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
-
mixed-function
-
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
-
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
ECTree
1.13.11.2 catechol 2,3-dioxygenaseAdvanced search results
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results (Organism
Organism on EC 1.13.11.2 - catechol 2,3-dioxygenase
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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
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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.
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no activity 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.
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no activity 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.
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strain Pmen PC1 - strain Pmen PC12 and Pmen PC19, all analysed stains contain catechol 2,3-dioxygenase genes
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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
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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.
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activity detected with 2-hydroxyboenzothiazole as growth substrate
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activity detected with 2-hydroxyboenzothiazole as growth substrate
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enzyme subgroup I.2.B, hybrid enzymes with type I.2.A enzyme from Pseudomonas sp.
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isolated from the marine sediment, chromosomal-encoded gene nahH
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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
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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
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enzyme subgroup I.2.A, hybrid enzymes with type I.2.B enzyme from Sphingomonas sp.
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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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UniProt
