Any feedback?
Information on EC 1.10.3.1 - catechol oxidase and Organism(s) Ipomoea batatas and UniProt Accession Q9ZP19
for references in articles please use BRENDA:EC1.10.3.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.10.3.1 catechol oxidaseIUBMB 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.
Specify your search results
Word Map
- 1.10.3.1
-
limpet
-
keyhole
- brown
- catalase
- lymphocyte
- dismutase
- hemolymph
- igm
-
humoral
- larvae
- shrimp
- mushroom
-
haptens
- vannamei
- sod
-
antigen-specific
-
melanization
-
arthropod
- haemocyte
- melanin
- crab
- litopenaeus
-
idiotype
- o-quinones
-
crustacean
- hepatopancreas
-
chlorogenic
-
delayed-type
-
ammonia-lyase
- l-dopa
-
postharvest
- laccase
-
shelf
-
molluscan
-
anti-idiotypic
-
dinuclear
-
gastropod
- crayfish
- nutrition
- pyrogallol
- agriculture
- drug development
- lobster
- alginolyticus
-
entomopathogenic
-
copper-binding
-
antiferromagnetic
- penaeus
-
kojic
-
copper-containing
- pomatia
- food industry
- toxoid
- limulus
The taxonomic range for the selected organisms is: Ipomoea batatas
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
hemocyanin, polyphenol oxidase, phenoloxidase, polyphenoloxidase, diphenolase, catecholase, catechol oxidase, dopa oxidase, cresolase, o-diphenoloxidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
catecholase
Diphenol oxidase
-
-
-
-
dopa oxidase
-
-
-
-
o-diphenol oxidoreductase
-
-
-
-
o-diphenol:oxygen oxidoreductase
-
-
-
-
o-diphenolase
-
-
-
-
phenolase
-
-
-
-
polyphenol oxidase
-
-
-
-
pyrocatechol oxidase
-
-
-
-
tyrosinase
-
-
-
-
catecholase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 catechol + O2 = 2 1,2-benzoquinone + 2 H2O
catalytic reaction mechanism of the enzyme in a copper(II) complex with a macrocyclic ligand
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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
9002-10-2
not distinguished from EC 1.14.18.1
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
3,4-dihydroxyphenylacetic acid + O2
(3,4-dioxocyclohexa-1,5-dien-1-yl)acetic acid + H2O
-
-
-
?
3,5-di-tert-butylcatechol + O2
3,5-di-tert-butyl-o-benzoquinone + H2O
-
mechanism, the rate-determining step is found to change with the substrate to complex ratio, I2+ reacts with DTBCH2, while undergoing a one-electron reduction, leading to the formation of mixed-valence CuIICuIsemiquinone species DTSQ
-
-
?
additional information
?
-
-
reduction of dioxygen to dihydrogen peroxide upon catechol oxidation by copper(II) complexes, overview, dioxygen undergoes a two-electron reduction to dihydrogen peroxide, and a second mechanism in which it is converted into water upon four-electron reduction, catecholase activity of a tetranuclear carbonato-bridged copper(II) cluster with the macrocyclic ligand 9,22-dipropyl-1,4,9,14,17,22,27,28,29,30-decaazapentacyclotriacontane-5,7(28),11(29),12,18,20(30),24(27),25-octaene, ferromagnetic interaction between the two copper ions within one macrocyclic ring, and a weak antiferromagnetic interaction between the two neighboring copper ions of two different macrocyclic units, solution stability, electrochemical properties, and crystal structure of (I)2(CF3SO3)4 - 2CH3CN- 4H2O, detailed overview, mechanisms versus a coordination mode of the substrate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
additional information
-
artificial dinuclear copper complexes as functional models for catechol oxidase
Cu2+
-
type 3 copper enzyme, coordination number of 4 for each copper atom, CuII-CuII distance of 2.9 A
Cu2+
-
binuclear copper center each coordinated by three histidine nitrogen atoms, in the oxidized enzyme structure the 2 copper II centers contain a hydroxide bridging group completing the four-coordinated trigonal pyramidal coordination sphere, in the reduced form the CuI-CuI separation increases to 4.4 A and a water molecule coordinates to one copper
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hydrogen peroxide
-
activating at higher concentrations, however, the concentration of dihydrogen peroxide, formed during the reaction, does not reach this level
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics, tetranuclear carbonato-bridged copper(II) cluster with the macrocyclic ligand, overview
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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). PPO1_IPOBA
496
0
55011
Swiss-Prot
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme in resting dicupric CII-CuII state, in reduced dicuprous CuI-CuI form and in complex with the inhibitor phenylthiourea
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Klabunde, T.; Eicken, C.; Sacchettini, J.C.; Krebs, B.
Crystal structure of a plant catechol oxidase containing a dicopper center
Nat. Struct. Biol.
5
1084-1090
1998
Ipomoea batatas
Gentschev, P.; Moller, N.; Krebs, B.
New functional models for catechol oxidases
Inorg. Chim. Acta
300-302
442-452
2000
Ipomoea batatas
-
Haase, W.; Ostrovsky, S.
Catecholase activity of a series of dicopper(II) complexes with variable Cu-OH(phenol) moieties
Inorg. Chem.
41
1788-1794
2002
Ipomoea batatas
Koval,I.A.; Selmeczi, K.; Belle, C.; Philouze, C.; Saint-Aman, E.; Gautier-Luneau, I.; Schuitema, A.M.; van Vliet, M.; Gamez, P.; Roubeau, O.; Lueken, M.; Krebs, B.; Lutz, M.; Spek, A.L.; Pierre, J.L.; Reedijk, J.
Catecholase activity of a copper(II) complex with a macrocyclic ligand: unraveling catalytic mechanisms
Chem. Eur. J.
12
6138 - 6150
2006
Ipomoea batatas
EXTERNAL LINKS (specific for EC-Number 1.10.3.1)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
