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Information on EC 1.14.18.1 - tyrosinase and Organism(s) Pholiota nameko and UniProt Accession A7BHQ9

for references in articles please use BRENDA:EC1.14.18.1
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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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Pholiota nameko
UNIPROT: A7BHQ9
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The taxonomic range for the selected organisms is: Pholiota nameko
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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L-tyrosine
+
O2
=
dopaquinone
+
H2O
+
=
+
2
L-dopa
+
O2
=
2
dopaquinone
+
2
H2O
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
monophenol, 3,4-dihydroxy L-phenylalanine (L-DOPA):oxygen oxidoreductase
-
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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
3-(3,4-dihydroxyphenyl) propionic acid + 1/2 O2
3-(3,4-dihydroxyphenyl)propionic acid + H2O
show the reaction diagram
-
-
-
?
4-t-butylphenol + O2 + AH2
4-t-butyl 1,2-benzoquinone + H2O + A
show the reaction diagram
-
-
-
?
4-tert-butylcatechol + 1/2 O2
4-(tert-butyl)benzo-1,2-quinone + H2O
show the reaction diagram
-
-
-
?
D-dopa + 1/2 O2
D-dopaquinone + H2O
show the reaction diagram
-
-
-
?
dopamine + 1/2 O2
dopamine quinone + H2O
show the reaction diagram
-
-
-
?
L-dopa + 1/2 O2
L-dopaquinone + H2O
show the reaction diagram
-
-
-
?
L-tyrosine + O2 + AH2
L-3,4-dihydroxyphenylalanine + H2O + A
show the reaction diagram
-
-
-
?
p-cresol + O2 + AH2
4-methyl-o-quinone + H2O + A
show the reaction diagram
-
-
-
?
tyramine + O2
4-(2-aminoethyl)cyclohexa-3,5-diene-1,2-dione + H2O
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
enzyme contains 1.9 copper atoms per molecule
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1240
3-(3,4-dihydroxyphenyl) propionic acid
-
136
4-t-butylcatechol
-
119
4-t-butylphenol
-
122
dopamine
-
1930
L-Dopa
-
30.6
p-Cresol
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
544
3-(3,4-dihydroxyphenyl) propionic acid
-
294
4-t-butylcatechol
-
13.2
4-t-butylphenol
-
1590
dopamine
-
107
p-Cresol
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
412
purification step, Superdex 200
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TYRO_PHONA
625
0
67499
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
by gel filtration chromatography
42000
by SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kawamura-Konishi, Y.; Tsuji, M.; Hatana, S.; Asanuma, M.; Kakuta, D.; Kawano, T.; Mukouyama, E.B.; Goto, H.; Suzuki, H.
Purification, characterization, and molecular cloning of tyrosinase from Pholiota nameko
Biosci. Biotechnol. Biochem.
71
1752-1760
2007
Pholiota nameko (A7BHQ9), Pholiota nameko
Manually annotated by BRENDA team