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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 = 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 = 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 = 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
catalytic mechanism, overview. In contrast to conclusions reported previously, the second product of the HspB reaction is shown to be succinate, with isotope labeling experiments providing direct evidence that the newly introduced oxygen atom of succinate is derived from H2O. Reduced HspB reacts with oxygen to form a C(4a)-(hydro)peroxyflavin intermediate before it is converted to the oxidized flavoenzyme species. The formed C(4a)-hydroperoxyflavin intermediate reacts with HSP to form an intermediate that is hydrolyzed to the products 2,5-dihydroxypyridine and succinate
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 = 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
catalytic mechanism, overview. In contrast to conclusions reported previously, the second product of the HspB reaction is shown to be succinate, with isotope labeling experiments providing direct evidence that the newly introduced oxygen atom of succinate is derived from H2O. Reduced HspB reacts with oxygen to form a C(4a)-(hydro)peroxyflavin intermediate before it is converted to the oxidized flavoenzyme species. The formed C(4a)-hydroperoxyflavin intermediate reacts with HSP to form an intermediate that is hydrolyzed to the products 2,5-dihydroxypyridine and succinate
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
6-hydroxy-3-succinoylpyridine + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
additional information
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
oxidative decarboxylation of HSP to 2,5-dihydroxypyridine in presence of NADH and FAD
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
oxidative decarboxylation of HSP to 2,5-dihydroxypyridine in presence of NADH and FAD
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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the enzyme efficiently catalyzes the conversion of 6-hydroxy-3-succinoylpyridine (HSP) into 2,5-dihydroxypyridine (2,5-DHP) and succinic acid in the presence of NADH and FAD
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
Stenotrophomonas geniculata
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
Stenotrophomonas geniculata N1
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6-hydroxy-3-succinoylpyridine + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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6-hydroxy-3-succinoylpyridine + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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additional information
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no activity with p-nitrophenol or 6-hydroxynicotinate as substrates
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additional information
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no activity with p-nitrophenol or 6-hydroxynicotinate as substrates
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additional information
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no activity with p-nitrophenol or 6-hydroxynicotinate as substrates
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additional information
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mass spectrometric analysis of substrates and products, with recombinant enzyme
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additional information
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mass spectrometric analysis of substrates and products, with recombinant enzyme
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additional information
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assay method optimization, overview. Product identification by LC-MS
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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evolution
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phylogenetic analysis reveals that HspB is the most closely related to two p-nitrophenol 4-monooxygenases, and the experimental results exhibit that p-nitrophenol is a substrate of HspB
evolution
sequence alignment and phylogenetic analysis suggests that the VPP pathway, which evolved independently from nicotinic acid degradation, might have a closer relationship with the pyrrolidine pathway
evolution
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phylogenetic analysis reveals that HspB is the most closely related to two p-nitrophenol 4-monooxygenases, and the experimental results exhibit that p-nitrophenol is a substrate of HspB
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metabolism
6-hydroxy-3-succinoylpyridine hydroxylase catalyzes a central step of nicotine degradation. 6-Hydroxy-3-succinoylpyridine (HSP) is a key intermediate connecting the two pathways, pyridine pathway and pyrrolidine pathway, detailed overview
metabolism
6-hydroxy-3-succinoylpyridine hydroxylase catalyzes a central step of nicotine degradation. 6-Hydroxy-3-succinoylpyridine (HSP) is a key intermediate connecting the two pathways, pyridine pathway and pyrrolidine pathway, overview
metabolism
strain SJY1 efficiently degrades nicotine via a variant of the pyridine and pyrrolidine pathways (the VPP pathway), highlighting bacterial metabolic diversity in relation to nicotine degradation, a 97-kbp DNA fragment containing six nicotine degradation-related genes is obtained by gap closing from the genome sequence of strain SJY1, gene vppD gene encodes an NADH-dependent flavin-containing monooxygenase, which catalyzes the hydroxylation of 6-hydroxy-3-succinoylpyridine to 2,5-dihydroxypyridine. Nicotine degradation pathway in strain SJY1, detailed overview
metabolism
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6-hydroxy-3-succinoylpyridine hydroxylase catalyzes a central step of nicotine degradation. 6-Hydroxy-3-succinoylpyridine (HSP) is a key intermediate connecting the two pathways, pyridine pathway and pyrrolidine pathway, detailed overview
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metabolism
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6-hydroxy-3-succinoylpyridine hydroxylase catalyzes a central step of nicotine degradation. 6-Hydroxy-3-succinoylpyridine (HSP) is a key intermediate connecting the two pathways, pyridine pathway and pyrrolidine pathway, overview
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physiological function
gene is essential for nicotine degradation
physiological function
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strain S33 can transform nicotine into renewable hydroxylated-pyridine intermediates by a special pathway, in which at least three intermediates, 6-hydroxy-L-nicotine, 6-hydroxy-3-succinoylpyridine, and 2,5-dihydroxypyridine, have potential to be further chemically modified into useful compounds. Strain S33 is able to transform nicotine to 6-hydroxy-pseudooxynicotine first via the pyridine pathway through 6-hydroxy-L-nicotine and 6-hydroxy-N-methylmyosmine, and then, it turns to the pyrrolidine pathway with the formation of 6-hydroxy-3-succinoylpyridine and 2,5-dihydroxypyridine
physiological function
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6-hydroxy-3-succinoyl-pyridine (HSP) 3-monooxygenase (HspB) is a flavoprotein essential to the pyrrolidine pathway of nicotine degradation, it catalyzes pyridine-ring beta-hydroxylation, resulting in carbon-carbon cleavage and production of 2,5-dihydroxypyridine
physiological function
the key enzyme HSP hydroxylase is involved in the fused nicotine degradation pathway of the pyridine and pyrrolidine pathways
physiological function
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strain S33 can transform nicotine into renewable hydroxylated-pyridine intermediates by a special pathway, in which at least three intermediates, 6-hydroxy-L-nicotine, 6-hydroxy-3-succinoylpyridine, and 2,5-dihydroxypyridine, have potential to be further chemically modified into useful compounds. Strain S33 is able to transform nicotine to 6-hydroxy-pseudooxynicotine first via the pyridine pathway through 6-hydroxy-L-nicotine and 6-hydroxy-N-methylmyosmine, and then, it turns to the pyrrolidine pathway with the formation of 6-hydroxy-3-succinoylpyridine and 2,5-dihydroxypyridine
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physiological function
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the key enzyme HSP hydroxylase is involved in the fused nicotine degradation pathway of the pyridine and pyrrolidine pathways
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physiological function
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6-hydroxy-3-succinoyl-pyridine (HSP) 3-monooxygenase (HspB) is a flavoprotein essential to the pyrrolidine pathway of nicotine degradation, it catalyzes pyridine-ring beta-hydroxylation, resulting in carbon-carbon cleavage and production of 2,5-dihydroxypyridine
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physiological function
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gene is essential for nicotine degradation
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additional information
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free H2O2 does not catalyze the HspB enzyme reaction
additional information
the ativity of VppD is 10fold higher than the activity of the hydroxylase (HspB) from Pseudomonas putida strain S16
additional information
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free H2O2 does not catalyze the HspB enzyme reaction
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synthesis
development of an efficient process to transform HSP into 2,5-dihydroxypyridine (2,5-DHP) with heterologously expressed HSP hydroxylase and NADH-regenerating system, because 2,5-DHP, the product of the reaction catalyzed by HSP hydroxylase, is a valuable precursor for the chemical synthesis of 5-aminolevulinic acid, which is applied as a plant growth hormone, a herbicide and in cancer therapy
synthesis
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enzyme HSPHZZ can be used for the enzymatic production of 2,5-dihydroxypyridine in biotechnology applications. 85.3 mg/l 2,5-dihydroxypyridine is produced in 40 min with a conversion of 74.9% at 30°C, pH 8.5, 1.0 mM substrate concentration, and 0.001 mM enzyme concentration
synthesis
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production of 2,5-dihydroxypyridine from 6-hydroxy-3-succinoylpyridine in the presence of NADH and FAD using nicotine hydroxylase covalently immobilized on Immobead 150. At a protein loading of 15 mg/g, ImmHSPHZZ converts 93.6% of 6-hydroxy-3-succinoylpyridine to 2,5-dihydroxypyridine in 6 h. The optimal concentrations of ImmHSPHZZ and substrate are 30 mg/l and 0.75 mM, respectively. Under optimal conditions, 94.5 mg/l of 2,5-dihydroxypyridine is produced after 30 min with 85.4% conversion
synthesis
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development of an efficient process to transform HSP into 2,5-dihydroxypyridine (2,5-DHP) with heterologously expressed HSP hydroxylase and NADH-regenerating system, because 2,5-DHP, the product of the reaction catalyzed by HSP hydroxylase, is a valuable precursor for the chemical synthesis of 5-aminolevulinic acid, which is applied as a plant growth hormone, a herbicide and in cancer therapy
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Tang, H.; Wang, S.; Ma, L.; Meng, X.; Deng, Z.; Zhang, D.; Ma, C.; Xu, P.
A novel gene, encoding 6-hydroxy-3-succinoylpyridine hydroxylase, involved in nicotine degradation by Pseudomonas putida strain S16
Appl. Environ. Microbiol.
74
1567-1574
2008
Pseudomonas putida (B1N1A2), Pseudomonas putida S16 (B1N1A2), Pseudomonas putida S16
brenda
Wang, S.; Huang, H.; Xie, K.; Xu, P.
Identification of nicotine biotransformation intermediates by Agrobacterium tumefaciens strain S33 suggests a novel nicotine degradation pathway
Appl. Microbiol. Biotechnol.
95
1567-1578
2012
Agrobacterium tumefaciens, Agrobacterium tumefaciens S33
brenda
Tang, H.; Yao, Y.; Zhang, D.; Meng, X.; Wang, L.; Yu, H.; Ma, L.; Xu, P.
A novel NADH-dependent and FAD-containing hydroxylase is crucial for nicotine degradation by Pseudomonas putida
J. Biol. Chem.
286
39179-39187
2011
Pseudomonas putida (F8G0M4), Pseudomonas putida, Pseudomonas putida S16 (F8G0M4), Pseudomonas putida S16
brenda
Yu, H.; Tang, H.; Zhu, X.; Li, Y.; Xu, P.
Molecular mechanism of nicotine degradation by a newly isolated strain, Ochrobactrum sp. strain SJY1
Appl. Environ. Microbiol.
81
272-281
2015
Ochrobactrum sp. (A0A075XAG5)
brenda
Li, H.; Xie, K.; Yu, W.; Hu, L.; Huang, H.; Xie, H.; Wang, S.
Nicotine dehydrogenase complexed with 6-hydroxypseudooxynicotine oxidase involved in the hybrid nicotine-degrading pathway in Agrobacterium tumefaciens S33
Appl. Environ. Microbiol.
82
1745-1755
2016
Agrobacterium tumefaciens (W8E0Y0), Agrobacterium tumefaciens S33 (W8E0Y0)
brenda
Wei, T.; Zang, J.; Zheng, Y.; Tang, H.; Huang, S.; Mao, D.
Characterization of a novel nicotine hydroxylase from Pseudomonas sp. ZZ-5 that catalyzes the conversion of 6-hydroxy-3-succinoylpyridine into 2,5-dihydroxypyridine
Catalysts
7
272-281
2017
Pseudomonas sp. ZZ-5
brenda
Yu, H.; Hausinger, R.; Tang, H.; Xu, P.
Mechanism of the 6-hydroxy-3-succinoyl-pyridine 3-monooxygenase flavoprotein from Pseudomonas putida S16
J. Biol. Chem.
289
29158-29170
2014
Pseudomonas putida, Pseudomonas putida S16
brenda
Li, H.; Xie, K.; Huang, H.; Wang, S.
6-hydroxy-3-succinoylpyridine hydroxylase catalyzes a central step of nicotine degradation in Agrobacterium tumefaciens S33
PLoS ONE
9
e103324
2014
Agrobacterium tumefaciens (W8E0Y0), Agrobacterium tumefaciens S33 (W8E0Y0), Agrobacterium tumefaciens S33
brenda
Dong, C.; Zheng, Y.; Tang, H.; Long, Z.; Li, J.; Zhang, Z.; Liu, S.; Mao, D.; Wei, T.
Highly efficient synthesis of 2,5-dihydroxypyridine using Pseudomonas sp. ZZ-5 nicotine hydroxylase immobilized on immobead 150
Catalysts
8
548
2018
Pseudomonas sp. ZZ-5
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brenda
Wang, W.; Zhu, X.; Liu, X.; Wu, W.; Xu, P.; Tang, H.
Cloning and characterization the nicotine degradation enzymes 6-hydroxypseudooxynicotine amine oxidase and 6-hydroxy-3-succinoylpyridine hydroxylase in Pseudomonas geniculata N1
Int. Biodeter. Biodegrad.
142
83-90
2019
Stenotrophomonas geniculata (A0A0L8AFM7), Stenotrophomonas geniculata N1 (A0A0L8AFM7)
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brenda