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Information on EC 1.14.13.166 - 4-nitrocatechol 4-monooxygenase
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1.14.13.166 4-nitrocatechol 4-monooxygenaseIUBMB Comments
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 . 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 .
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Word Map
- 1.14.13.166
- hydroquinone
-
monooxygenation
-
1,2-dioxygenase
- burkholderia
- putida
- fad
- hydroxyquinol
- p-benzoquinone
- catechols
-
para-benzoquinone
- maleylacetate
-
single-component
- 1,4-benzoquinone
-
arthrobacter
-
priority
- pesticides
-
two-component
- dioxygenase
- flavin
-
cepacia
-
trihydroxybenzene
-
glide
- semialdehyde
-
errat
- flavoprotein
-
reliability
-
enzyme-substrate
-
manufacturing
- 3-methyl-4-nitrophenol
-
desmond
- methylhydroquinone
- 2-chloro-4-nitrophenol
- fenitrothion
-
prosa
-
maestro
- chlorophenol
-
procheck
-
dinucleotide-dependent
- sphaericus
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-nitrophenol 4-monooxygenase/4-nitrocatechol 2-monooxygenase
NpcA
npcB
p-nitrophenol monooxygenase-II
para-nitrophenol 4-monooxygenase
PdcA
PNP 4-monooxygenase
PNP monooxygenase
pnpA
two-component PNP monooxygenase
4-nitrophenol 4-monooxygenase/4-nitrocatechol 2-monooxygenase
UniProt
4-nitrophenol 4-monooxygenase/4-nitrocatechol 2-monooxygenase
UniProt
4-nitrophenol 4-monooxygenase/4-nitrocatechol 2-monooxygenase
UniProt
-
PNP monooxygenase
-
the enzyme system consists of two components that catalyze two consecutive monooxygenation reactions
PNP monooxygenase
-
the enzyme system consists of two components that catalyze two consecutive monooxygenation reactions
-
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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 SOURCE
PATHWAYS
MetaCyc
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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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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 + 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 + NADPH + H+ + O2
1,2,4-trihydroxybenzene + nitrite + NADP+ + H2O
-
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
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 + 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
D2STN9
-
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
D2STN9
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
additional information
?
-
hydroquinone, resorcinol, and catechol are not substrates for NpdA2
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-
-
additional information
?
-
-
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 SUBSTRATE
NATURAL 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
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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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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INHIBITOR
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
PNP monooxygenase belongs to a two-component flavin-diffusible monooxygenase family
evolution
-
PNP monooxygenase belongs to a two-component flavin-diffusible monooxygenase family
-
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
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
-
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
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
-
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
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. Docking of substrates into the active site of PNP monooxygenase, Arg100, Gln158 and Thr193 are the key catalytic residues, overview
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A0A1Y2NUP8_STRFR
174
0
18427
TrEMBL
A0A1V5RWN6_9CHLR
157
1
17003
TrEMBL
A0A2N9BK27_STRCX
163
0
17040
TrEMBL
A0A418SIQ7_9RHOB
497
0
53951
TrEMBL
A0A1V5RWM9_9CHLR
170
0
18621
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Leung, K.T.; Campbell, S.; Gan, Y.; White, D.C.; Lee, H.; Trevors, J.T.
The role of the Sphingomonas species UG30 pentachlorophenol-4-monooxygenase in p-nitrophenol degradation
FEMS Microbiol. Lett.
173
247-253
1999
Sphingomonas sp.
brenda
Kadiyala, V.; Spain, J.C.
A two-component monooxygenase catalyzes both the hydroxylation of p-nitrophenol and the oxidative release of nitrite from 4-nitrocatechol in Bacillus sphaericus JS905
Appl. Environ. Microbiol.
64
2479-2484
1998
Lysinibacillus sphaericus, Lysinibacillus sphaericus JS905
brenda
Zhang, J.J.; Liu, H.; Xiao, Y.; Zhang, X.E.; Zhou, N.Y.
Identification and characterization of catabolic para-nitrophenol 4-monooxygenase and para-benzoquinone reductase from Pseudomonas sp. strain WBC-3
J. Bacteriol.
191
2703-2710
2009
Pseudomonas sp. (C1I201), Pseudomonas sp.
brenda
Wei, M.; Zhang, J.J.; Liu, H.; Zhou, N.Y.
para-Nitrophenol 4-monooxygenase and hydroxyquinol 1,2-dioxygenase catalyze sequential transformation of 4-nitrocatechol in Pseudomonas sp. strain WBC-3
Biodegradation
21
915-921
2010
Pseudomonas sp.
brenda
Liu, W.; Shen, W.; Zhao, X.; Cao, H.; Cui, Z.
Expression, purification, crystallization and preliminary X-ray analysis of para-nitrophenol 4-monooxygenase from Pseudomonas putida DLL-E4
Acta Crystallogr. Sect. F
65
1004-1006
2009
Pseudomonas putida (C6FI48), Pseudomonas putida DLL-E4 (C6FI48), Pseudomonas putida DLL-E4
brenda
Zhang, S.; Sun, W.; Xu, L.; Zheng, X.; Chu, X.; Tian, J.; Wu, N.; Fan, Y.
Identification of the para-nitrophenol catabolic pathway, and characterization of three enzymes involved in the hydroquinone pathway, in Pseudomonas sp. 1-7
BMC Microbiol.
12
27
2012
Pseudomonas sp. 1-7 (D2STN9), Pseudomonas sp. (D2STN9), Pseudomonas sp.
brenda
Perry, L.; Zylstra, G.
Cloning of a gene cluster involved in the catabolism of p-nitrophenol by Arthrobacter sp. strain JS443 and characterization of the p-nitrophenol monooxygenase
J. Bacteriol.
189
7563-7572
2007
Arthrobacter sp. (A7YVV2), Arthrobacter sp.
brenda
Min, J.; Zhang, J.; Zhou, N.
A two-component para-nitrophenol monooxygenase initiates a novel 2-chloro-4-nitrophenol catabolism pathway in Rhodococcus imtechensis RKJ300
Appl. Environ. Microbiol.
82
714-723
2016
no activity in Rhodococcus imtechensis
brenda
Kallubai, M.; Amineni, U.; Mallavarapu, M.; Kadiyala, V.
In silico approach to support that p-nitrophenol monooxygenase from Arthrobacter sp. strain JS443 catalyzes the initial two sequential monooxygenations
Interdiscip. Sci. Comput. Life Sci.
7
157-167
2015
Arthrobacter sp. JS443 (A7YVV2), Lysinibacillus sphaericus (Q6F4M8 AND Q6F4M9), Lysinibacillus sphaericus JS905 (Q6F4M8 AND Q6F4M9)
brenda
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