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2-chloro-4-nitrophenol + NADH + H+ + O2
2-chloro-4-nitrocatechol + NAD+ + H2O
2-chloro-4-nitrophenol + NADPH + O2
1,2,4-trihydroxybenzene + ?
3-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
1 mM NADH, 5 M FAD, 1 mM DTT, NphA1 (approximately 0.5 mg of purified protein), and NphA2 (approximately 0.1 mg of purified protein) in 1 ml of 50 mM Tris-HCl buffer, pH 8.0, slow degradation of substrate
-
-
?
3-nitrophenol + NADH + O2
?
-
-
-
-
?
4-chlorophenol + NADH + H+ + O2
4-chlorocatechol + NAD+ + H2O
1 mM NADH, 5 M FAD, 1 mM DTT, NphA1 (approximately 0.5 mg of purified protein), and NphA2 (approximately 0.1 mg of purified protein) in 1 ml of 50 mM Tris-HCl buffer, pH 8.0
-
-
?
4-nitrocatechol + NADH + H+ + O2
4-nitrobenzene-1,2,3-triol + NAD+ + H2O
4-nitrocatechol + NADPH + H+ + O2
4-nitrobenzene-1,2,3-triol + NADP+ + H2O
-
-
-
-
?
4-nitrophenol + NAD(P)H + H+ + O2
4-nitrocatechol + NAD(P)+ + H2O
4-nitrophenol + NAD(P)H + O2
4-nitrocatechol + NAD(P)+ + H2O
-
-
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
4-nitrophenol + NADH + O2
4-nitrocatechol + NAD+ + H2O
4-nitrophenol + NADPH + H+ + O2
4-nitrocatechol + NADP+ + H2O
-
-
-
-
?
4-nitrophenol + NADPH + O2
4-nitrocatechol + NADP+ + H2O
-
-
-
-
?
chlorzoxazone + NADH + O2
?
p-nitrophenol + NADH + H+ + O2
p-nitrocatechol + NAD+ + H2O
-
-
-
-
?
p-nitrophenol + NADPH + H+ + O2
p-nitrocatechol + NADP+ + H2O
-
200 microM substrate, 0.4 mg microsomal protein, 1 mM NADPH
-
-
?
phenol + NADH + H+ + O2
catechol + NAD+ + H2O
1 mM NADH, 5 M FAD, 1 mM DTT, NphA1 (approximately 0.5 mg of purified protein), and NphA2 (approximately 0.1 mg of purified protein) in 1 ml of 50 mM Tris-HCl buffer, pH 8.0
-
-
?
additional information
?
-
2-chloro-4-nitrophenol + NADH + H+ + O2
2-chloro-4-nitrocatechol + NAD+ + H2O
-
-
-
-
?
2-chloro-4-nitrophenol + NADH + H+ + O2
2-chloro-4-nitrocatechol + NAD+ + H2O
-
-
-
-
?
2-chloro-4-nitrophenol + NADH + H+ + O2
2-chloro-4-nitrocatechol + NAD+ + H2O
-
-
-
-
?
2-chloro-4-nitrophenol + NADPH + O2
1,2,4-trihydroxybenzene + ?
-
-
-
-
?
2-chloro-4-nitrophenol + NADPH + O2
1,2,4-trihydroxybenzene + ?
-
-
-
-
?
2-chloro-4-nitrophenol + NADPH + O2
1,2,4-trihydroxybenzene + ?
-
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
4-nitrobenzene-1,2,3-triol + NAD+ + H2O
-
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
4-nitrobenzene-1,2,3-triol + NAD+ + H2O
-
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
4-nitrobenzene-1,2,3-triol + NAD+ + H2O
-
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
4-nitrobenzene-1,2,3-triol + NAD+ + H2O
1 mM NADH, 5 M FAD, 1 mM DTT, NphA1 (approximately 0.5 mg of purified protein), and NphA2 (approximately 0.1 mg of purified protein) in 1 ml of 50 mM Tris-HCl buffer, pH 8.0, very slow degradation of substrate, no unambiguous identification of products by HPLC due to overlaps
-
-
?
4-nitrophenol + NAD(P)H + H+ + O2
4-nitrocatechol + NAD(P)+ + H2O
-
-
-
-
?
4-nitrophenol + NAD(P)H + H+ + O2
4-nitrocatechol + NAD(P)+ + H2O
-
-
-
-
?
4-nitrophenol + NAD(P)H + H+ + O2
4-nitrocatechol + NAD(P)+ + H2O
-
-
-
-
?
4-nitrophenol + NAD(P)H + H+ + O2
4-nitrocatechol + NAD(P)+ + H2O
-
-
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
in the presence of FAD and histidin-tagged NphA2
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
1 mM NADH, 5 M FAD, 1 mM DTT, NphA1 (approximately 0.5 mg of purified protein), and NphA2 (approximately 0.1 mg of purified protein) in 1 ml of 50 mM Tris-HCl buffer, pH 8.0
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
-
catalyzed by p-nitrophenol hydroxylase component A
GC-MS product identification
-
?
4-nitrophenol + NADH + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
-
?
4-nitrophenol + NADH + O2
4-nitrocatechol + NAD+ + H2O
-
NADPH: 50% of the activity with NADH
-
?
4-nitrophenol + NADH + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
?
4-nitrophenol + NADH + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
?
4-nitrophenol + NADH + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
?
4-nitrophenol + NADH + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
?
chlorzoxazone + NADH + O2
?
-
6-hydroxylation
-
-
?
chlorzoxazone + NADH + O2
?
-
-
-
-
?
additional information
?
-
-
no substrates: 2-nitrophenol, 2,4-dinitrophenol
-
-
?
additional information
?
-
-
PnpA1 is the oxygenase component of the two-component PNP 2-monooxygenase from Gram-positive Rhodococcus imtechensis strain RKJ300. It also catalyzes the hydroxylation of 4-nitrocatechol (4NC) and 2-chloro-4-nitrophenol (2C4NP)
-
-
-
additional information
?
-
-
PnpA1 is the oxygenase component of the two-component PNP 2-monooxygenase from Gram-positive Rhodococcus imtechensis strain RKJ300. It also catalyzes the hydroxylation of 4-nitrocatechol (4NC) and 2-chloro-4-nitrophenol (2C4NP)
-
-
-
additional information
?
-
-
PnpA1 is the oxygenase component of the two-component PNP 2-monooxygenase from Gram-positive Rhodococcus imtechensis strain RKJ300. It also catalyzes the hydroxylation of 4-nitrocatechol (4NC) and 2-chloro-4-nitrophenol (2C4NP)
-
-
-
additional information
?
-
no degradation of 2-nitrophenol, 2-hydroxyphenylacetate, 3-hydroxyphenylacetate, 4-hydroxyphenylacetate
-
-
?
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4-nitrophenol + NAD(P)H + H+ + O2
4-nitrocatechol + NAD(P)+ + H2O
4-nitrophenol + NAD(P)H + O2
4-nitrocatechol + NAD(P)+ + H2O
-
-
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
p-nitrophenol + NADH + H+ + O2
p-nitrocatechol + NAD+ + H2O
-
-
-
-
?
p-nitrophenol + NADPH + H+ + O2
p-nitrocatechol + NADP+ + H2O
-
200 microM substrate, 0.4 mg microsomal protein, 1 mM NADPH
-
-
?
4-nitrophenol + NAD(P)H + H+ + O2
4-nitrocatechol + NAD(P)+ + H2O
-
-
-
-
?
4-nitrophenol + NAD(P)H + H+ + O2
4-nitrocatechol + NAD(P)+ + H2O
-
-
-
-
?
4-nitrophenol + NAD(P)H + H+ + O2
4-nitrocatechol + NAD(P)+ + H2O
-
-
-
-
?
4-nitrophenol + NAD(P)H + H+ + O2
4-nitrocatechol + NAD(P)+ + H2O
-
-
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
in the presence of FAD and histidin-tagged NphA2
-
-
?
4-nitrophenol + NADH + H+ + O2
4-nitrocatechol + NAD+ + H2O
-
-
-
-
?
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alpha-naphthoflavone
-
slight
catalase
-
30% inhibition at 1000 units
-
chlorzoxazone
-
mutual competitive inhibition with 4-nitrophenol
Co2+
-
slight effect, crude enzyme extract
Cu2+
-
94% inhibition at 1 mM,crude enzyme extract
diethyldithiocarbamate
-
50% inhibition at 0.002-0.003 mM
FAD
inhibition at concentrations higher than 10 microM FAD, complete inhibition at concentrations higher than 50 microM FAD
Fe2+
-
slight effect, crude enzyme extract
Fe3+
-
slight effect, crude enzyme extract
Hg2+
-
63% inhibition at 1 mM, crude enzyme extract
Horseradish peroxidase
-
complete inhibition at 25 units
-
N-Methylmaleimide
-
84% inhibition at 5 mM
Ni2+
-
slight effect, crude enzyme extract
p-chloromercuribenzoate
-
81% inhibition at 1 mM
Sn2+
-
57% inhibition at 1 mM,crude enzyme extract
4-nitrophenol
-
mutual competitive inhibition with chlorzoxazone
4-nitrophenol
-
substrate inhibition above 0.1 mM
sesamin
-
mechanism-based inhibition with decrease in the IC50 value when 5 min pre-incubation step is included
sesamin
-
mechanism-based inhibition with decrease in the IC50 value when 5 min pre-incubation step is included
additional information
-
inhibition at high ionic strength of all common buffers and salts e.g. phosphate, Tris, KCl, (NH4)2SO4, 60% inhibition above 300 mM, crude enzyme extract
-
additional information
-
no inhibitory effects of testosterone (4, 8, 17, 34 pmol/ml), 17beta-estradiol (18, 3.6, 36, 72 pmol/ml), estrone (1.9, 3.7, 9, 18 pmol/ml), androstenone (55, 180, 3760, 7520 pmol/ml)
-
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Adenocarcinoma
Expression of cytochrome P-450 2E1 messenger ribonucleic acid in adenocarcinoma at ureterosigmoidostomy site after bladder exstrophy.
Avitaminosis
Activity of xenobiotic-metabolizing enzymes in the liver of rats with multi-vitamin deficiency.
Bladder Exstrophy
Expression of cytochrome P-450 2E1 messenger ribonucleic acid in adenocarcinoma at ureterosigmoidostomy site after bladder exstrophy.
Brain Edema
[Expression of CYP2E1 in different brain regions during the formation of toxic cerebral edema induced by 1, 2-DCE in mice and its effect on cerebral edema formation].
Carcinogenesis
The effect of rosmarinic acid on 1,2-dimethylhydrazine induced colon carcinogenesis.
Carcinoma, Hepatocellular
Characterization of cytochrome P450 2E1 induction in a rat hepatoma FGC-4 cell model by ethanol.
Carcinoma, Hepatocellular
Expression of Cytochromes P-450 2E1, 3A4 and 1A1/1A2 in Growing and Confluent Human HepG2 Hepatoma Cells-Effect of Ethanol.
Carcinoma, Hepatocellular
Post-translational inhibition of cytochrome P-450 2E1 expression by chlomethiazole in Fao hepatoma cells.
Carcinoma, Hepatocellular
Role of ethanol-inducible cytochrome P-450 2E1 in the development of hepatocellular carcinoma by the chemical carcinogen, N-nitrosodimethylamine.
Carcinoma, Hepatocellular
Selective fast degradation of cytochrome P-450 2E1 in serum-deprived hepatoma cells by a mechanism sensitive to inhibitors of vesicular transport.
Cardiomyopathy, Dilated
New Molecular Mechanism Underlying Myc-Mediated Cytochrome P450 2E1 Upregulation in Apoptosis and Energy Metabolism in the Myocardium.
Cardiomyopathy, Hypertrophic
New Molecular Mechanism Underlying Myc-Mediated Cytochrome P450 2E1 Upregulation in Apoptosis and Energy Metabolism in the Myocardium.
Chemical and Drug Induced Liver Injury
Cytochrome P450 2E1 genotype and the susceptibility to antituberculosis drug-induced hepatitis.
Colonic Neoplasms
Colorectal cancer risk in relation to genetic polymorphism of cytochrome P450 1A1, 2E1, and glutathione-S-transferase M1 enzymes.
Colorectal Neoplasms
Association between allelic polymorphisms of metabolizing enzymes (CYP 1A1, CYP 1A2, CYP 2E1, mEH) and occurrence of colorectal cancer in Hungary.
Colorectal Neoplasms
Colorectal cancer risk in relation to genetic polymorphism of cytochrome P450 1A1, 2E1, and glutathione-S-transferase M1 enzymes.
Diabetes Mellitus
[Role of lipid peroxidation in non-alcoholic steatohepatitis]
Dyslipidemias
Treatment of non-alcoholic fatty liver disease.
Endotoxemia
Microsomal Ethanol-Oxidizing System: Success Over 50 Years and an Encouraging Future.
Fatty Liver
Detection of carcinogenic etheno-DNA adducts in children and adolescents with non-alcoholic steatohepatitis (NASH).
Fatty Liver
Etiopathogenesis of nonalcoholic steatohepatitis.
Heart Diseases
New Molecular Mechanism Underlying Myc-Mediated Cytochrome P450 2E1 Upregulation in Apoptosis and Energy Metabolism in the Myocardium.
Hepatitis
Minimal effect of cytokine-independent hepatitis induced by anti-Fas antibodies on hepatic cytochrome P450 gene expression in mice.
Insulin Resistance
High-fat emulsion-induced rat model of nonalcoholic steatohepatitis.
Insulin Resistance
Treatment of non-alcoholic fatty liver disease.
Iron Overload
[Role of oxidative stress in non-alcoholic steatohepatitis]
Liver Diseases
Hepatic Lipid Peroxidation and Cytochrome P-450 2E1 in Pediatric Nonalcoholic Fatty Liver Disease and Its Subtypes.
Liver Diseases, Alcoholic
Lipopolysaccharide-induced liver injury in rats treated with the CYP2E1 inducer pyrazole.
Liver Diseases, Alcoholic
Role of cytochrome P-450 2E1 in ethanol-, carbon tetrachloride- and iron-dependent microsomal lipid peroxidation.
Lung Injury
Selective inhibition and induction of CYP activity discriminates between the isoforms responsible for the activation of butylated hydroxytoluene and naphthalene in mouse lung.
Malnutrition
Effects of chronic ethanol on growth hormone secretion and hepatic cytochrome P450 isozymes of the rat.
Malnutrition
Undernutrition during hyperoxic exposure induces CYP2E1 in rat liver.
Myocardial Ischemia
New Molecular Mechanism Underlying Myc-Mediated Cytochrome P450 2E1 Upregulation in Apoptosis and Energy Metabolism in the Myocardium.
Neoplasms
Dissimilar characteristics of N-methyl-N-nitrosourea-initiated foci and tumors promoted by dichloroacetic acid or trichloroacetic acid in the liver of female B6C3F1 mice.
Neoplasms
Interaction between cytochrome P-450 2E1 polymorphisms and environmental factors with risk of esophageal and stomach cancers in Chinese.
Neoplasms
The effect of rosmarinic acid on 1,2-dimethylhydrazine induced colon carcinogenesis.
Neoplasms
Zonated expression of cytokines in rat liver: effect of chronic ethanol and the cytochrome P450 2E1 inhibitor, chlormethiazole.
Non-alcoholic Fatty Liver Disease
Analysis of hepatic genes involved in the metabolism of fatty acids and iron in nonalcoholic fatty liver disease.
Non-alcoholic Fatty Liver Disease
Hepatic Lipid Peroxidation and Cytochrome P-450 2E1 in Pediatric Nonalcoholic Fatty Liver Disease and Its Subtypes.
Obesity
[Role of lipid peroxidation in non-alcoholic steatohepatitis]
Parkinson Disease
Acetaldehyde and parkinsonism: role of CYP450 2E1.
Parkinson Disease
Cytochrome P450 and Parkinson's disease: protective role of neuronal CYP 2E1 from MPTP toxicity.
Parkinsonian Disorders
Acetaldehyde and parkinsonism: role of CYP450 2E1.
Starvation
[Effect of starvation and acetone on the enzyme systems of biotransformation and toxicity of xenobiotics--CYP2E1 substrates in rats]
Stomach Neoplasms
Interaction between cytochrome P-450 2E1 polymorphisms and environmental factors with risk of esophageal and stomach cancers in Chinese.
Stomach Neoplasms
Polymorphisms in NEIL-2, APE-1, CYP2E1 and MDM2 Genes are Independent Predictors of Gastric Cancer Risk in a Northern Jiangsu Population (China).
Stomach Neoplasms
[Meta-analysis on association between genetic polymorphisms of cytochrome P450 2E1 and susceptibility to Chinese gastric cancer].
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0.000037
-
microsomal fraction
0.00275
-
malaria infected mouse, real time kinetic method
0.00411
-
mouse without infection, real time kinetic method
0.0128
-
substrate 2-chloro-4-nitrophenol, pH 7.6, 22°C
0.0179
-
substrate 4-nitrocatechol, pH 7.6, 22°C
0.034
-
substrate 4-nitrophenol, pH 7.6, 22°C
11.2
cell extract, 0.3 mM 4-nitrophenol as substrate, 1 mM NADH, 5 M FAD, 1 mM DTT, NphA1 (approximately 0.5 mg of purified protein), and NphA2 (approximately 0.1 mg of purified protein) in 1 ml of 50 mM Tris-HCl buffer (pH 7.5), 22°C
12.8
-
substrate 2-chloro-4-nitrophenol, pH 7.6, 23°C
132.8
-
surgically castrated pig, pH 6.8
161.5
-
immunocastrated pig, pH 6.8
17.9
-
substrate 4-nitrocatechol, pH 7.6, 23°C
24.5
HiTrap Q-Sepharose purified enzyme, 0.3 mM 4-nitrophenol as substrate, 1 mM NADH, 5 M FAD, 1 mM DTT, NphA1 (approximately 0.5 mg of purified protein), and NphA2 (approximately 0.1 mg of purified protein) in 1 ml of 50 mM Tris-HCl buffer (pH 7.5), 22°C
34.2
-
substrate 4-nitrophenol, pH 7.6, 23°C
98.3
-
entire male pig, pH 6.8
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evolution
-
PNP monooxygenase belongs to a two-component flavin-diffusible monooxygenase family
evolution
-
PnpA1 is structurally determined to be a member of the group D flavin-dependent monooxygenases with an acyl coenzyme A (acyl-CoA) dehydrogenase fold, crystal structure analysis, overview. PnpA1 shows an obvious difference in substrate selectivity with its close homologues TcpA and TftD, which may be caused by the unique Thr296 and a different conformation in the loop from positions 449 to 454 (loop 449-454)
evolution
-
PnpA1 is structurally determined to be a member of the group D flavin-dependent monooxygenases with an acyl coenzyme A (acyl-CoA) dehydrogenase fold, crystal structure analysis, overview. PnpA1 shows an obvious difference in substrate selectivity with its close homologues TcpA and TftD, which may be caused by the unique Thr296 and a different conformation in the loop from positions 449 to 454 (loop 449-454)
-
evolution
-
PNP monooxygenase belongs to a two-component flavin-diffusible monooxygenase family
-
evolution
-
PnpA1 is structurally determined to be a member of the group D flavin-dependent monooxygenases with an acyl coenzyme A (acyl-CoA) dehydrogenase fold, crystal structure analysis, overview. PnpA1 shows an obvious difference in substrate selectivity with its close homologues TcpA and TftD, which may be caused by the unique Thr296 and a different conformation in the loop from positions 449 to 454 (loop 449-454)
-
malfunction
-
an N450A variant is found with improved activity for 4NC and 2C4NP, probably because of reduced steric hindrance
malfunction
-
an N450A variant is found with improved activity for 4NC and 2C4NP, probably because of reduced steric hindrance
-
malfunction
-
an N450A variant is found with improved activity for 4NC and 2C4NP, probably because of reduced steric hindrance
-
metabolism
NphA1 oxidizes 4-nitrophenol into 4-nitrocatechol in the presence of FAD, NADH and NphA2 (reduces FAD in the presence of NADH)
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
-
para-nitrophenol (PNP) is a hydrolytic product of organophosphate insecticides, such as parathion and methylparathion, in soil. Aerobic microbial degradation of PNP has been classically shown to proceed via the benzenetriol (BT) pathway in Gram-positive degraders. The BT pathway is initiated by a two-component PNP 2-monooxygenase. Comparison of the degradation pathways in Gram-negative and Gram-positive strains. Degradation pathways of PNP and 4NC in Gram-negative strains. PNP and 4NC are oxidized to p-benzoquinone and hydroxyl-1,4-benzoquinone, respectively, and the latter two can be reduced and degraded by other enzymes. Degradation pathways of PNP and 2C4NP in Gram-positive strains. PnpA1 oxidizes PNP to 4NC, and the latter is further oxidized to hydroxyl-1,4-benzoquinone, which can be nonenzymatically reduced to BT. 2C4NP can also be oxidized to produce chloro-1,4-benzoquinone, which is immediately converted to hydroxyl-1,4-benzoquinone by hydrolytic dechlorination and reduced to BT
metabolism
-
PnpA1 is a member of the group D flavin-dependent monooxygenases with an acyl-CoA dehydrogenase fold. Residues Arg100 and His293 are directly involved in catalysis. The bulky side chain of Val292 pushes the substrate toward FAD, hence positioning the substrate properly
metabolism
-
para-nitrophenol (PNP) is a hydrolytic product of organophosphate insecticides, such as parathion and methylparathion, in soil. Aerobic microbial degradation of PNP has been classically shown to proceed via the benzenetriol (BT) pathway in Gram-positive degraders. The BT pathway is initiated by a two-component PNP 2-monooxygenase. Comparison of the degradation pathways in Gram-negative and Gram-positive strains. Degradation pathways of PNP and 4NC in Gram-negative strains. PNP and 4NC are oxidized to p-benzoquinone and hydroxyl-1,4-benzoquinone, respectively, and the latter two can be reduced and degraded by other enzymes. Degradation pathways of PNP and 2C4NP in Gram-positive strains. PnpA1 oxidizes PNP to 4NC, and the latter is further oxidized to hydroxyl-1,4-benzoquinone, which can be nonenzymatically reduced to BT. 2C4NP can also be oxidized to produce chloro-1,4-benzoquinone, which is immediately converted to hydroxyl-1,4-benzoquinone by hydrolytic dechlorination and reduced to BT
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metabolism
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PnpA1 is a member of the group D flavin-dependent monooxygenases with an acyl-CoA dehydrogenase fold. Residues Arg100 and His293 are directly involved in catalysis. The bulky side chain of Val292 pushes the substrate toward FAD, hence positioning the substrate properly
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metabolism
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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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metabolism
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para-nitrophenol (PNP) is a hydrolytic product of organophosphate insecticides, such as parathion and methylparathion, in soil. Aerobic microbial degradation of PNP has been classically shown to proceed via the benzenetriol (BT) pathway in Gram-positive degraders. The BT pathway is initiated by a two-component PNP 2-monooxygenase. Comparison of the degradation pathways in Gram-negative and Gram-positive strains. Degradation pathways of PNP and 4NC in Gram-negative strains. PNP and 4NC are oxidized to p-benzoquinone and hydroxyl-1,4-benzoquinone, respectively, and the latter two can be reduced and degraded by other enzymes. Degradation pathways of PNP and 2C4NP in Gram-positive strains. PnpA1 oxidizes PNP to 4NC, and the latter is further oxidized to hydroxyl-1,4-benzoquinone, which can be nonenzymatically reduced to BT. 2C4NP can also be oxidized to produce chloro-1,4-benzoquinone, which is immediately converted to hydroxyl-1,4-benzoquinone by hydrolytic dechlorination and reduced to BT
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metabolism
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PnpA1 is a member of the group D flavin-dependent monooxygenases with an acyl-CoA dehydrogenase fold. Residues Arg100 and His293 are directly involved in catalysis. The bulky side chain of Val292 pushes the substrate toward FAD, hence positioning the substrate properly
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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
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the enzyme comprises two components, a flavoprotein reductase and an oxygenase, catalyzes the initial two sequential monooxygenations to convert PNP to trihydroxybenzene, EC 1.14.13.29 and EC 1.14.13.166
physiological function
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PnpA1 is the oxygenase component of the two-component PNP 2-monooxygenase from Gram-positive Rhodococcus imtechensis strain RKJ300. It also catalyzes the hydroxylation of 4-nitrocatechol (4NC) and 2-chloro-4-nitrophenol (2C4NP)
physiological function
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PnpA1 is the oxygenase component of the two-component PNP 2-monooxygenase from Gram-positive Rhodococcus imtechensis strain RKJ300. It also catalyzes the hydroxylation of 4-nitrocatechol (4NC) and 2-chloro-4-nitrophenol (2C4NP)
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physiological function
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the enzyme comprises two components, a flavoprotein reductase and an oxygenase, catalyzes the initial two sequential monooxygenations to convert PNP to trihydroxybenzene, EC 1.14.13.29 and EC 1.14.13.166
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physiological function
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PnpA1 is the oxygenase component of the two-component PNP 2-monooxygenase from Gram-positive Rhodococcus imtechensis strain RKJ300. It also catalyzes the hydroxylation of 4-nitrocatechol (4NC) and 2-chloro-4-nitrophenol (2C4NP)
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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
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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 of substrates into the active site of PNP monooxygenase, 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
additional information
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PnpA1 is the oxygenase component of the two-component PNP 2-monooxygenase from Gram-positive Rhodococcus imtechensis strain RKJ300. It also catalyzes the hydroxylation of 4-nitrocatechol (4NC) and 2-chloro-4-nitrophenol (2C4NP). The crystal structure and site-directed mutagenesis underlined the direct involvement of residues Arg100 and His293 in catalysis. The bulky side chain of residue Val292 is proposed to push the substrate toward flavin adenine dinucleotide (FAD), hence positioning the substrate properly. Different PNP binding manners determine the choice of ortho- or para-hydroxylation on PNP by single-component PNP 4-monooxygenases and two-component PNP 2-monooxygenases. Substrate binding site structure of PnpA1, overview. For two-component flavin-dependent monooxygenases, reduced flavin must be bound to the enzyme before the substrate's entry. The PnpA1-FAD model shows that a substrate can only enter the binding pocket through a narrow hydrophobic tunnel, mainly consisting of Val156, Leu456, and Leu207, because of the prepositioned FAD. The perimeter of the substrate-binding site is mainly made with four fragments including a7, loop 449-454, loop 93-102, and loop 154-175. Among those fragments, loop 449-454 has a relatively high temperature factor and shows the most heterogeneous conformations among the four subunits, reflecting its flexibility. The residues lining the substrate-binding pocket are predominantly hydrophobic ones, including Phe446, Phe155, Phe289, Val292, and Leu207. Molecular docking of FAD and substrates
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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homotetramer
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crystal structure analysis, the functional unit of PnpA1 is a tetramer, overview
homotetramer
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crystal structure analysis, the functional unit of PnpA1 is a tetramer, overview
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homotetramer
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crystal structure analysis, the functional unit of PnpA1 is a tetramer, overview
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tetramer
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crystallization data
tetramer
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crystallization data
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tetramer
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crystallization data
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tetramer
4 * x, gel filtration chromatography
additional information
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the PnpA1 monomer consists of 15 alpha-helices, 13 beta-strands, and four 310 helices and can be divided into three sequential segments based on their constituent secondary structural elements. Those three segments are tightly interconnected in the three-dimensional structure. Moreover, they form three faces of the hydrophobic substrate pocket. The first segment (residues 1 to 147) is composed of six helices (alpha1 to alpha6) and three short beta-strands (beta1 to beta3). This area is located in the periphery of the tetramer and constitutes the inner side of the pocket. The second segment (residues 148 to 277) has eight beta-strands (b4 to b11). These beta-strands are arranged as a small beta-barrel. The third segment, namely, the C-terminal segment, is composed of 8 helices (alpha7 to alpha15) and 2 short beta-strands (beta12 and beta13). Six alpha-helices (alpha7, alpha8, alpha9, alpha11, alpha12, and alpha13) form a helix bundle, which is mainly maintained by hydrophobic interaction among them. This segment is located at the tetramerization interface and involved in interacting with neighboring subunits. Alpha14 and alpha15 are the most extensive two of the eight helices. They clearly protrude from the protein core and extend into the neighboring subunit. No electron density is observed for residues 162 to 168 and residues 506 to 528 because of their high flexibility, which is common among PnpA1's homologues
additional information
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the PnpA1 monomer consists of 15 alpha-helices, 13 beta-strands, and four 310 helices and can be divided into three sequential segments based on their constituent secondary structural elements. Those three segments are tightly interconnected in the three-dimensional structure. Moreover, they form three faces of the hydrophobic substrate pocket. The first segment (residues 1 to 147) is composed of six helices (alpha1 to alpha6) and three short beta-strands (beta1 to beta3). This area is located in the periphery of the tetramer and constitutes the inner side of the pocket. The second segment (residues 148 to 277) has eight beta-strands (b4 to b11). These beta-strands are arranged as a small beta-barrel. The third segment, namely, the C-terminal segment, is composed of 8 helices (alpha7 to alpha15) and 2 short beta-strands (beta12 and beta13). Six alpha-helices (alpha7, alpha8, alpha9, alpha11, alpha12, and alpha13) form a helix bundle, which is mainly maintained by hydrophobic interaction among them. This segment is located at the tetramerization interface and involved in interacting with neighboring subunits. Alpha14 and alpha15 are the most extensive two of the eight helices. They clearly protrude from the protein core and extend into the neighboring subunit. No electron density is observed for residues 162 to 168 and residues 506 to 528 because of their high flexibility, which is common among PnpA1's homologues
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additional information
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the PnpA1 monomer consists of 15 alpha-helices, 13 beta-strands, and four 310 helices and can be divided into three sequential segments based on their constituent secondary structural elements. Those three segments are tightly interconnected in the three-dimensional structure. Moreover, they form three faces of the hydrophobic substrate pocket. The first segment (residues 1 to 147) is composed of six helices (alpha1 to alpha6) and three short beta-strands (beta1 to beta3). This area is located in the periphery of the tetramer and constitutes the inner side of the pocket. The second segment (residues 148 to 277) has eight beta-strands (b4 to b11). These beta-strands are arranged as a small beta-barrel. The third segment, namely, the C-terminal segment, is composed of 8 helices (alpha7 to alpha15) and 2 short beta-strands (beta12 and beta13). Six alpha-helices (alpha7, alpha8, alpha9, alpha11, alpha12, and alpha13) form a helix bundle, which is mainly maintained by hydrophobic interaction among them. This segment is located at the tetramerization interface and involved in interacting with neighboring subunits. Alpha14 and alpha15 are the most extensive two of the eight helices. They clearly protrude from the protein core and extend into the neighboring subunit. No electron density is observed for residues 162 to 168 and residues 506 to 528 because of their high flexibility, which is common among PnpA1's homologues
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M192I
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site-directed mutagenesis, the mutant shows significantly reduced activity compared to wild-type enzyme
V292A
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site-directed mutagenesis, the mutant shows significantly reduced activity compared to wild-type enzyme
V292L
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site-directed mutagenesis, the mutant shows slightly reduced activity compared to wild-type enzyme
H293A
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complete loss of activity
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H293A
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complete loss of activity
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H293A
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complete loss of activity
H293A
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site-directed mutagenesis, inactive mutant
N450A
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site-directed mutagenesis, the mutant shows slightly altered substrate specificity compared to wild-type enzyme
N450A
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variant displays improved activity for 4-nitrocatechol and 2-chloro-4-nitrophenol
R100A
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complete loss of activity
R100A
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site-directed mutagenesis, inactive mutant
R370A
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complete loss of activity
R370A
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site-directed mutagenesis, inactive mutant
R100A
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complete loss of activity
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R100A
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site-directed mutagenesis, inactive mutant
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R370A
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complete loss of activity
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R370A
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site-directed mutagenesis, inactive mutant
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R100A
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complete loss of activity
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R100A
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site-directed mutagenesis, inactive mutant
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R370A
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complete loss of activity
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R370A
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site-directed mutagenesis, inactive mutant
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Mitra, D.; Vaidyanathan, C.S.
A new 4-nitrophenol 2-hydroxylase from a Nocardia sp
Biochem. Int.
8
609-615
1984
Nocardia sp.
brenda
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Hydroxylation of p-nitrophenol by rabbit ethanol-inducible cytochrome P-450 isozyme 3a
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1986
Oryctolagus cuniculus
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Arinc, E.; Aydan, A.
Lung microsomal p-nitrophenol hydroxylase - characterization and reconstitution of its activity
Comp. Biochem. Physiol. B
97
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1990
Ovis aries
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Reinke, L.A.; Moyer, M.J.
p-Nitrophenol hydroxylation. A microsomal oxidation which is highly inducible by ethanol
Drug Metab. Dispos.
13
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Rattus norvegicus
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Allis, J.W.; Robinson, B.L.
A kinetic assay for p-nitrophenyl hydroxylase in rat liver microsomes
Anal. Biochem.
219
49-52
1994
Rattus norvegicus
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Hanioka, N.; Watanabe, K.; Yoda, R.; Ando, M.
Effect of alachlor on hepatic cytochrome P 450 enzymes in rats
Drug Chem. Toxicol.
25
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2002
Rattus norvegicus
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Tassaneeyakul, W.; Veronese, M.E.; Birkett, D.J.; Gonzalez, F.J.; Miners, J.O.
Validation of 4-nitrophenol as an in vitro substrate probe for human liver CYP2E1 using cDNA expression and microsomal kinetic techniques
Biochem. Pharmacol.
46
1975-1981
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Homo sapiens
brenda
Vences-Mejia, A.; Labra-Ruiz, N.; Hernandez-Martinez, N.; Dorado-Gonzalez, V.; Gomez-Garduno, J.; Perez-Lopez, I.; Nosti-Palacios, R.; Camacho Carranza, R.; Espinosa-Aguirre, J.J.
The effect of aspartame on rat brain xenobiotic-metabolizing enzymes
Hum. Exp. Toxicol.
25
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Pakala, S.B.; Gorla, P.; Pinjari, A.B.; Krovidi, R.K.; Baru, R.; Yanamandra, M.; Merrick, M.; Siddavattam, D.
Biodegradation of methyl parathion and p-nitrophenol: Evidence for the presence of a p-nitrophenol 2-hydroxylase in a Gram-negative Serratia sp. strain DS001
Appl. Microbiol. Biotechnol.
73
1452-1462
2007
Serratia sp. DS001
brenda
Zamaratskaia, G.; Zlabek, V.; Chen, G.; Madej, A.
Modulation of porcine cytochrome P450 enzyme activities by surgical castration and immunocastration
Animal
3
1124-1132
2009
Sus scrofa
brenda
Carvalho, R.S.; Friedrich, K.; De-Oliveira, A.C.; Suarez-Kurtz, G.; Paumgartten, F.J.
Malaria downmodulates mRNA expression and catalytic activities of CYP1A2, 2E1 and 3A11 in mouse liver
Eur. J. Pharmacol.
616
265-269
2009
Mus musculus
brenda
Takeo, M.; Murakami, M.; Niihara, S.; Yamamoto, K.; Nishimura, M.; Kato, D.; Negoro, S.
Mechanism of 4-nitrophenol oxidation in Rhodococcus sp. Strain PN1: characterization of the two-component 4-nitrophenol hydroxylase and regulation of its expression
J. Bacteriol.
190
7367-7374
2008
Rhodococcus sp. PN1 (Q8RQQ0)
brenda
Wagner, L.; Zlabek, V.; Trattner, S.; Zamaratskaia, G.
In vitro inhibition of 7-ethoxyresorufin-O-deethylase (EROD) and p-nitrophenol hydroxylase (PNPH) activities by sesamin in hepatic microsomes from two fish species
Mol. Biol. Rep.
40
457-462
2013
Cyprinus carpio, Salmo salar
brenda
Min, J.; Zhang, J.J.; Zhou, N.Y.
The gene cluster for para-nitrophenol catabolism is responsible for 2-chloro-4-nitrophenol degradation in Burkholderia sp. strain SJ98
Appl. Environ. Microbiol.
80
6212-6222
2014
Rhodococcus opacus, Rhodococcus opacus RKJ300
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.
7
157-167
2015
Arthrobacter sp. JS443
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
Lysinibacillus sphaericus, Arthrobacter sp. (A7YVV2), Arthrobacter sp., Lysinibacillus sphaericus JS905
brenda
Guo, Y.; Li, D.F.; Zheng, J.; Xu, Y.; Zhou, N.Y.
Single-component and two-component para-nitrophenol monooxygenases structural basis for their catalytic difference
Appl. Environ. Microbiol.
87
e0117121
2021
Rhodococcus opacus, Rhodococcus opacus JCM 13270, Rhodococcus opacus RKJ300
brenda