1.14.13.166: 4-nitrocatechol 4-monooxygenase
This is an abbreviated version!
For detailed information about 4-nitrocatechol 4-monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.166
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1.14.13.166
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hydroquinone
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fad
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1,2-dioxygenase
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burkholderia
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monooxygenation
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putida
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catechols
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hydroxyquinol
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two-component
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single-component
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p-benzoquinone
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1,4-benzoquinone
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para-benzoquinone
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arthrobacter
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2-chloro-4-nitrophenol
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flavin
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pesticides
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dioxygenase
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priority
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maleylacetate
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ortho
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trihydroxybenzene
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chlorophenol
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glide
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dinucleotide-dependent
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flavin-dependent
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prosa
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bioremediation
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insecticide
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maestro
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sphaericus
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3-methyl-4-nitrophenol
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cepacia
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fenitrothion
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semialdehyde
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procheck
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errat
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parathion
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methylhydroquinone
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desmond
- 1.14.13.166
- hydroquinone
- fad
-
1,2-dioxygenase
- burkholderia
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monooxygenation
- putida
- catechols
- hydroxyquinol
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two-component
-
single-component
- p-benzoquinone
- 1,4-benzoquinone
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para-benzoquinone
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arthrobacter
- 2-chloro-4-nitrophenol
- flavin
- pesticides
- dioxygenase
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priority
- maleylacetate
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ortho
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trihydroxybenzene
- chlorophenol
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glide
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dinucleotide-dependent
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flavin-dependent
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prosa
-
bioremediation
-
insecticide
-
maestro
- sphaericus
- 3-methyl-4-nitrophenol
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cepacia
- fenitrothion
- semialdehyde
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procheck
-
errat
- parathion
- methylhydroquinone
-
desmond
Reaction
Synonyms
4-nitrophenol 4-monooxygenase/4-nitrocatechol 2-monooxygenase, NpcA, npcB, NpdA2, p-nitrophenol monooxygenase, p-nitrophenol monooxygenase-II, para-nitrophenol 4-monooxygenase, PdcA, pentachlorophenol-4-monooxygenase, PNP 4-monooxygenase, PNP monooxygenase, pnpA, two-component PNP monooxygenase
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General Information
General Information on EC 1.14.13.166 - 4-nitrocatechol 4-monooxygenase
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evolution
metabolism
physiological function
additional information
PNP monooxygenase belongs to a two-component flavin-diffusible monooxygenase family
evolution
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PNP monooxygenase belongs to a two-component flavin-diffusible monooxygenase family
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the enzyme PNP monoxygenase is involved in the degradation of 4-nitrophenol, proposed pathway, overview. 4-Nitrophenol is converted to 4-nitrocatechol by a 4-nitrophenol 2-monooxygenase, EC 1.14.13.29, of the enzyme, which is subsequently converted to 2-hydroxy-1,4-benzoquinone, EC 1.14.13.166
metabolism
the enzyme PNP monoxygenase is involved in the degradation of 4-nitrophenol, proposed pathway, overview. 4-Nitrophenol is converted to 4-nitrocatechol by a 4-nitrophenol 2-monooxygenase, EC 1.14.13.29, of the enzyme, which is subsequently converted to 2-hydroxy-1,4-benzoquinone, EC 1.14.13.166
metabolism
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the enzyme PNP monoxygenase is involved in the degradation of 4-nitrophenol, proposed pathway, overview. 4-Nitrophenol is converted to 4-nitrocatechol by a 4-nitrophenol 2-monooxygenase, EC 1.14.13.29, of the enzyme, which is subsequently converted to 2-hydroxy-1,4-benzoquinone, EC 1.14.13.166
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the enzyme comprises two components, a flavoprotein reductase and an oxygenase, catalyzes the initial two sequential monooxygenations to convert 4-nitrophenol to trihydroxybenzene, EC 1.14.13.29 and EC 1.14.13.166
physiological function
the enzyme comprises two components, a flavoprotein reductase and an oxygenase, catalyzes the initial two sequential monooxygenations to convert 4-nitrophenol to trihydroxybenzene, EC 1.14.13.29 and EC 1.14.13.166
physiological function
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the enzyme comprises two components, a flavoprotein reductase and an oxygenase, catalyzes the initial two sequential monooxygenations to convert 4-nitrophenol to trihydroxybenzene, EC 1.14.13.29 and EC 1.14.13.166
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enzyme structure homology model for PNP monooxygenase using crystal structure of chlorophenol 4-monooxygenase from Burkholderia cepacia AC1100, PDB IS 3HWC, as template. Molecular dynamics simulations performed for docking complexes show the stable interaction between enzyme and substrate 4-nitrocatechol. Docking of substrates into the active site of PNP monooxygenase, Arg100, Gln158 and Thr193 are the key catalytic residues, overview
additional information
enzyme structure homology model for PNP monooxygenase using crystal structure of chlorophenol 4-monooxygenase from Burkholderia cepacia AC1100, PDB IS 3HWC, as template. Molecular dynamics simulations performed for docking complexes show the stable interaction between enzyme and substrate 4-nitrocatechol. of substrates into the active site of PNP monooxygenase, overview
additional information
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enzyme structure homology model for PNP monooxygenase using crystal structure of chlorophenol 4-monooxygenase from Burkholderia cepacia AC1100, PDB IS 3HWC, as template. Molecular dynamics simulations performed for docking complexes show the stable interaction between enzyme and substrate 4-nitrocatechol. Docking of substrates into the active site of PNP monooxygenase, Arg100, Gln158 and Thr193 are the key catalytic residues, overview
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