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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-chlorophenol + NADH + H+ + O2
? + NAD+ + H2O
poor substrate
-
-
?
3-cresol + NADH + H+ + O2
? + 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 + NAD(P)H + H+ + O2
1,2,4-trihydroxybenzene + 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
2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
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-nitrocatechol + NADPH + H+ + O2
?
-
-
-
?
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
-
-
?
additional information
?
-
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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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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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