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Information on EC 1.14.18.1 - tyrosinase

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EC Tree
IUBMB 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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UNIPROT: B2ZB02
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
2
+
=
2
+
2
Synonyms
tyrosinase, monophenolase, oxygen oxidoreductase, phenol oxidases, murine tyrosinase, melc2, o-diphenol oxidase, monophenol oxidase, met-tyrosinase, jrppo1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
catechol oxidase
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catecholase
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chlorogenic acid oxidase
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-
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chlorogenic oxidase
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-
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cresolase
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Diphenol oxidase
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dopa oxidase
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-
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monophenol dihydroxyphenylalanine:oxygen oxidoreductase
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monophenol monooxidase
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monophenol oxidase
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monophenol, dihydroxy-L-phenylalanine oxygen oxidoreductase
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monophenolase
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N-acetyl-6-hydroxytryptophan oxidase
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o-diphenol oxidase
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o-diphenol oxidoreductase
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o-diphenol:O2 oxidoreductase
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o-diphenol:oxygen oxidoreductase
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o-diphenolase
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phenol oxidase
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phenolase
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polyaromatic oxidase
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polyphenol oxidase
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polyphenolase
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pyrocatechol oxidase
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tyrosinase
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tyrosine-dopa oxidase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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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 hide
9002-10-2
not distinguished from EC 1.10.3.1
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 catechol + O2
2 1,2-benzoquinone + 2 H2O
show the reaction diagram
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-
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?
L-DOPA + O2
L-dopachrome + H2O
show the reaction diagram
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?
L-Dopa + O2
L-dopaquinone + H2O
show the reaction diagram
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?
L-tyrosine + O2
dopachrome + H2O
show the reaction diagram
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?
L-tyrosine + O2
dopaquinone + H2O
show the reaction diagram
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?
L-tyrosine + O2
L-dopaquinone + H2O
show the reaction diagram
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-
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?
phenol + O2
?
show the reaction diagram
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-DOPA + O2
L-dopachrome + H2O
show the reaction diagram
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-
-
?
L-Dopa + O2
L-dopaquinone + H2O
show the reaction diagram
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-
-
?
L-tyrosine + O2
dopaquinone + H2O
show the reaction diagram
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-
-
?
L-tyrosine + O2
L-dopaquinone + H2O
show the reaction diagram
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-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
a type 3 copper protein
Cu2+
tyrosinase is a member of the type 3 copper enzyme family, two Cu2+ ions serveas the major cofactors within the active site
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-ethyl-3-methylimidazolium ethyl sulfate
in the presence of 10 or 20% (w/v) 1-ethyl-3-methylimidazolium ethyl sulfate, the activity decreases dramatically and becomes negligible
kojic acid
i.e. 5-hydroxy-2-(hydroxymethyl)-g-pyrone
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-butyl-3-methylimidazolium tetrafluoroborate
in the presence of 1-butyl-3-methylimidazolium tetrafluoroborate the selectivity of tyrosinase is altered, and the ratio of monophenolase/diphenolase activity increases by up to 5fold
ethylammonium nitrate
in the presence of ethylammonium nitrate the selectivity of tyrosinase is altered, and the ratio of monophenolase/diphenolase activity increases by up to 5fold
SDS
the addition of SDS at levels of 2-50 mM increases the activity of the enzyme by 2fold towards the natural substrates L-tyrosine and L-Dopa and 15-20fold towards the non-native phenol and catechol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.8 - 1.1
L-Dopa
0.05 - 1.4
L-tyrosine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21 - 73.3
L-Dopa
4 - 44.1
L-tyrosine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19.1 - 73.7
L-Dopa
11.9 - 80
L-tyrosine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
B2ZB02_PRIMG
297
0
34410
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
2 * 35000, X-ray crystallography
70000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 35000, X-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R209H
V218F
the monophenolase activity of the mutant on L-tyrosine improves, as the Vmax and kcat values increase 4.2fold. Th same values for diphenolase activity on L-Dopa, however, decrease 2.1fold
V218G
in this mutant, the Vmax and kcat values towards L-tyrosine increase by 7.8fold and towards L-DOPA by 1.7fold, respectively
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sendovski, M.; Kanteev, M.; Ben-Yosef, V.S.; Adir, N.; Fishman, A.
First structures of an active bacterial tyrosinase reveal copper plasticity
J. Mol. Biol.
405
227-237
2011
Priestia megaterium (B2ZB02), Priestia megaterium
Manually annotated by BRENDA team
Goldfeder, M.; Egozy, M.; Shuster Ben-Yosef, V.; Adir, N.; Fishman, A.
Changes in tyrosinase specificity by ionic liquids and sodium dodecyl sulfate
Appl. Microbiol. Biotechnol.
97
1953-1961
2013
Priestia megaterium (B2ZB02), Priestia megaterium
Manually annotated by BRENDA team
Goldfeder, M.; Kanteev, M.; Adir, N.; Fishman, A.
Influencing the monophenolase/diphenolase activity ratio in tyrosinase
Biochim. Biophys. Acta
1834
629-633
2013
Priestia megaterium (B2ZB02), Priestia megaterium
Manually annotated by BRENDA team