Degradation of pyridine by<i>Arthrobacter crystallopoietes</i>and<i>Rhodococcus opocus</i>strains

Зефиров, Н. С.; Agapova, S R; Terentiev, Petr B.; Bulakhova, Irina M.; Vasyukova, N. I.; Modyanova, L. V.

doi:10.1111/j.1574-6968.1994.tb06805.x

Cited by 37 publications

(10 citation statements)

References 3 publications

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“…Although N-heterocycles are usually oxidatively cleaved by dioxygenases (1, 3), the hydrolytic cleavage of the pyridine ring was proposed in Rhodococcus opacus (13), A. nicotinovorans, Nocardioides sp. strain JS614, and R. opacus (12), yet to our knowledge, no protein/gene has been shown to be responsible for THP (the precursor of the blue pigment) metabolism to date, probably due to the high degree of instability of THP.…”

Section: Resultsmentioning

confidence: 99%

“…To identify the reaction product of the oxidation of 2HP by the HpoBCDF dioxygenase system, E. coli BL21(DE3) cells carrying pB/D and pF/C (harboring the hpoBCDF genes) were used to transform larger amounts of 2HP. After a flash column purification of the product, HPLC-MS, 13 C NMR, and 1 H NMR analyses were performed (see the text in the supplemental material). The product of 2HP oxidation was identified to be 3,6-dihydroxy-1,2,3,6-tetrahydropyridin-2-one.…”

Section: Resultsmentioning

confidence: 99%

“…The structures of the bioconversion products were determined using 1 H nuclear magnetic resonance (NMR) and 13 C NMR. 1 H and 13 C NMR spectra were recorded on a Varian Unity Inova 300 spectrometer (300 and 75 MHz, respectively).…”

Section: Methodsmentioning

confidence: 99%

“…1). While the detailed analysis of intermediate metabolites has allowed the steps leading to pyridine biodegradation in the aforementioned bacteria to be described, no enzymes involved in this bioconversion have been identified yet (13). In this study, we report the characterization of the 2HP catabolic pathway in Rhodococcus rhodochrous PY11, which has been isolated on the basis of its ability to utilize 2HP as a carbon source for growth (14).…”

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A 2-Hydroxypyridine Catabolism Pathway in Rhodococcus rhodochrous Strain PY11

Vaitekūnas

Gasparavičiūtė

Rutkienė

et al. 2016

Appl Environ Microbiol

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Rhodococcus rhodochrous PY11 (DSM 101666) is able to use 2-hydroxypyridine as a sole source of carbon and energy. By investigating a gene cluster (hpo) from this bacterium, we were able to reconstruct the catabolic pathway of 2-hydroxypyridine degradation. Here, we report that in Rhodococcus rhodochrous PY11, the initial hydroxylation of 2-hydroxypyridine is catalyzed by a four-component dioxygenase (HpoBCDF). A product of the dioxygenase reaction (3,6-dihydroxy-1,2,3,6-tetrahydropyridin-2-one) is further oxidized by HpoE to 2,3,6-trihydroxypyridine, which spontaneously forms a blue pigment. In addition, we show that the subsequent 2,3,6-trihydroxypyridine ring opening is catalyzed by the hypothetical cyclase HpoH. The final products of 2-hydroxypyridine degradation in Rhodococcus rhodochrous PY11 are ammonium ion and ␣-ketoglutarate. Pyridine and its derivatives are ubiquitous in nature. The pyridine ring is found in alkaloids (e.g., nicotine, actinidine), coenzymes [NAD(P)H, pyridoxal], and man-made solvents, pesticides, and herbicides (e.g., paraquat). Hydroxypyridines are common intermediate metabolites produced during microbial biodegradation of various N-heterocycles (pyridine, nicotine, picoline, 2,6-dipicolinic acid) (1-3).It has previously been reported that Arthrobacter crystallopoietes, Arthrobacter pyridinolis, and Arthrobacter viridescens (4), Achromobacter sp. strain G2 (5), and Nocardia sp. strain PNO (6) use 2-hydroxypyridine (2HP) as a sole carbon and energy source. Through more than 50 years of investigation of pyridine ring metabolism, many intermediates have been identified and metabolic pathways have been proposed. However, the genes and enzymes responsible for 2HP biodegradation have seldom been reported.In Achromobacter sp. G2, 2HP is metabolized via the maleamate pathway (5) (Fig. 1). No enzymes responsible for the initial hydroxylation step of 2HP leading to the formation of 2,5-dihydroxypyridine (2,5DHP) have been reported to date. Nevertheless, the degradation of 2,5DHP, an intermediate of nicotinic acid metabolism, has been fully investigated by Jiménez et al. (7), and all genes encoding the enzymes involved in the maleamate pathway have been identified and characterized (7).Arthrobacter crystallopoietes, A. pyridinolis, and A. viridescens (4) and Arthrobacter sp. strain PY22 (8) produce a blue pigment (nicotine blue) in the medium when grown on 2HP. The nicotine blue has been shown to be a 4,5,4=,5=-tetrahydroxy-3,3=-diazadiphenoquinone-(2,2=) (9) that is an autoxidation product of 2,3,6-trihydroxypyridine (THP). THP can be synthesized via hydroxylation of 2,5DHP, 2,3-dihydroxypyridine (2,3DHP), or 2,6-dihydroxypyridine (2,6DHP); however, only the 2,6DHP 3-hydroxylase, which is involved in the biodegradation of nicotine by Arthrobacter nicotinovorans, has been identified to date (10).We have previously reported that HpyB monooxygenase from Arthrobacter sp. PY22 is sufficient for the conversion of 2HP to THP (8). Since no reaction intermediates have been detected, a consecutive two-st...

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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A 2-Hydroxypyridine Catabolism Pathway in Rhodococcus rhodochrous Strain PY11

Vaitekūnas

Gasparavičiūtė

Rutkienė

et al. 2016

Appl Environ Microbiol

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“…involved in the biodegradation of pyridine have been discovered since then, including Arthrobacter (3)(4)(5), Nocardia (6), Bacillus (6), Paracoccus (7,8), Pseudomonas (9), Rhodococcus (10), Shewanella (11), Alcaligenes (12), Shinella (13), Gordonia (14), Pimelobacter (15), and Achromobacter (16) species. Despite more than 100 years of investigation of pyridine ring metabolism, only recently the enzymes and genes essential for biodegradation of the hydroxylated or carboxylated pyridine derivatives have been identified (1,(17)(18)(19).…”

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confidence: 99%

Microbial Degradation of Pyridine: a Complete Pathway inArthrobactersp. Strain 68b Deciphered

Časaitė

Stanislauskienė

Vaitekūnas

et al. 2020

Appl Environ Microbiol

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Pyridine and its derivatives constitute the majority of heterocyclic aromatic compounds that occur largely as a result of human activities and contribute to environmental pollution. It is known that they can be degraded by various bacteria in the environment; however, the degradation of unsubstituted pyridine has not yet been completely resolved. In this study, we present data on the pyridine catabolic pathway in Arthrobacter sp. strain 68b at the level of genes, enzymes, and metabolites. The pyr gene cluster, responsible for the degradation of pyridine, was identified in a catabolic plasmid, p2MP. The pathway of pyridine metabolism consisted of four enzymatic steps and ended by the formation of succinic acid. The first step in the degradation of pyridine proceeds through a direct ring cleavage catalyzed by a two-component flavin-dependent monooxygenase system, encoded by pyrA (pyridine monooxygenase) and pyrE genes. The genes pyrB, pyrC, and pyrD were found to encode (Z)-N-(4-oxobut-1-enyl)formamide dehydrogenase, amidohydrolase, and succinate semialdehyde dehydrogenase, respectively. These enzymes participate in the subsequent steps of pyridine degradation. The metabolites of these enzymatic reactions were identified, and this allowed us to reconstruct the entire pyridine catabolism pathway in Arthrobacter sp. 68b. IMPORTANCE The biodegradation pathway of pyridine, a notorious toxicant, is relatively unexplored, as no genetic data related to this process have ever been presented. In this paper, we describe the plasmid-borne pyr gene cluster, which includes the complete set of genes responsible for the degradation of pyridine. A key enzyme, the monooxygenase PyrA, which is responsible for the first step of the catabolic pathway, performs an oxidative cleavage of the pyridine ring without typical activation steps such as reduction or hydroxylation of the heterocycle. This work provides new insights into the metabolism of N-heterocyclic compounds in nature.

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The role of electron donors generated from UV photolysis for accelerating pyridine biodegradation

Tang

Zhang

Yan

et al. 2015

Biotech & Bioengineering

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Employing an internal circulation baffled biofilm reactor (ICBBR), we evaluated the mechanisms by which photolysis accelerated the biodegradation and mineralization of pyridine (C5 H5 N), a nitrogen-containing heterocyclic compound. We tested the hypothesis that pyridine oxidation is accelerated because a key photolysis intermediate, succinate, is as electron donor that promotes the initial mono-oxygenation of pyridine. Experimentally, longer photolysis time generated more electron-donor products (succinate), which stimulated faster pyridine biodegradation. This pattern was confirmed by directly adding succinate, and the stimulation effect occurred similarly with addition of the same equivalents of acetate and formate. Succinate, whether generated by UV photolysis or added directly, also accelerated mono-oxygenation of the first biodegradation intermediate, 2-hydroxyl pyridine (2HP). 2HP and pyridine were mutually inhibitory in that their mono-oxygenations competed for internal electron donor; thus, the addition of any readily biodegradable donor accelerated both mono-oxygenation steps, as well as mineralization.

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Degradation of pyridine byArthrobacter crystallopoietesandRhodococcus opocusstrains

Cited by 37 publications

References 3 publications

A 2-Hydroxypyridine Catabolism Pathway in Rhodococcus rhodochrous Strain PY11

A 2-Hydroxypyridine Catabolism Pathway in Rhodococcus rhodochrous Strain PY11

Microbial Degradation of Pyridine: a Complete Pathway inArthrobactersp. Strain 68b Deciphered

The role of electron donors generated from UV photolysis for accelerating pyridine biodegradation

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