1.13.11.2: catechol 2,3-dioxygenase
This is an abbreviated version!
For detailed information about catechol 2,3-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.2
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1.13.11.2
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heme
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putida
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carboxylase
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hydroxylase
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rubisco
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ferredoxins
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ribulose-1,5-bisphosphate
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l-arginine
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non-heme
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rieske
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tetrahydrobiopterin
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dioxygenation
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ribulose
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toluene
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2-oxoglutarate
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naphthalene
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biphenyls
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rhodococcus
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fmn
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nnos
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bioremediation
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mixed-function
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nitric-oxide
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phenanthrene
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photorespiration
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photorespiratory
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1,5-bisphosphate
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biliverdin
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bh4
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l-citrulline
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sphingomonas
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ring-hydroxylating
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comamonas
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dihydroxylation
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carbazole
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xylene
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l-arg
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2-oxoglutarate-dependent
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heme-heme
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diiron
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ironii
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4-methylcatechol
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monooxygenation
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rubp
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testosteroni
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sphingobium
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ethylbenzene
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4.1.1.39
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degradation
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environmental protection
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fluoranthene
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rhodochrous
- 1.13.11.2
- heme
- putida
- carboxylase
- hydroxylase
- rubisco
- ferredoxins
- ribulose-1,5-bisphosphate
- l-arginine
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non-heme
-
rieske
- tetrahydrobiopterin
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dioxygenation
- ribulose
- toluene
- 2-oxoglutarate
- naphthalene
- biphenyls
- rhodococcus
- fmn
- nnos
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bioremediation
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mixed-function
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nitric-oxide
- phenanthrene
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photorespiration
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photorespiratory
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1,5-bisphosphate
- biliverdin
- bh4
- l-citrulline
- sphingomonas
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ring-hydroxylating
- comamonas
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dihydroxylation
- carbazole
- xylene
- l-arg
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2-oxoglutarate-dependent
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heme-heme
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diiron
-
ironii
- 4-methylcatechol
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monooxygenation
- rubp
- testosteroni
- sphingobium
- ethylbenzene
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4.1.1.39
- degradation
- environmental protection
- fluoranthene
- rhodochrous
Reaction
Synonyms
2,3-dihydroxybenzenesulfonate 2,3-dioxygenase, 3-sulfocatechol-2,3-dioxygenase, 3SC23O, A23O, AtdB, BupB, C2,3O, C23D, C23o, C23O-2G, C23O1, C23O2, C23Os, CatE, catechol 2,3 dioxygenase, catechol 2,3-di-2,3-pyrocatechase, catechol 2,3-dioxygenase, catechol 2,3-oxygenase, catechol oxygenase, catechol-2,3-dioxygenase, CbzE, CD-2,3, EC 1.13.1.2, ECDO, extradiol dioxygenase MhpB, Extradiol-cleaving catecholic dioxygenase, meta-cleavage dioxygenase, metapyrocatechase, More, oxygenase, PheB, pyrocatechol 2,3-dioxygenase, Saci_2295, SSO1223, SsoC2,3O, ssol_2912, tbuE, TdnC, TodE, XylE
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General Information
General Information on EC 1.13.11.2 - catechol 2,3-dioxygenase
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evolution
malfunction
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inactivation of TodE and the subsequent accumulation of 3-vinylcatechol results in toxicity and cell death
metabolism
physiological function
additional information
the enzyme belongs to the single-ring substrate subfamily of the extradiol dioxygenase
evolution
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the enzyme belongs to the single-ring substrate subfamily of the extradiol dioxygenase
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the enzyme catalyzes a step in the degradation of phenanthrene, overview
metabolism
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the enzyme catalyzes a step in the degradation of phenanthrene, overview
metabolism
the enzyme catalyzes a step in the degradation of phenanthrene, overview
metabolism
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the enzyme catalyzes a step in the degradation of phenanthrene, overview
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metabolism
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the enzyme catalyzes a step in the degradation of phenanthrene, overview
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metabolism
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the enzyme catalyzes a step in the degradation of phenanthrene, overview
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catechol-2,3-dioxygenase contributes to quinone resistance
physiological function
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overexpressing TodE is necessary to allow Pseudomonas putida strain F1 to grow on styrene
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
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catechol 2,3-dioxygenases play a role in the degradation of monoaromatic hydrocarbons
physiological function
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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
important enzyme in many bacterial pathways for the degradation of aromatic compounds
physiological function
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key enzyme in the biodegradation of aromatic compounds
physiological function
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strain is able to degrade a solution containing benzene, toluene, ethylbenzene, and xylene at 7% NaCl (w/v) and pH 9
physiological function
the enzyme (XylE) is recruited in pathways that are involved in the degradation of chlorinated aromatic compounds such as pentachlorophenol. It is involved in pathways that generate catechol as a degradation pathway intermediate. XylE will also play a role in degradation pathways that produce alkylcatechols
physiological function
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catechol-2,3-dioxygenase contributes to quinone resistance
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physiological function
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catechol 2,3-dioxygenases play a role in the degradation of monoaromatic hydrocarbons
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physiological function
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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
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physiological function
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key enzyme in the biodegradation of aromatic compounds
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physiological function
Sphingobium scionense DSM 19371
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the enzyme (XylE) is recruited in pathways that are involved in the degradation of chlorinated aromatic compounds such as pentachlorophenol. It is involved in pathways that generate catechol as a degradation pathway intermediate. XylE will also play a role in degradation pathways that produce alkylcatechols
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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
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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
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the enzyme is a member of the superfamily I, subfamily 2A of extradiol dioxygenases
additional information
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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
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the enzyme is a member of the superfamily I, subfamily 2A of extradiol dioxygenases
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additional information
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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
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additional information
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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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