu2+
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bound to the enzyme, the central domain contains two copper binding sites, mettyrosinase, the resting form of tyrosinase, contains two tetragonal Cu(II) ions antiferromagnetically coupled through an endogenous bridge, although hydroxide exogenous ligands other than peroxide are bound to the copper site, the exogenous oxygen molecule is bound as peroxide and bridges the two copper centers
Cu2+
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tyrosinases is a copper-containing enzyme belonging to the type 3 copper protein family
Cu2+
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a copper-containing enzyme, copper is an important element for tyrosinase activity, binding to tyrosinase depends on pH in melanosomes
Cu2+
a copper-containing enzyme, the two copper ions (CuA and CuB) essential for activity
Cu2+
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a copper-containing enzyme. During the catalytic cycle, the dinuclear copper center passes through three different oxidation states. In the resting met form, the copper atoms (CuII) are bridged by a hydroxide ion or water molecule. The deoxy form represents the reduced (CuI) state, which is converted into the reactive oxy form upon oxygen binding. In the crystal structure, CuA exhibits an intermediate geometry between a distorted tetrahedron and a trigonal bipyramid with one unoccupied coordination site, whereas CuB exhibits an almost perfect tetrahedral geometry with the solvent molecule in apical position
Cu2+
a type-3 copper enzyme containing two copper ions, each coordinated by three histidine residues
Cu2+
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a copper-containing enzyme, exogenous Cu2+ inhibits the enzyme by avbout 55% at 1-10 mM
Cu2+
a copper-containing enzyme, two Cu2+ ions CuA and CuB, copper domain structure with the conserved histidines coordinating CuA (His86, His107 and His116) and CuB (His238, His242 and His272) and the positions of the mutated residues, namely the two activity controllers alanine (Ala239) and leucine (Leu243), the water keeper glutamic acid (Glu234) and the gatekeeper phenylalanine (Phe259), overview
Cu2+
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tyrosinases is a copper-containing enzyme belonging to the type 3 copper protein family
Cu2+
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bound to the enzyme, the central domain contains two copper binding sites, mettyrosinase, the resting form of tyrosinase, contains two tetragonal Cu(II) ions antiferromagnetically coupled through an endogenous bridge, although hydroxide exogenous ligands other than peroxide are bound to the copper site, the exogenous oxygen molecule is bound as peroxide and bridges the two copper centers
Cu2+
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a type 3 copper enzyme possessing two copper ions in the active site
Cu2+
tyrosinase is a member of the type 3 copper enzyme family, two Cu2+ ions serveas the major cofactors within the active site
Cu2+
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tyrosinases is a copper-containing enzyme belonging to the type 3 copper protein family
Cu2+
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bound to the enzyme, presently available for any tyrosinases, the central domain contains two copper binding sites, mettyrosinase, the resting form of tyrosinase, contains two tetragonal Cu(II) ions antiferromagnetically coupled through an endogenous bridge, although hydroxide exogenous ligands other than peroxide are bound to the copper site, the exogenous oxygen molecule is bound as peroxide and bridges the two copper centers
H2O2
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the exogenous oxygen molecule is bound as peroxide and bridges the two copper centers, conferring a distinct O2-Cu(II) charge transfer
H2O2
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the exogenous oxygen molecule is bound as peroxide and bridges the two copper centers, conferring a distinct O2-Cu(II) charge transfer
H2O2
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the exogenous oxygen molecule is bound as peroxide and bridges the two copper centers, conferring a distinct O2-Cu(II) charge transfer
H2O2
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the exogenous oxygen molecule is bound as peroxide and bridges the two copper centers, conferring a distinct O2-Cu(II) charge transfer
H2O2
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the exogenous oxygen molecule is bound as peroxide and bridges the two copper centers, conferring a distinct O2-Æ Cu(II) charge transfer
Mg2+
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the enzymatic activity of the SDS-treated hemocyanin can be switched between that of catechol oxidase and that of tyrosinase by addition of Mg2+-ions
additional information
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the enzyme is not influenced by Zn2+, Cr2+, Na+, K+, Mg2+, and Cd2+
additional information
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the partially purified active enzyme is not affected by copper acetate, SDS, methanol, and trypsin
additional information
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tyrosinase activity is enhanced in general by all the cations tested, apart for Ca2+ and Fe2+, that are poor inhibitors of the enzyme. No inhibition by 1 mM NaCl
additional information
tyrosinase activity is enhanced in general by all the cations tested, apart for Ca2+ and Fe2+, that are poor inhibitors of the enzyme. No inhibition by 1 mM NaCl
