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Information on EC 1.10.3.1 - catechol oxidase and Organism(s) Vitis vinifera and UniProt Accession P43311

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IUBMB Comments
A type 3 copper protein that catalyses exclusively the oxidation of catechol (i.e., o-diphenol) to the corresponding o-quinone. The enzyme also acts on a variety of substituted catechols. It is different from tyrosinase, EC 1.14.18.1, which can catalyse both the monooxygenation of monophenols and the oxidation of catechols.
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This record set is specific for:
Vitis vinifera
UNIPROT: P43311
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Word Map
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The taxonomic range for the selected organisms is: Vitis vinifera
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
2
catechol
+
O2
=
2
1,2-benzoquinone
+
2
H2O
2
+
=
2
+
2
Synonyms
hemocyanin, polyphenol oxidase, phenoloxidase, polyphenoloxidase, diphenolase, catecholase, dopa oxidase, catechol oxidase, cresolase, o-diphenoloxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,2-benzenediol:oxygen oxidoreductase
-
catecholase
Diphenol oxidase
-
-
-
-
dopa oxidase
-
-
-
-
o-diphenol oxidoreductase
-
-
-
-
o-diphenol:oxygen oxidoreductase
-
-
-
-
o-diphenolase
-
-
-
-
phenolase
-
-
-
-
polyphenol oxidase
pyrocatechol oxidase
-
-
-
-
tyrosinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
1,2-benzenediol:oxygen oxidoreductase
A type 3 copper protein that catalyses exclusively the oxidation of catechol (i.e., o-diphenol) to the corresponding o-quinone. The enzyme also acts on a variety of substituted catechols. It is different from tyrosinase, EC 1.14.18.1, which can catalyse both the monooxygenation of monophenols and the oxidation of catechols.
CAS REGISTRY NUMBER
COMMENTARY hide
9002-10-2
not distinguished from EC 1.14.18.1
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
-
-
-
?
4-tert-butylcatechol + O2
4-tert-butyl-1,2-benzoquinone + H2O
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
copper-containing enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
inactivation of the enzyme in freshly prepared grape must under high hydrostatic pressure of 100-800 MPa, combined with moderate temperature (20-70°C), or atmospheric pressure conditions in a temperature range of 55-70°C, pressure and temperature act synergistically, except in the hightemperature-low-pressure region where an antagonistic effect is found, kinetics of thermal inactivation, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
sultana grape
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
high expression levels in developing berries and leaves
Manually annotated by BRENDA team
-
grape must
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PPO_VITVI
607
0
67347
Swiss-Prot
Chloroplast (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
1 * 40000, mature enzyme, SDS-PAGE
56700
1 * 56700, mature enzyme, enzyme is synthesized as a 67300 Da precursor protein, predicted from nucleotide sequence
40000
SDS-PAGE
56700
calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 30% (w/v) PEG-4000 in 100 mM buffer citrate pH 5.6 and 200 mM ammonium acetate, at 18°C
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
inactivation of the enzyme in freshly prepared grape must under high hydrostatic pressure of 100-800 MPa, combined with moderate temperature (20-70°C), or atmospheric pressure conditions in a temperature range of 55-70°C, pressure and temperature act synergistically, except in the hightemperature-low-pressure region where an antagonistic effect is found, overview, thermal inactivation of PPO in a biphasic model
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hexadecyltrimethylammonium bromide extraction, ammonium sulfate, Q-Sepharose, Phenyl-Sepharose, hydroxylapatite
ammonium sulfate precipitation, Superose-R 12 column chromatography, and Sephadex G-75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of cDNA
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme needs to be inactivated in wine production from grape must, since it causes undesirable color and turbidity modifications, which can change the stability and organoleptic characteristics of grape juice and musts, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dry, I.B.; Robinson, S.P.
Molecular cloning and characterisation of grape berry polyphenol oxidase
Plant Mol. Biol.
26
495-502
1994
Vitis vinifera (P43311), Vitis vinifera
Manually annotated by BRENDA team
Rapeanu, G.; Van Loey, A.; Smout, C.; Hendrichx, M.
Thermal and high-pressure inactivation kinetics of polyphenol oxidase in victoria grape must
J. Agric. Food Chem.
53
2988-2994
2005
Vitis vinifera
Manually annotated by BRENDA team
Virador, V.M.; Reyes Grajeda, J.P.; Blanco-Labra, A.; Mendiola-Olaya, E.; Smith, G.M.; Moreno, A.; Whitaker, J.R.
Cloning, sequencing, purification, and crystal structure of Grenache (Vitis vinifera) polyphenol oxidase
J. Agric. Food Chem.
58
1189-1201
2010
Vitis vinifera (P93622), Vitis vinifera
Manually annotated by BRENDA team