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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
- burkholderia
-
monooxygenation
-
1,2-dioxygenase
- catechols
- hydroxyquinol
- putida
- fad
- p-benzoquinone
-
two-component
- pesticides
- 1,4-benzoquinone
-
para-benzoquinone
- flavin
-
single-component
-
priority
- dioxygenase
-
arthrobacter
- maleylacetate
- chlorophenol
-
procheck
-
prosa
- fenitrothion
-
cepacia
-
glide
-
trihydroxybenzene
-
reliability
- 2-chloro-4-nitrophenol
-
maestro
-
desmond
- sphaericus
- methylhydroquinone
- semialdehyde
- flavoprotein
-
dinucleotide-dependent
- 3-methyl-4-nitrophenol
-
errat
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
pentachlorophenol-4-monooxygenase
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
5-chlorohydroxyquinol + ? + 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
-
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
-
-
-
?
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
-
-
-
?
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
-
-
?
additional information
?
-
-
hydroquinone, resorcinol, and catechol are not substrates for NpdA2
-
-
?
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
-
-
-
?
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
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
dependent on, negligible activity is observed when FMN replaces FAD
FAD
-
required for full activity. The reductase component of the enzyme has a loosely bound FAD
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
addition of Mg2+ or Mn2+ ions has no effect on the activity
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
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
0.0013
-
cell extract, using 4-nitrocatechol as substrate, at pH 8.0 and 30°C
0.0013
-
cell extract, 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. 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
-
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
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A2N9BK27_STRCX
163
0
17040
TrEMBL
-
A0A644VLQ3_9ZZZZ
497
0
54048
TrEMBL
other Location (Reliability: 5)
A0A418SIQ7_9RHOB
497
0
53951
TrEMBL
-
A0A101RYH0_9ACTN
169
0
17812
TrEMBL
-
A0A1Y2NUP8_STRFR
174
0
18427
TrEMBL
-
A0A1Y2NSU8_STRFR
179
0
18128
TrEMBL
-
A0A1V5RWM9_9CHLR
170
0
18621
TrEMBL
-
A0A6J5K659_9BURK
172
0
19187
TrEMBL
-
A0A2C9D0J7_9RHIZ
495
0
53705
TrEMBL
-
A0A1V5RWN6_9CHLR
157
1
17003
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., Sphingomonas sp. UG30
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. (D2STN9), Pseudomonas sp., Pseudomonas sp. 1-7 (D2STN9)
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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