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evolution

Q6F4M8 AND Q6F4M9
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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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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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
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-
?
3-cresol + NADH + H+ + O2
? + 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
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-
?
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
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monooxygenation, the enzyme completely degrades 0.1 mM 4-nitrocatechol in 80 min
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?
4-nitrocatechol + NADPH + H+ + O2
?
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?
4-nitrophenol + NADH + H+ + O2
2-hydroxy-1,4-benzoquinone + 1,2,4-trihydroxybenzene + nitrite + NAD+ + H2O
best substrate
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?
phenol + NADH + H+ + O2
hydroquinone + ? + NAD+ + H2O
poor substrate
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-
?
additional information
?
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4-nitrocatechol + NAD(P)H + H+ + O2

1,2,4-trihydroxybenzene + nitrite + NAD(P)+ + H2O
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about 31.2% of the nitro substituent of 4-nitrocatechol (initial concentration of 0.2 mM) is cleaved to yield nitrite over 2 h
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?
4-nitrocatechol + NAD(P)H + H+ + O2
1,2,4-trihydroxybenzene + nitrite + NAD(P)+ + H2O
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about 31.2% of the nitro substituent of 4-nitrocatechol (initial concentration of 0.2 mM) is cleaved to yield nitrite over 2 h
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-
?
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
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-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
Q6F4M8 AND Q6F4M9
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-
-
?
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
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-
-
?
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

?
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hydroquinone, resorcinol, and catechol are not substrates for NpdA2
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additional information
?
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NADPH does not support 4-nitrophenol or 4-nitrocatechol oxidation
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additional information
?
-
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NADPH does not support 4-nitrophenol or 4-nitrocatechol oxidation
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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. 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