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Enzyme Nomenclature
Information on EC 1.13.11.2 - catechol 2,3-dioxygenase
for references in articles please use BRENDA:EC1.13.11.2
Word Map on EC 1.13.11.2
- 1.13.11.2
- heme
-
carboxylase
- putida
- rubisco
-
ferredoxins
-
biodegradation
- flavin
- l-arginine
- toluene
- tetrahydrobiopterin
- ribulose-1,5-bisphosphate
-
dioxygenation
- naphthalene
-
ferrous
- ribulose
-
rieske
- biphenyls
- fmn
- 2-oxoglutarate
- rhodococcus
-
non-heme
-
bioremediation
- semialdehyde
-
multicomponent
-
mixed-function
-
nitric-oxide
- sphingomonas
-
1,5-bisphosphate
-
bisphosphate
-
photorespiration
- 4-methylcatechol
-
2-oxoglutarate-dependent
- xylene
- bh4
-
dihydroxylation
- l-citrulline
- comamonas
- biliverdin
- carbazole
- l-arg
- phenanthrene
-
photorespiratory
-
4.1.1.39
-
diiron
- rhodochrous
-
monooxygenation
-
heme-heme
- ethylbenzene
- fluorene
- testosteroni
- environmental protection
- degradation
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
1.13.11.2
-
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RECOMMENDED NAME
GeneOntology No.
catechol 2,3-dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catechol + O2 = 2-hydroxymuconate-6-semialdehyde
ordered bi uni mechanism
-
catechol + O2 = 2-hydroxymuconate-6-semialdehyde
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
catechol:oxygen 2,3-oxidoreductase (decyclizing)
Requires FeII. The enzyme initiates the meta-cleavage pathway of catechol degradation.
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CAS REGISTRY NUMBER
COMMENTARY
9029-46-3
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
glucose grown cells do not possess catechol 2,3-dioxygenase activity in appreciable quantity
-
-
epigeic earthworm used in vermicomposting processes. Comparing initial wet olive cake and wet olive cake inoculated with Eisenia fetida catechol dioxygenase activity is detected. The catechol-dioxygenase apppears to be due to high microbial activity, catechol-dioxygenase is only detected when a vermincomposting process takes place on the wet olive cake.
-
-
no actvity in Fusarium sp.
no catechol 2,3-dioxygenase is dectectable. Activity is measured by production of maleylpyruvate (increase in A375 nm) for catechol 2,3-dosygenase.
-
-
no actvity in Fusarium sp. BI
no catechol 2,3-dioxygenase is dectectable. Activity is measured by production of maleylpyruvate (increase in A375 nm) for catechol 2,3-dosygenase.
-
-
strain Pmen PC1 - strain Pmen PC12 and Pmen PC19, all analysed stains contain catechol 2,3-dioxygenase genes
-
-
Pseudomonas putida mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182 mt-2 / ATCC 33015 / DSM 3931 / NCIB 12182 / NCIMB 12182
-
UniProt
Ppu PC16, Ppu PC30, Ppu PC35, Ppu PC36 and Ppu PC39 contain catechol 2,3-dioxygenase genes. The stains Ppu PC14-PC16 and Ppu PC30 do not contain catechol 2,3-dioxygenase genes
-
-
isolated from the marine sediment, plasmid-encoded gene nahH
UniProt
amino acid sequence of nahH from Pseudomonas stutzeri NA1 shows 96% sequence identity with the catechol 2,3-dioxygenase gene from Pseudomonas putida strain H.; Absorption spectra and gas chromatography/mass spectrometry analyses of intermediate metabolites of salicylate or catechol degradation by a crude extract of Pseudomonas stutzeri NA1 reveals the presence of the meta-ring cleavage product 2-hydroxymuconate semialdehyde as a major constituent.
-
-
activity detected with 2-hydroxyboenzothiazole as growth substrate
-
-
activity detected with 2-hydroxyboenzothiazole as growth substrate
-
-
enzyme subgroup I.2.B, hybrid enzymes with type I.2.A enzyme from Pseudomonas sp.
-
-
isolated from the marine sediment, chromosomal-encoded gene nahH
-
-
PfF PC20, PfB PC21 - PfB PC23, PfC PC24 - PfB PC26, PfB PC28, PfC PC31, PfB PC32 - PfB PC34, PfB PC37, PfB PC38 and PfF P69 contain catechol 2,3-dioxygenase genes. The strains PfF PC17 and PfF p69 do not contain catechol 2,3-dioxygenase genes
-
-
-
-
-
mt-2, used for identifying potential sites of introducing disulfide bond of C23O from Pseudomonas sp.
UniProt
Ppu PC16, Ppu PC30, Ppu PC35, Ppu PC36 and Ppu PC39 contain catechol 2,3-dioxygenase genes. The stains Ppu PC14-PC16 and Ppu PC30 do not contain catechol 2,3-dioxygenase genes
-
-
enzyme subgroup I.2.A, hybrid enzymes with type I.2.B enzyme from Sphingomonas sp.
-
-
amino acid sequence of nahH from Pseudomonas stutzeri NA1 shows 96% sequence identity with the catechol 2,3-dioxygenase gene from Pseudomonas putida strain H.; Absorption spectra and gas chromatography/mass spectrometry analyses of intermediate metabolites of salicylate or catechol degradation by a crude extract of Pseudomonas stutzeri NA1 reveals the presence of the meta-ring cleavage product 2-hydroxymuconate semialdehyde as a major constituent.
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
inactivation of TodE and the subsequent accumulation of 3-vinylcatechol results in toxicity and cell death
metabolism
physiological function
additional information
evolution
the enzyme belongs to the single-ring substrate subfamily of the extradiol dioxygenase
evolution
-
the enzyme belongs to the single-ring substrate subfamily of the extradiol dioxygenase
-
metabolism
-
the enzyme catalyzes a step in the degradation of phenanthrene, overview
metabolism
the enzyme catalyzes a step in the degradation of phenanthrene, overview
metabolism
-
the enzyme catalyzes a step in the degradation of phenanthrene, overview
metabolism
-
the enzyme catalyzes a step in the degradation of phenanthrene, overview
-
metabolism
-
the enzyme catalyzes a step in the degradation of phenanthrene, overview
-
metabolism
-
the enzyme catalyzes a step in the degradation of phenanthrene, overview
-
physiological function
-
catechol-2,3-dioxygenase contributes to quinone resistance
physiological function
-
overexpressing TodE is necessary to allow Pseudomonas putida strain F1 to grow on styrene
physiological function
-
catechol 2,3-dioxygenases play a role in the degradation of monoaromatic hydrocarbons
physiological function
-
both the ortho- and the meta-degradation pathways are functional in presence of phenol. However, the activation of the catechol 2,3-dioxygenase, only when phenol is present, and the accumulation of only intermediary compounds related to this pathway lead us to the conclusion that the aromatic ring is preferentially opened through the meta-pathway
physiological function
-
isolate A235 shows high phenol degradation capacity on solid and liquid media containing 20% (w/v) NaCl and phenol as sole carbon and energy source. Degradation of phenol is achieved through a meta-cleavage pathway involving catechol 2,3-dioxygenase
physiological function
-
catechol-2,3-dioxygenase contributes to quinone resistance
-
physiological function
-
catechol 2,3-dioxygenases play a role in the degradation of monoaromatic hydrocarbons
-
physiological function
-
both the ortho- and the meta-degradation pathways are functional in presence of phenol. However, the activation of the catechol 2,3-dioxygenase, only when phenol is present, and the accumulation of only intermediary compounds related to this pathway lead us to the conclusion that the aromatic ring is preferentially opened through the meta-pathway
-
additional information
Planococcus sp. strain S5 grown on 1 or 2 mM phenol shows activity of both a catechol 1,2- and catechol 2,3-dioxygenase while at a higher concentrations of phenol only catechol 2,3-dioxygenase activity is observed
additional information
-
there is a hydrophobic channel in the active site of catechol 2,3-dioxygenase. Through this channel catechol penetrates into the active site of the enzyme
additional information
-
the enzyme is a member of the superfamily I, subfamily 2A of extradiol dioxygenases
additional information
-
Planococcus sp. strain S5 grown on 1 or 2 mM phenol shows activity of both a catechol 1,2- and catechol 2,3-dioxygenase while at a higher concentrations of phenol only catechol 2,3-dioxygenase activity is observed; the enzyme is a member of the superfamily I, subfamily 2A of extradiol dioxygenases
-
additional information
-
there is a hydrophobic channel in the active site of catechol 2,3-dioxygenase. Through this channel catechol penetrates into the active site of the enzyme
-
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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-formylcatechol + O2
3-formyl-2-hydroxymuconate semialdehyde
-
-
-
?
3-methoxycatechol + O2
2-hydroxy-3-methoxy-6-oxohexa-2,4-dienoate
-
-
-
-
?
3-phenylcatechol + O2
2-hydroxy-3-phenylmuconate semialdehyde
-
-
-
?
3-sulfocatechol + O2 + H2O
(2E,4Z)-2-hydroxymuconate + bisulfite + H+
-
-
-
-
?
4-bromocatechol + O2
4-bromo-2-hydroxymuconate semialdehyde
-
-
-
?
4-hydroxymethylcatechol + O2
2-hydroxy-4-hydroxymethylmuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-methylcatechol + O2
2-hydroxy-5-methyl-6-oxohexa-2,4-dienoate + H+
-
-
-
-
?
4-n-butylcatechol + O2
?
activity is 1.85fold higher than with catechol
-
-
?
tetrachlorohydroquinone + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
2,3-dihydroxybiphenyl + O2
?
1.3% of the activity with 2,3-dihydroxybiphenyl
-
-
?
2,3-dihydroxybiphenyl + O2
?
1.3% of the activity with 2,3-dihydroxybiphenyl
-
-
?
3,4-dimethylcatechol + O2
2-hydroxy-5-methyl-6-oxo-hepta-2,4-dienoate
-
-
-
-
?
3,4-dimethylcatechol + O2
2-hydroxy-5-methyl-6-oxo-hepta-2,4-dienoate
-
-
-
-
?
3,5-dichlorocatechol + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
3,5-dichlorocatechol + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
3,5-dimethylcatechol + O2
2-hydroxy-3,5-dimethyl-6-oxohexa-2,4-dienoic acid
-
-
-
-
?
3,5-dimethylcatechol + O2
2-hydroxy-3,5-dimethyl-6-oxohexa-2,4-dienoic acid
-
-
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
weak
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
weak
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
weak
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
-
?
3-chlorocatechol + O2
2-chloro-2-hydroxy-6-oxohexa-2,4-dienoate
-
weak
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
about 9% of the rate with catechol
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
about 95% of the rate with catechol
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
about 95% of the rate with catechol
-
-
?
3-chlorocatechol + O2
3-chloro-2-hydroxymuconate semialdehyde
about 9% of the rate with catechol
-
-
?
3-methoxycatechol + O2
2-hydroxy-3-methoxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
3-methoxycatechol + O2
2-hydroxy-3-methoxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
-
19% of the activity with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
-
19% of the activity with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
poor substrate
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
-
most effective substrate
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
-
most effective substrate
-
-
?
3-methylcatechol + O2
2-hydroxy-3-methylmuconate semialdehyde
about 30% of activity with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
weak
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
weak
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
6.12% activity compared to catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 105% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 43% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 43% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 105% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
-
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 30% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
about 30% of the rate with catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoate
-
isoform C23O1 shows 49.5% activity compared to catechol, isoform C23O2 shows 239.2% activity compared to catechol
-
-
?
3-methylcatechol + O2
2-hydroxy-6-oxohepta-2,4-dienoic acid
-
-
-
-
?
3-methylcatechol + O2
?
33% of the activity with 4-chlorocatechol
-
-
?
3-methylcatechol + O2
?
33% of the activity with 4-chlorocatechol
-
-
?
3-methylcatechol + O2
cis,cis-2-hydroxy-6-oxohepta-2,4-dienoate + H+
-
-
-
-
?
3-methylcatechol + O2
cis,cis-2-hydroxy-6-oxohepta-2,4-dienoate + H+
-
-
-
-
?
4-alkylcatechol + O2
?
initial step of long-chain alkylphenol cleavage pathway
-
-
?
4-alkylcatechol + O2
?
alkyl chain length C1-C5 is accepted as substrate
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
-
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
-
44.88% activity compared to catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
-
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
about 16% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
about 75% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
about 75% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
about 16% of the rate with catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
at the same rate as catechol
-
-
?
4-chlorocatechol + O2
4-chloro-2-hydroxymuconate semialdehyde
-
isoform C23O1 shows 50.8% activity compared to catechol, isoform C23O2 shows 226.4% activity compared to catechol
-
-
?
4-chlorocatechol + O2
5-chloro-2-hydroxymuconic semialdehyde
-
-
-
?
4-chlorocatechol + O2
?
39% of the activity with 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
?
39% of the activity with 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
?
-
the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
4-chlorocatechol + O2
?
-
the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
4-ethylcatechol + O2
4-ethyl-2-hydroxymuconate semialdehyde
effective substrate
-
-
?
4-ethylcatechol + O2
4-ethyl-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-ethylcatechol + O2
4-ethyl-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-formylcatechol + O2
4-formyl-2-hydroxymuconate semialdehyde
-
-
-
?
4-formylcatechol + O2
4-formyl-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-formylcatechol + O2
4-formyl-2-hydroxymuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
weak
-
-
-
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
weak
-
-
-
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
101.91% activity compared to catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
highly specific for
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
-
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
hypoxic strains with significantly higher affinities
-
-
?
4-methylcatechol + O2
2-hydroxy-3-methyl-6-oxohexa-2,4-dienoate
-
best substrate for isoform C23O2 (280.7% activity compared to catechol), while isoform C23O1 shows 87.4% activity compared to catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 47% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 89% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 89% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 47% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 65% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methyl-6-oxohexa-2,4-dienoate
about 65% of the rate with catechol
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
very effective substrate
-
-
?
4-methylcatechol + O2
2-hydroxy-4-methylmuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
4-methylcatechol + O2
?
activity is 5.72fold higher than with catechol
-
-
?
4-methylcatechol + O2
?
about 65% of activity with catechol
-
-
?
4-nitrocatechol + O2
2-hydroxy-4-nitromuconate semialdehyde
-
-
-
?
4-nitrocatechol + O2
2-hydroxy-4-nitromuconate semialdehyde
rapid inactivation of enzyme during turnover
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
extradiol dioxygenase reaction
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
metacleavage enzyme of catechol metabolism
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
metapyrocatechase 1 takes part in oxidation of aromatic compounds, producing catechol as an intermediate, metapyrocatechase 2 is involved in oxidation of methyl-substituted aromatic substrates
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is induced by benzenesulfonate, catechol or toluene p-sulfonate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
benzoate degadation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key role in the degradation of aromatic molecules
-
-
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a key enzyme in the catabolism of monocyclic aromatic compounds including aniline and catalyzes the extradiol cleavage of catechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
involved in metabolism of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key enzyme for the degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a critical enzyme in the multistep biodegradation of 3,4-dichloroaniline by Pseudomonas sp. KB35B
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a critical enzyme in the multistep biodegradation of 3,4-dichloroaniline by Pseudomonas sp. KB35B
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
highly specific for
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
most effective substrate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
most effective substrate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
hypoxic strains have enzymes with significantly higher affinities for catechol than for nonhypoxic strains
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key enzyme for the degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
and 4-chlorocatechol, best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
both the ortho- and the meta-degradation pathways are functional in presence of phenol. However, the activation of the catechol 2,3-dioxygenase, only when phenol is present, and the accumulation of only intermediary compounds related to this pathway lead us to the conclusion that the aromatic ring is preferentially opened through the meta-pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
both the ortho- and the meta-degradation pathways are functional in presence of phenol. However, the activation of the catechol 2,3-dioxygenase, only when phenol is present, and the accumulation of only intermediary compounds related to this pathway lead us to the conclusion that the aromatic ring is preferentially opened through the meta-pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
the enzyme shows the highest activity against catechol and 4-chlorocatechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
and 4-chlorocatechol, best substrates
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
100% activity
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
best substrate for isoform C23O1 (100% activity)
-
-
?
hydroquinone + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
hydroquinone + O2
?
-
immobilized enzyme, no activity with the free enzyme
-
-
?
phenol + O2
2-hydroxymuconic semialdehyde
utilize phenol as sole carbon and energy source, concentration of phenol diversify from 25 mg/l to 1000 mg/l, assay at 28°C, pH 6.8-7.0
-
-
?
phenol + O2
2-hydroxymuconic semialdehyde
utilize phenol as sole carbon and energy source, concentration of phenol diversify from 25 mg/l to 1000 mg/l, assay at 28°C, pH 6.8-7.0
-
-
?
additional information
?
-
no cleavage of 4-carboxycatechol, 4-carboxymethylcatechol and 4-tert-butylcatechol
-
-
-
additional information
?
-
no activity with 4-tert-butylcatechol
-
-
-
additional information
?
-
no activity with 4-tert-butylcatechol
-
-
-
additional information
?
-
-
the two isoforms cannot oxidize 1, 2-dihydroxynaphthalene
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
4-alkylcatechol + O2
?
Q7WYF5
initial step of long-chain alkylphenol cleavage pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
metacleavage enzyme of catechol metabolism
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
metapyrocatechase 1 takes part in oxidation of aromatic compounds, producing catechol as an intermediate, metapyrocatechase 2 is involved in oxidation of methyl-substituted aromatic substrates
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is induced by benzenesulfonate, catechol or toluene p-sulfonate
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
P06622
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
benzoate degadation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key role in the degradation of aromatic molecules
-
-
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a key enzyme in the catabolism of monocyclic aromatic compounds including aniline and catalyzes the extradiol cleavage of catechol
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
Q83U22
degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
Q7WYF5
involved in metabolism of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key enzyme for the degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a critical enzyme in the multistep biodegradation of 3,4-dichloroaniline by Pseudomonas sp. KB35B
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is a critical enzyme in the multistep biodegradation of 3,4-dichloroaniline by Pseudomonas sp. KB35B
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
cleavage of aromatic compounds, involved in alpha-ketoadiapate pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
catechol 2,3-dioxygenase is involved in the meta phenol degradation pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
enzyme is a important component in the degradation pathways of toluene and xylene and catalyses the dioxygenolytic cleavage of the aromatic ring
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
involved in biodegradation of benzothiazoles
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
degradation of aromatic compounds, involved in toluene and ortho-xylene metabolism
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
key enzyme for the degradation of aromatic compounds
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
both the ortho- and the meta-degradation pathways are functional in presence of phenol. However, the activation of the catechol 2,3-dioxygenase, only when phenol is present, and the accumulation of only intermediary compounds related to this pathway lead us to the conclusion that the aromatic ring is preferentially opened through the meta-pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
-
both the ortho- and the meta-degradation pathways are functional in presence of phenol. However, the activation of the catechol 2,3-dioxygenase, only when phenol is present, and the accumulation of only intermediary compounds related to this pathway lead us to the conclusion that the aromatic ring is preferentially opened through the meta-pathway
-
-
?
catechol + O2
2-hydroxymuconate semialdehyde
C3W4L8, C3W4L9, C3W4M0, C3W4M1, C3W4M2, C3W4M3, C3W4M4, C3W4M5, C3W4M6, C3W4M7
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
E7DDG2
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
A7LB47
-
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
-
the enzyme is constitutively transcribed
-
-
?
catechol + O2
2-hydroxymuconate-6-semialdehyde
V5W6K5
the enzyme is constitutively transcribed
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe3+
-
the enzyme activity increases in the presence of Fe3+ (isoform C23O2 shows 377.37% activity at 5 mM)
Iron
Fe2+
-
incubation of the purified enzyme (PheB) with Fe2+ and ascorbate increases its activity by approximately sevenfold
Fe2+
-
FeCl2 and FeSO4 activate metapyrocatechase 2, no effect on metapyrocatechase 1
Fe2+
-
the activity loss following H2O2 treatment is directly correlated with nearly stoichiometric titration of the active site Fe2+
Fe2+
-
3 gatom of iron per mol of enzyme; activity is closely related to specific content of iron in this protein
Fe2+
-
3.7 mol of iron per mol of enzyme or 0.93 mol per mol of the subunit
Fe2+
-
enzyme might undergo oxidation of its active-site ferrous iron atom
Fe2+
-
the active site comprises three Fe2+ ligands His153, His214 and Glu265
Fe2+
Fe2þ ion binding is facilitated via four ligands: two histidine residues, one glutamate residue and one molecule of water, overview
Fe2+
-
the enzyme activity increases in the presence of Fe2+ (isoform C23O1 shows 265.65% activity at 5 mM)
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-vinylcatechol
-
C23O activity (TodE) is almost completely abrogated by exposure to 0.2 mM 3-vinylcatechol
Cd2+
-
minimal inhibitory concentrations cadmium to Variovorax sp. 12S strain in different media, overview
NaN3
-
the immobilized enzyme is less sensitive compared to the free enzyme
catechol
-
wild-type enzyme: substrate inhibition. Mutant enzyme E286K: no substrate inhibition
CuSO4
-
the immobilized enzyme is less sensitive compared to the free enzyme
H2O2
-
complete inhibition at 0.06 mM, addition of ascorbic acid suppresses the inhibitory effect of hydrogen peroxide
H2O2
-
the immobilized enzyme is less sensitive compared to the free enzyme
additional information
-
C23O activity (TodE) is unaffected by styrene, toluene, and 3-methylcatechol
-
additional information
-
not inhibitory: EDTA, o-phenanthroline, 2,2'-dipyridyl
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
-
incubation of the purified enzyme (PheB) with Fe2+ and ascorbate increases its activity by approximately sevenfold
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0003
2,2',3-trihydroxybiphenylether
pH and temperature not specified in the publication
-
0.0012
2,3-Dihydroxybiphenyl
pH and temperature not specified in the publication