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IUBMB Comments Contains FAD. The enzyme, isolated from the bacterium Burkholderia sp. DNT, can use both NADH and NADPH, but prefers NADPH. It has a narrow substrate range, but can also act on 4-nitrocatechol.
The enzyme appears in viruses and cellular organisms
Synonyms
mnc monooxygenase, mnc oxygenase, 4-methyl-5-nitrocatechol monooxygenase, 4m5nc monooxygenase,
more
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4-methyl-5-nitrocatechol monooxygenase
4-methyl-5-nitrocatechol oxygenase
4-methyl-5-nitrocatechol monooxygenase
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4-methyl-5-nitrocatechol monooxygenase
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4-methyl-5-nitrocatechol oxygenase
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4-methyl-5-nitrocatechol oxygenase
P71029
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4-methyl-5-nitrocatechol oxygenase
P71029
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4M5NC monooxygenase
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dntB
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MNC
P71029
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MNC monooxygenase
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MNC monooxygenase
P71029
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MNC monooxygenase
P71029
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MNC oxygenase
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4-methyl-5-nitrocatechol + NAD(P)H + H+ + O2 = 2-hydroxy-5-methylquinone + nitrite + NAD(P)+ + H2O
4-methyl-5-nitrocatechol + NAD(P)H + H+ + O2 = 2-hydroxy-5-methylquinone + nitrite + NAD(P)+ + H2O
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4-methyl-5-nitrocatechol + NAD(P)H + H+ + O2 = 2-hydroxy-5-methylquinone + nitrite + NAD(P)+ + H2O
mechanism of removal of the nitro group from 4-methyl-5-nitrocatechol and subsequent reactions leading to ring fission, overview
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4-methyl-5-nitrocatechol + NAD(P)H + H+ + O2 = 2-hydroxy-5-methylquinone + nitrite + NAD(P)+ + H2O
mechanism of removal of the nitro group from 4-methyl-5-nitrocatechol and subsequent reactions leading to ring fission, overview
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4-methyl-5-nitrocatechol,NAD(P)H:oxygen 5-oxidoreductase (5-hydroxylating, nitrite-forming)
Contains FAD. The enzyme, isolated from the bacterium Burkholderia sp. DNT, can use both NADH and NADPH, but prefers NADPH. It has a narrow substrate range, but can also act on 4-nitrocatechol.
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3-methyl-4-nitrophenol + O2 + NADPH + H+
2-methyl-4-benzoquinone + nitrite + H2O + NADP+
4-methyl-5-nitrocatechol + O2 + NADPH + H+
2-hydroxy-5-methylquinone + nitrite + H2O + NADP+
4-nitrophenol + O2 + NADPH + H+
4-benzoquinone + nitrite + H2O + NADP+
5-nitrocatechol + O2 + NADPH + H+
2-hydroxyquinone + nitrite + H2O + NADP+
additional information
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3-methyl-4-nitrophenol + O2 + NADPH + H+
2-methyl-4-benzoquinone + nitrite + H2O + NADP+
low activity with the wild-type enzyme, higher activity with enzyme mutant M22L/L380I
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3-methyl-4-nitrophenol + O2 + NADPH + H+
2-methyl-4-benzoquinone + nitrite + H2O + NADP+
low activity with the wild-type enzyme, higher activity with enzyme mutant M22L/L380I
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4-methyl-5-nitrocatechol + O2 + NADPH + H+
2-hydroxy-5-methylquinone + nitrite + H2O + NADP+
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4-methyl-5-nitrocatechol + O2 + NADPH + H+
2-hydroxy-5-methylquinone + nitrite + H2O + NADP+
P71029
the enzyme is highly specific for 4-methyl-5-nitrocatechol
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4-methyl-5-nitrocatechol + O2 + NADPH + H+
2-hydroxy-5-methylquinone + nitrite + H2O + NADP+
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4-methyl-5-nitrocatechol + O2 + NADPH + H+
2-hydroxy-5-methylquinone + nitrite + H2O + NADP+
P71029
the enzyme is highly specific for 4-methyl-5-nitrocatechol
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4-methyl-5-nitrocatechol + O2 + NADPH + H+
2-hydroxy-5-methylquinone + nitrite + H2O + NADP+
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4-methyl-5-nitrocatechol + O2 + NADPH + H+
2-hydroxy-5-methylquinone + nitrite + H2O + NADP+
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4-nitrophenol + O2 + NADPH + H+
4-benzoquinone + nitrite + H2O + NADP+
P71029
58% of the activity with 4-methyl-5-nitrocatechol
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4-nitrophenol + O2 + NADPH + H+
4-benzoquinone + nitrite + H2O + NADP+
low activity with the wild-type enzyme, higher activity with enzyme mutant M22L/L380I
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4-nitrophenol + O2 + NADPH + H+
4-benzoquinone + nitrite + H2O + NADP+
low activity with the wild-type enzyme, higher activity with enzyme mutant M22L/L380I
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4-nitrophenol + O2 + NADPH + H+
4-benzoquinone + nitrite + H2O + NADP+
P71029
58% of the activity with 4-methyl-5-nitrocatechol
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5-nitrocatechol + O2 + NADPH + H+
2-hydroxyquinone + nitrite + H2O + NADP+
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5-nitrocatechol + O2 + NADPH + H+
2-hydroxyquinone + nitrite + H2O + NADP+
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additional information
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the enzyme DntB has a very narrow substrate range
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additional information
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the enzyme DntB has a very narrow substrate range
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additional information
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P71029
the enzyme has a narrow substrate specificity. 3-Methyl-4-nitrophenol, 3-methyl-4-nitrocatechol, 4-nitrophenol, 3-nitrophenol, and 4-chlorocatechol are no substrates
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additional information
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the enzyme DntB has a very narrow substrate range
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additional information
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P71029
the enzyme has a narrow substrate specificity. 3-Methyl-4-nitrophenol, 3-methyl-4-nitrocatechol, 4-nitrophenol, 3-nitrophenol, and 4-chlorocatechol are no substrates
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4-methyl-5-nitrocatechol + O2 + NADPH + H+
2-hydroxy-5-methylquinone + nitrite + H2O + NADP+
4-methyl-5-nitrocatechol + O2 + NADPH + H+
2-hydroxy-5-methylquinone + nitrite + H2O + NADP+
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4-methyl-5-nitrocatechol + O2 + NADPH + H+
2-hydroxy-5-methylquinone + nitrite + H2O + NADP+
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4-methyl-5-nitrocatechol + O2 + NADPH + H+
2-hydroxy-5-methylquinone + nitrite + H2O + NADP+
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4-methyl-5-nitrocatechol + O2 + NADPH + H+
2-hydroxy-5-methylquinone + nitrite + H2O + NADP+
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NADH
P71029
the enzyme uses either NADH or NADPH as electron donors, and NADPH is the preferred cofactor
FAD
enzyme DntB is a flavoprotein
FAD
P71029
the purified enzyme contains 1 mol of FAD per mol of protein
NADPH
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NADPH
P71029
the enzyme uses either NADH or NADPH as electron donors, and NADPH is the preferred cofactor
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4-nitrophenol
inhibitory at concentrations above 1 mM
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additional information
additional information
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0.1
4-nitrophenol
mutant M22L/L380I, pH 8.0, 37°C
0.35
4-nitrophenol
wild-type enzyme, pH 8.0, 37°C
additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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0.014 - 0.015
4-nitrophenol
0.014
4-nitrophenol
wild-type enzyme, pH 8.0, 37°C
0.015
4-nitrophenol
mutant M22L/L380I, pH 8.0, 37°C
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0.04 - 0.45
4-nitrophenol
0.04
4-nitrophenol
wild-type enzyme, pH 8.0, 37°C
0.45
4-nitrophenol
mutant M22L/L380I, pH 8.0, 37°C
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0.03
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strain DNT grown on yeast extract, pH and temperature not specified in the publication
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gene dntB
UniProt
brenda
gene dntB
P71029
UniProt
brenda
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brenda
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brenda
gene dntB
UniProt
brenda
gene dntB
P71029
UniProt
brenda
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evolution
P71029
enzyme DntB contains the highly conserved ADP and flavin adenine dinucleotide (FAD) binding motifs characteristic of flavoprotein hydroxylases
evolution
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enzyme DntB contains the highly conserved ADP and flavin adenine dinucleotide (FAD) binding motifs characteristic of flavoprotein hydroxylases
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metabolism
4-methyl-5-nitrocatechol monooxygenase catalyzes the second step of 2,4-dinitrotoluene degradation by converting 4-methyl-5-nitrocatechol to 2-hydroxy-5-methylquinone with the concomitant removal of the nitro group
metabolism
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4-methyl-5-nitrocatechol monooxygenase catalyzes the second step of 2,4-dinitrotoluene degradation by converting 4-methyl-5-nitrocatechol to 2-hydroxy-5-methylquinone with the concomitant removal of the nitro group
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DNTB_BURSP
Burkholderia sp
548
1
59083
Swiss-Prot
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A0A6J5FJM7_9BURK
549
0
60519
TrEMBL
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A0A6S6Z5Z4_9BURK
549
0
60506
TrEMBL
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A0A6J5ADT7_9BURK
549
0
60348
TrEMBL
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A0A6S7A208_9BURK
543
1
59910
TrEMBL
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A0A6S7B874_9BURK
493
1
54855
TrEMBL
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60200
P71029
1 * 60200, SDS-PAGE
65000
P71029
gel filtration
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monomer
P71029
1 * 60200, SDS-PAGE
monomer
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1 * 60200, SDS-PAGE
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L380I
site-directed mutagenesis, the mutant shows unaltered activity with 4-nitrophenol compared to the wild-type enzyme
M22L
site-directed mutagenesis, the mutant shows slightly reduced activity with 4-nitrophenol compared to the wild-type enzyme
M22L/L380I
error-prone PCR, protein engineering for nitrite removal, the mutant enzyme accepts two addtional substrates 4-nitrophenol and 3-methyl-4-nitrophenol. With 4-nitrophenol, the initial rate of the mutant M22L/L380I enzyme is 10fold higher than that of the wild-type enzyme, the catalytic efficiency for 4-nitrophenol degradation is 11fold higher, and with 3-methyl-4-nitrophenol, the initial rate is 4fold higher compared to the wild-type enzyme
M22L/L380M
simultaneous saturation mutagenesis, the mutant shows slightly reduced activity with 4-nitrophenol compared to the wild-type enzyme
M22S/L380V
simultaneous saturation mutagenesis, the mutant shows 20% enhanced degradation of 4-nitrophenol compared to mutant M22L/L380I
L380I
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site-directed mutagenesis, the mutant shows unaltered activity with 4-nitrophenol compared to the wild-type enzyme
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M22L
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site-directed mutagenesis, the mutant shows slightly reduced activity with 4-nitrophenol compared to the wild-type enzyme
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M22L/L380I
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error-prone PCR, protein engineering for nitrite removal, the mutant enzyme accepts two addtional substrates 4-nitrophenol and 3-methyl-4-nitrophenol. With 4-nitrophenol, the initial rate of the mutant M22L/L380I enzyme is 10fold higher than that of the wild-type enzyme, the catalytic efficiency for 4-nitrophenol degradation is 11fold higher, and with 3-methyl-4-nitrophenol, the initial rate is 4fold higher compared to the wild-type enzyme
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M22L/L380M
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simultaneous saturation mutagenesis, the mutant shows slightly reduced activity with 4-nitrophenol compared to the wild-type enzyme
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M22S/L380V
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simultaneous saturation mutagenesis, the mutant shows 20% enhanced degradation of 4-nitrophenol compared to mutant M22L/L380I
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native enzme to homogeneity from strain DNT by anion exchange chromatography and gel filtration
P71029
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
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gene dntB, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain TG1
gene dntB, sequence comparisons
P71029
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Leungsakul, T.; Johnson, G.R.; Wood, T.K.
Protein engineering of the 4-methyl-5-nitrocatechol monooxygenase from Burkholderia sp. strain DNT for enhanced degradation of nitroaromatics
Appl. Environ. Microbiol.
72
3933-3939
2006
Burkholderia sp. (Q2PWU9), Burkholderia sp., Burkholderia sp. DNT (Q2PWU9)
brenda
Haigler, B.E.; Nishino, S.F.; Spain, J.C.
Biodegradation of 4-methyl-5-nitrocatechol by Pseudomonas sp. strain DNT
J. Bacteriol.
176
3433-3437
1994
Pseudomonas sp., Pseudomonas sp. DNT
brenda
Haigler, B.E.; Suen, W.C.; Spain, J.C.
Purification and sequence analysis of 4-methyl-5-nitrocatechol oxygenase from Burkholderia sp. strain DNT
J. Bacteriol.
178
6019-6024
1996
Burkholderia sp. (P71029), Burkholderia sp. RASC (P71029)
brenda
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