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Enzyme Nomenclature
Information on EC 1.14.13.166 - 4-nitrocatechol 4-monooxygenase
for references in articles please use BRENDA:EC1.14.13.166
Word Map on EC 1.14.13.166
- 1.14.13.166
- hydroquinone
-
monooxygenation
-
1,2-dioxygenase
- catechols
- burkholderia
- fad
- putida
-
pollutant
- hydroxyquinol
- flavin
-
two-component
- maleylacetate
- 1,4-benzoquinone
-
arthrobacter
-
para-benzoquinone
-
his-tagged
-
priority
-
single-component
- p-benzoquinone
- sphaericus
-
dioxygenase
-
trihydroxybenzene
-
semialdehyde
-
prosa
-
errat
-
pesticides
- 2-chloro-4-nitrophenol
-
procheck
-
desmond
-
flavoprotein
-
enzyme-substrate
-
glide
-
maestro
- chlorophenol
-
manufacturing
-
reliability
-
cepacia
-
dinucleotide-dependent
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.166
-
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RECOMMENDED NAME
GeneOntology No.
4-nitrocatechol 4-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-nitrocatechol + NAD(P)H + H+ + O2 = 2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
4-nitrocatechol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming)
Contains FAD. The enzyme catalyses the oxidation of 4-nitrocatechol with the concomitant removal of the nitro group as nitrite. Forms a two-component system with a flavoprotein reductase [1]. The enzymes from the bacteria Lysinibacillus sphaericus JS905 and Rhodococcus sp. strain PN1 were shown to also catalyse EC 1.14.13.29, 4-nitrophenol 2-monooxygenase [1,2] while the enzyme from Pseudomonas sp. WBC-3 was shown to also catalyse EC 1.14.13.167, 4-nitrophenol 4-monooxygenase [3].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
Q6F4M8 AND Q6F4M9
PNP monooxygenase belongs to a two-component flavin-diffusible monooxygenase family
evolution
-
PNP monooxygenase belongs to a two-component flavin-diffusible monooxygenase family
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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
Q6F4M8 AND Q6F4M9
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
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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
Q6F4M8 AND Q6F4M9
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
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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
Q6F4M8 AND Q6F4M9
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
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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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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
2,4,5-trichlorophenol + NADH + H+ + O2
2,5-dichlorohydroquinone + 5-chloro-2-hydroxyquinol + ? + NAD+ + H2O
poor substrate
-
-
?
2,4,6-trichlorophenol + NADH + H+ + O2
2,6-dichlorohydroquinone + 6-chloro-2-hydroxyquinol + ? + NAD+ + H2O
poor substrate
-
-
?
2,4-dinitrophenol + NADH + H+ + O2
2-nitrohydroquinone + nitrite + NAD+ + H2O
poor substrate
-
-
?
3-nitrophenol + NADH + H+ + O2
3-nitrohydroquinone + NAD+ + H2O
-
-
-
?
4-chlorocatechol + NADH + H+ + O2
1,2,4-trihydroxybenzene + ? + NAD+ + H2O
good substrate
-
-
?
4-chlorophenol + NADH + H+ + O2
1,2,4-trihydroxybenzene + 2-hydroxy-1,4-benzoquinone + ? + NAD+ + H2O
-
-
-
?
4-chlororesorcinol + NADH + H+ + O2
1,2,4-trihydroxybenzene + ? + NAD+ + H2O
good substrate
-
-
?
4-cresol + NADH + H+ + O2
4-hydroxy-4-methyl-2,5-cyclohexadien-1-one + NAD+ + H2O
poor substrate
-
-
?
4-methylcatechol + NADH + H+ + O2
? + NAD+ + H2O
poor substrate
-
-
?
4-nitrocatechol + NADPH + H+ + O2
1,2,4-trihydroxybenzene + nitrite + NADP+ + H2O
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monooxygenation, the enzyme completely degrades 0.1 mM 4-nitrocatechol in 80 min
-
-
?
4-nitrophenol + NADH + H+ + O2
2-hydroxy-1,4-benzoquinone + 1,2,4-trihydroxybenzene + nitrite + NAD+ + H2O
best substrate
-
-
?
phenol + NADH + H+ + O2
hydroquinone + ? + NAD+ + H2O
poor substrate
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
1,2,4-trihydroxybenzene + nitrite + NAD(P)+ + H2O
-
about 31.2% of the nitro substituent of 4-nitrocatechol (initial concentration of 0.2 mM) is cleaved to yield nitrite over 2 h
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
1,2,4-trihydroxybenzene + nitrite + NAD(P)+ + H2O
-
about 31.2% of the nitro substituent of 4-nitrocatechol (initial concentration of 0.2 mM) is cleaved to yield nitrite over 2 h
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
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-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
Q6F4M8 AND Q6F4M9
-
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
Q6F4M8 AND Q6F4M9
-
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
1,2,4-trihydroxybenzene + nitrite + NAD+ + H2O
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
1,2,4-trihydroxybenzene + nitrite + NAD+ + H2O
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
good substrate
-
-
?
4-nitrocatechol + NADH + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
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-
-
-
?
4-nitrocatechol + NADH + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
Q6F4M8 AND Q6F4M9
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
Q6F4M8 AND Q6F4M9
-
-
-
?
additional information
?
-
hydroquinone, resorcinol, and catechol are not substrates for NpdA2
-
-
-
additional information
?
-
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NADPH does not support 4-nitrophenol or 4-nitrocatechol oxidation
-
-
-
additional information
?
-
-
NADPH does not support 4-nitrophenol or 4-nitrocatechol oxidation
-
-
-
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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-nitrocatechol + NAD(P)H + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
A7YVV2
-
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
Q6F4M8 AND Q6F4M9
-
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
Q6F4M8 AND Q6F4M9
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-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
required for full activity. The reductase component of the enzyme has a loosely bound FAD
FAD
dependent on, negligible activity is observed when FMN replaces FAD
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
addition of Mg2+ or Mn2+ ions has no effect on the activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
alpha-naphthoflavone, miconazole, and metyrapone at 0.5 mM have very little effect (less than 5% inhibition) on enzyme activity
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0013
-
cell extract, using 4-nitrocatechol as substrate, at pH 8.0 and 30°C; cell extract, using 4-nitrophenol as substrate, at pH 8.0 and 30°C
0.038
-
after 28fold purification, using 4-nitrocatechol as substrate, at pH 8.0 and 30°C
0.04
-
after 32fold purification, using 4-nitrophenol as substrate, at pH 8.0 and 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 20 mM HEPES pH 7.0, 15% (w/v) PEG 4000 and 15% (v/v) 2-propanol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, extracts prepared without added FAD, 48 h, 52% loss of activity
-
0°C, storage medium, no loss of activity after several hours, 30% loss of activity after 12 h, 80% loss of activity after 40 h
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose column chromatography, Q-Sepharose column chromatography, and Sephacryl S-300 gel filtration
-
Ni-NTA agarose column chromatography and Sephadex G-100 gel filtration
Ni-NTA column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.166)
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