A new pathway for isonicotinate degradation by Mycobacterium sp. INA1

Kretzer, Annette; Andreesen, Jan R.

doi:10.1099/00221287-137-5-1073

Cited by 30 publications

(10 citation statements)

References 40 publications

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“…Rather, it suggests that the formyl group is dehydrogenated while still bound to the primary amino group of methanofuran yielding N-carboxymethanofuran as product (reaction b) which should break down non-enzymically to CO, and methanofuran (Ewing et al, 1980) : 0 R Reaction (b) indicates that formylmethanofuran dehydrogenase belongs to the group of molybdenum enzymes that catalyze an insertion of an oxygen atom derived from H,O into a C-H bond (Pilato and Stiefel, 1993). Enzymes belonging to this group are xanthine dehydrogenases and xanthine oxidases (Bray, 1988;Wootton et al, 1991), molybdenum-containing formate dehydrogenases (Adams and Mortenson, 1985;Barber et al, 1986;Friedebold and Bowien, 1993), formate-ester dehydrogenase (van Ophem et al, 1992), aldehyde oxidase (Branzoli and Massey, 1974), aldehyde dehydrogenase (Poels et al, 1987), aldehyde oxidoreductase (White et al, 1993), nicotine dehydrogenase (Freudenberg et al, 1988), nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase (Nagel and Andreesen, 1990), isonicotinate dehydrogenase and 2-hydroxyisonicotinate dehydrogenase (Kretzer and Andreesen, 1991), quinoline oxidoreductase (Hettrich et al, 1991), quinoline-4-carboxylic acid oxidoreductase (Bauer and Lingens, 19921, quinaldine oxidoreductase (de Beyer and Lingens, 1993), quinaldic acid 4-oxidoreductase (Fetzner and Lingens, 1993), picolinate dehydrogenase (Siegmund et al, 1990), 2-furoyl-coenzyme A dehydrogenase , and pyrimidine oxidase and pyridoxal oxidase (Burgmayer and Stiefel, 1985). Interestingly, one of these enzymes, milk xanthine oxidase, can even catalyze the dehydrogenation of formamide to carbamic acid (Morpeth et al, 1984) which is a reaction also catalyzed by formylrnethanofuran dehydrogenase.…”

Section: Discussionmentioning

confidence: 99%

Formylmethanofuran dehydrogenases from methanogenic Archaea Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron‐sulfur proteins

Bertram

Karrasch

Schmitz

et al. 1994

European Journal of Biochemistry

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Formylmethanofuran dehydrogenases, which are found in methanogenic Archaea, are molybdenum or tungsten iron-sulfur proteins containing a pterin cofactor. We report here on differences in substrate specificity, EPR properties and susceptibility towards cyanide inactivation of the enzymes from Methanosarcina barkeri, Methanobacterium thermoautotrophicum and Methanobacterium woljei.The molybdenum enzyme from M. barkeri (relative activity with N-formylmethanofuran = 100%) was found to catalyze, albeit at considerably reduced apparent V,,,,,, the dehydrogenation of N-furfurylformamide (11 %), N-methylformamide (0.2%), formamide (0.1 %) and formate (1 %). The molybdenum enzyme from M. wolfei could only use N-furfurylformamide (1 %) and formate (3 %) as pseudosubstrates. The molybdenum enzyme from M. thermoautotrophicum and the tungsten enzymes from M. thermoautotrophicum and M. wolfei were specific for N-formylmethanofuran.The molybdenum formylmethanofuran dehydrogenases exhibited at 77 K two rhombic EPR signals, designated FMDred and FMD,,, both derived from Mo as shown by isotopic substitution with 9 7 M~. The FMD,, signal was only displayed by the active enzyme in the reduced form and was lost upon enzyme oxidation; the FMD,, signal was displayed by an inactive form and was not quenched by 0,. The tungsten isoenzymes were EPR silent.The molybdenum formylmethanofuran dehydrogenases were found to be inactivated by cyanide whereas the tungsten isoenzymes, under the same conditions, were not inactivated. Inactivation was associated with a characteristic change in the molybdenum-derived EPR signal. Reactivation was possible in the presence of sulfide. Abbreviations. FMD,,,, EPR signal attributed to active formylmethanofuran dehydrogenase ; FMD,,, EPR signal attributed to inactive formylmethanofuran dehydrogenase ; R, Land6 splittina + co2 t P IE" = -497 mV (Thauer, 1990) factor; gx, gy-and g,, Land6 splitting factors in the x , y and directions for anisotropic systems; 1 U = 1 Fmol formylmethanofuran dehydrogenatedmin.The physiological electron accePtor/donor is not knownMethylviologen (E"' = -446 mV) can be used as artificial

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Section: Discussionmentioning

confidence: 99%

Formylmethanofuran dehydrogenases from methanogenic Archaea Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron‐sulfur proteins

Bertram

Karrasch

Schmitz

et al. 1994

European Journal of Biochemistry

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“…The scanning electron micrograph was taken with a DSM 950 scanning electron microscope (Zeiss, Oberkochen, Germany) at an accelerating voltage of 10 kV. Electron photomicrographs of thin sections of strain L1 cells were taken in accordance with the procedure of Kretzer and Andreesen (22).…”

Section: Microscopy Of Cell Suspensions and Stained Cellsmentioning

confidence: 99%

Isolation and Characterization of a New Gram-Negative, Acetone-Degrading, Nitrate-Reducing Bacterium from Soil, Paracoccus solventivorans sp. nov.

Siller

Rainey²,

Stackebrandt³

et al. 1996

International Journal of Systematic Bacteriology

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An acetone-degrading, nitrate-reducing, coccoid to rod-shaped bacterium, strain L1, was isolated from soil on the site of a natural gas company. Cells of the logarithmic growth phase reacted gram positive, while those of the stationary growth phase were gram negative. Single organisms were 0.4 to 0.5 by 0.9 to 1.5 pm in size, nonmotile, and non-spore forming and had poly-P-hydroxybutyrate inclusions. The doubling time of strain L1 on acetone-C0,-nitrate at the optimal pH of 7 to 8 and the optimal temperature of 30 to 37°C was 12 h. More than 0.2% NaCl or 10 mM thiosulfate inhibited growth. For oxygen or nitrate respiration, acetone and a few organic chemicals were utilized as carbon sources whereas many others could not be used (for details, see Results). Bicarbonate (or CO,) was essential for growth on acetone but not for growth on acetoacetate. The growth yields for acetone-CO, and acetoacetate were 28.3 and 27.3 g/mol, respectively. With acetone as the carbon source, poly-P-hydroxybutyrate accounted for up to 40% of the cellular dry weight. The DNA of strain L1 had a G+C content of 68.5 mol% (as determined by high-performance liquid chromatography of nucleotides) or 70 mol% (as determined by the T, method). The sequence of the gene coding for the 16s rRNA led to the classification of strain L1 in the paracoccus group of the alpha subclass of the Proteobucteriu. The new isolate is named Paracoccus solventivuruns sp. nov. DSM 6637.Acetone is a fermentation product of fungi (15), clostridia (see, for example, reference 43), and several other bacteria (6, 35,36,51,57,58). It is also excreted into the environment in ripening apples as a bioconversion product derived from p pvate. Commercially, acetone is produced from isopropanol, cumene, or propane to serve as a solvent for resins, fats, oil, plastics, waxes, etc. (30). Acetone may therefore occur in many ecosystems as a naturally produced substance or as an industrial pollutant. It is, however, not accumulating because of its degradability by aerobic (see, e.g., references 25 and 27) and anaerobic (see, e.g., references 28, 36, and 38) bacteria. Because of its biological degradability in the presence or absence of oxygen, it is an especially suitable, nontoxic elutant for extraction of polycyclic aromatic hydrocarbons (PAHs) from contaminated soil for bioremediation. After extraction, the acetone-PAH solution can be easily separated by evaporation or distillation of the solvent. The acetone residue in the soil is harmless because of its rapid biological degradation. In an attempt to study PAH degradation in contaminated soil Samples, PAHs were extracted with acetone. In the first enrichments, nitrate-reducing, acetone-degrading bacteria were obtained. From these enrichments, a new acetone-degrading organism, strain L1, was isolated and subsequently characterized in detail.MATERIALS AND METHODS Sources of organisms. Strain L1 was isolated from a soil sample taken at a depth of 1 m at the site of a defunct natural gas company. (2) and dispensed in an anaerobic c...

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“…Mycobacterium sp. INA1 (DSM 6387) was grown as described before [9] using 16 mM isonicotinate as sole source of carbon, nitrogen and energy. Cell extract was prepared by resuspending wet cells (1 g in 2 ml) in 50 mM citrate buffer, pH 5.5, containing 50 mM KCl (buffer A).…”

Section: Methodsmentioning

confidence: 99%

“…Activity measurements and isolation of 2‐hydroxyisonicotinate were performed as described previously [9]. Substrate specificity of 2‐hydroxyisonicotinate dehydrogenase was examined under the same conditions replacing 2‐hydroxyisonicotinate by the respective substances.…”

Section: Methodsmentioning

confidence: 99%

“…CMP, GMP and AMP were used for identification of the nucleotides [4]. Formation of 2,6‐dihydroxypyridine‐4‐carboxylate from 2‐hydroxyisonicotinate by catalysis of 2‐hydroxyisonicotinate dehydrogenase was monitored by the increase in absorption at 344 nm (2,6‐dihydroxypyridine‐4‐carboxylate) and the corresponding decrease at 312 nm (2‐hydroxyisonicotinate) [9]. N‐terminal sequence analysis were achieved by blotting highly purified 2‐hydroxyisonicotinate dehydrogenase from a 15% SDS‐polyacrylamide gel to a polyvinylidene difluoride membrane.…”

Section: Methodsmentioning

confidence: 99%

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2-Hydroxyisonicotinate dehydrogenase isolated fromMycobacteriumsp. INA1

Schräder

Hillebrand

Andreesen

1998

FEMS Microbiology Letters

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2-Hydroxyisonicotinate dehydrogenase from Mycobacterium sp. INA1 was purified 26-fold to apparent homogeneity. The enzyme is involved in isonicotinate degradation by Mycobacterium sp. INA1 and catalyzes the conversion of 2-hydroxyisonicotinate to 2,6-dihydroxypyridine-4-carboxylate. The purified protein exhibited a native molecular mass of 300 kDa and subunits of 97, 31 and 17 kDa, respectively, indicating an alpha 2 beta 2 gamma 2 structure. The absorption spectrum of the homogeneous enzyme was characteristic for an iron/sulfur flavoprotein, 3.8 mol of iron, 3.7 mol of acid labile sulfur, 0.94 mol of FAD and 0.75 mol of molybdenum were determined per mol of protomer. The molybdenum cofactor was identified as molybdopterin cytosine dinucleotide. 2-Hydroxyisonicotinate dehydrogenase was inactivated in the presence of cyanide. According to these basic properties the protein seems to belong to the class of molybdo-iron/sulfur flavoproteins of the xanthine oxidase family.

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A new pathway for isonicotinate degradation by Mycobacterium sp. INA1

Cited by 30 publications

References 40 publications

Formylmethanofuran dehydrogenases from methanogenic Archaea Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron‐sulfur proteins

Formylmethanofuran dehydrogenases from methanogenic Archaea Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron‐sulfur proteins

Isolation and Characterization of a New Gram-Negative, Acetone-Degrading, Nitrate-Reducing Bacterium from Soil, Paracoccus solventivorans sp. nov.

2-Hydroxyisonicotinate dehydrogenase isolated fromMycobacteriumsp. INA1

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