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Information on EC 1.13.11.1 - catechol 1,2-dioxygenase and Organism(s) Acinetobacter radioresistens and UniProt Accession Q9F103
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1.13.11.1 catechol 1,2-dioxygenaseIUBMB Comments
Requires Fe3+. Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida.
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Word Map
- 1.13.11.1
- phenol
- benzoate
- protocatechuate
-
ortho
-
intradiol
-
3,4-dioxygenase
- muconate
-
cis,cis-muconic
- chlorocatechols
-
ortho-cleavage
- 4-chlorocatechol
-
cycloisomerase
-
ironiii
- 3-methylcatechol
- opacus
-
beta-ketoadipate
-
phenol-degrading
- gentisate
- 3-chlorobenzoate
-
2-hydroxymuconic
-
voxel-based
- radioresistens
-
3,5-di-tert-butylcatecholate
-
cis-muconate
-
meta-cleavage
-
clavien-dindo
- chlorobenzene
-
precuneus
- environmental protection
- degradation
- biotechnology
- synthesis
The taxonomic range for the selected organisms is: Acinetobacter radioresistens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
catechol 1,2-dioxygenase, catechol dioxygenase, cat12, pyrocatechase, chlorocatechol 1,2-dioxygenase, cd ii, catechol 1,2-oxygenase, catechol 1,2 dioxygenase, 1,2-ctd, c1,2o, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,2-pyrocatechase
-
-
-
-
catechase
-
-
-
-
catechol 1,2-oxygenase
-
-
-
-
catechol dioxygenase
-
-
-
-
catechol oxygenase
-
-
-
-
catechol-oxygen 1,2-oxidoreductase
-
-
-
-
CD I
-
-
-
-
CD II
-
-
-
-
CD-I
-
-
-
-
CD-II
-
-
-
-
CD-III-1
-
-
-
-
CD-III-2
-
-
-
-
CDI1
-
-
-
-
CDI2
-
-
-
-
pyrocatechase
-
-
-
-
pyrocatechol 1,2-dioxygenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-
SYSTEMATIC NAME
IUBMB Comments
catechol:oxygen 1,2-oxidoreductase
Requires Fe3+. Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida.
CAS REGISTRY NUMBER
COMMENTARY
9027-16-1
-
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-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
the enzyme preferentially recognizes 4-substituted over 3-substituted catechols
-
-
?
4-chlorocatechol + O2
(2E,4Z)-3-chlorohexa-2,4-dienedioate
the enzyme preferentially recognizes 4-substituted over 3-substituted catechols
-
-
?
4-methylcatechol + O2
4-methyl-cis,cis-muconate
the enzyme preferentially recognizes 4-substituted over 3-substituted catechols
-
-
?
catechol + O2
cis-cis muconate
assay at pH 8.0, 30°C
-
-
?
3-methylcatechol + O2
(2Z,4Z)-2-methylhexa-2,4-dienedioate
-
-
-
-
?
4-methylcatechol + O2
(2Z,4Z)-3-methylhexa-2,4-dienedioate
-
-
-
-
?
4,5-dichlorocatechol + O2
?
the enzyme possesses only a quite rare capability to process 4,5-dichlorocatechol
-
-
?
additional information
?
-
-
extradiol cleavage of 3-methylcatechol, no substrate: 3-chlorocatechol, protocatechuic acid
-
-
?
additional information
?
-
-
both intradiol and extradiol cleavage of 3-methylcatechol
-
-
?
NATURAL SUBSTRATE
NATURAL 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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe3+
Iron
Iron
-
isoenzyme A: 0.96 mol per mol enzyme, isoenzyme B: 0.89 mol per mol enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00225
3-methylcatechol
wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.00595
3-methylcatechol
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.0001
4-Chlorocatechol
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.00198
4-Chlorocatechol
wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.0061
4-Chlorocatechol
mutant enzyme A72G, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.01
4-methylcatechol
mutant enzyme A72G, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.0128
4-methylcatechol
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.053
4-methylcatechol
wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.00204
catechol
wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.00576
catechol
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.0093
catechol
mutant enzyme A72G, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.52
3-methylcatechol
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
1.59
3-methylcatechol
wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.17
4,5-dichlorocatechol
mutant enzyme A72G, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.17
4,5-dichlorocatechol
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.18
4,5-dichlorocatechol
wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.34
4-Chlorocatechol
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.83
4-Chlorocatechol
wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
1.74
4-Chlorocatechol
mutant enzyme A72G, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
0.72
4-methylcatechol
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
5.45
4-methylcatechol
wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
5.51
4-methylcatechol
mutant enzyme A72G, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
4.42
catechol
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
13.6
catechol
mutant enzyme A72G, in100 mM Tris-HCl pH 8.5, temperature not specified in the publication
24.2
catechol
wild type enzyme, in100 mM Tris-HCl pH 8.5, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
880
3-methylcatechol
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
7100
3-methylcatechol
wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
280
4-Chlorocatechol
mutant enzyme A72G, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
3440
4-Chlorocatechol
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
4200
4-Chlorocatechol
wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
550
4-methylcatechol
mutant enzyme A72G, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
570
4-methylcatechol
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
1000
4-methylcatechol
wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
1460
catechol
mutant enzyme A72G, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
7800
catechol
mutant enzyme L69A, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
11800
catechol
wild type enzyme, in 100 mM Tris-HCl pH 8.5, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.6 - 8.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 10
-
below no enzyme activity, at pH 8.5 40% residual enzyme activity of the immobilized enzyme compared to inactive free form enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32.7 - 51.8
differences between wild-type and mutant enzymes
10 - 60
-
at 60°C still 70% residual activity of the immobilized enzyme form
30 - 40
-
complete loss of enzyme activity of the free form at 60°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
catechol 1,2-dioxygenase from Acinetobacter ADP1 is used as a template
UniProt
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
structure-function relationships of wild-type and mutant enzymes, overview
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38600
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homodimer
-
2 * 38700-39000, at low ionic strength, upon increasing the ionic strength the enzyme monomerizes, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 2 M ammonium sulfate, 0.1 M Tris-HCl, pH 8.5, at 4°C
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A72D
enhanced substrate specificity towards chlorinated substrates
A72G
A72N
enhanced substrate specificity towards chlorinated substrates
A72S
enhanced substrate specificity towards chlorinated substrates
L69A
A72D
-
site-directed mutagenesis, the mutant shows a low level of iron incorporation compared to the wild-type enzyme and altered thermal stability values, pH and temperature dependence
A72G
-
site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence
A72N
-
site-directed mutagenesis, the mutant shows a disturbed iron binding and altered thermal stability values, pH and temperature dependence
A72P
-
site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence
A72S
-
site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence
L69A
-
site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence
L69G/A72G
-
site-directed mutagenesis, the mutant shows altered thermal stability values, pH and temperature dependence
additional information
A72G
enhanced substrate specificity towards chlorinated substrates
A72G
the mutant shows decreased activity with catechol and no activity with 3-methylcatechol compared to the wild type enzyme
L69A
the mutant shows decreased activity with catechol and increased activity for 4-chlorocatechol compared to the wild type enzyme
additional information
catechol 1,2-dioxygenase from Acinetobacter ADP1 is used as a template
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
90 min, 60% residual activity for the immobilized protein versus 20% residual activity for the free enzyme
60
-
15 min, 75% residual activity for the immobilized protein versus total inactivation of the free enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
25°C, 11 days, complete inactivation for the immobilized protein
-
25°C, 4 days, residual activity 50% for the immobilized protein and 10% for the free form
-
4°C, 10 days, 50% residual acitivity for the immobilized protein and only 10% residual activity of the free form protein
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
product is precursor of the industrially important compound adipic acid
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Briganti, F.; Pessione, E.; Giunta, C.; Scozzafava, A.
Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens
FEBS Lett.
416
61-64
1997
Acinetobacter radioresistens
Briganti, F.; Pessione, E.; Giunta, C.; Mazzoli, R.; Scozzafava, A.
Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens
J. Protein Chem.
19
709-716
2000
Acinetobacter radioresistens
Caglio, R.; Valetti, F.; Caposio, P.; Gribaudo, G.; Pessione, E.; Giunta, C.
Fine-tuning of catalytic properties of catechol 1,2-dioxygenase by active site tailoring
ChemBioChem
10
1015-1024
2009
Acinetobacter baylyi ADP1 (P07773), Acinetobacter radioresistens (Q9F103), Acinetobacter radioresistens S13 (Q9F103)
Di Nardo, G.; Roggero, C.; Campolongo, S.; Valetti, F.; Trotta, F.; Gilardi, G.
Catalytic properties of catechol 1,2-dioxygenase from Acinetobacter radioresistens S13 immobilized on nanosponges
Dalton Trans.
33
6507-6512
2009
Acinetobacter radioresistens, Acinetobacter radioresistens S13
Micalella, C.; Martignon, S.; Bruno, S.; Pioselli, B.; Caglio, R.; Valetti, F.; Pessione, E.; Giunta, C.; Rizzi, M.
X-ray crystallography, mass spectrometry and single crystal microspectrophotometry: A multidisciplinary characterization of catechol 1,2 dioxygenase
Biochim. Biophys. Acta
1814
817-823
2011
Acinetobacter radioresistens (Q9F103), Acinetobacter radioresistens LMG S13 (Q9F103), Acinetobacter radioresistens LMG S13
Caglio, R.; Pessione, E.; Valetti, F.; Giunta, C.; Ghibaudi, E.
An EPR, thermostability and pH-dependence study of wild-type and mutant forms of catechol 1,2-dioxygenase from Acinetobacter radioresistens S13
Biometals
26
75-84
2013
Acinetobacter radioresistens, Acinetobacter radioresistens S13
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