Methanogenic degradation of acetone by an enrichment culture

Platen, Harald; Schink, Bernhard

doi:10.1007/bf00425079

Cited by 129 publications

(96 citation statements)

References 33 publications

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“…The sevenfold higher incorporation of 14COz into cell lipids during acetone degradation in comparison with 3-hydroxybutyrate degradation indicated that carbon dioxide is needed for acetone degradation as this was found also for other anaerobic acetone degraders (Siegel 1950;Platen and Schink 1987;Bonnet-Smits et al 1988;Platen and Schink 1989). If acetoacetyl-CoA, which plays a central role in the metabolism of strain KMRActS (see below), is formed after condensation of acetone with carbon dioxide, PHB and also membrane lipids become radioactively labelled.…”

Section: Physiologymentioning

confidence: 68%

Anaerobic degradation of acetone by Desulfococcus biacutus spec. nov.

1990

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Abstract.From anaerobic digestor sludge of a waste water treatment plant, a gram-negative, strictly anaerobic sulfate-reducing bacterium was isolated with acetone as sole organic substrate. The bacterium was characterized as a new species, Desulfocoecus biacutus. The strain grew with acetone with doubling times of 72 h to 120 h; the growth yield was 12.0 (+_2.1) g . [ m o l acetone] -1. Acetone was oxidized completely, and no isopropanol was formed. In labelling studies with 14CO2, cell lipids (including approx. 50% PHB) of acetone-grown cells became labelled 7 times as high as those of 3-hydroxybutyrate-grown cells. Enzyme studies indicated that acetone was degraded via acetoacetyl-CoA, and that acetone was channeled into the intermediary metabolism after condensation with carbon dioxide to a C4-compound, possibly free acetoacetate. Acetoacetyl-CoA is cleaved by a thiolase reaction to acetyl-CoA which is completely oxidized through the carbon monoxide dehydrogenase pathway. Strain K M R A c t S was deposited with the Deutsche Sammlung yon Mikroorganismen, Braunschweig, under the number DSM 5651.

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Section: Physiologymentioning

confidence: 68%

Anaerobic degradation of acetone by Desulfococcus biacutus spec. nov.

1990

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“…(d) A derivative of phenol is the actual substrate; work is in progress to corroborate this possibility. Recently, carboxylation of acetone to 3-oxobutyrate was described [18,191 which may have similar properties; the standard free energy change of that carboxylation at pH 7 is + 17.1 kJ x molF (calculated from data in [20].…”

Section: Discussionmentioning

confidence: 99%

Catalytic properties of phenol carboxylase In vitro study of CO₂: 4‐hydroxybenzoate isotope exchange reaction

Lack

Tommasi

Aresta

et al. 1991

European Journal of Biochemistry

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Phenol is metabolized in a denitrifying bacterium in the absence of molecular oxygen via para-carboxylation to 4-hydroxybenzoate (biological Kolbe-Schmitt synthesis). The enzyme system catalyzing the presumptive carboxylation of phenol, tentatively named 'phenol carboxylase', catalyzes an isotope exchange between 14C02 and the carboxyl group of 4-hydroxybenzoate (specific activity 0.1 pmol 14C02 incorporated into 4-hydroxybenzoate x min-x mg-cell protein) which is considered a partial reaction of the overall enzyme catalysis; 14C from [14C]phenol was not exchanged into 4-hydroxybenzoate ring positions to a significant extent. The 14C02 isotope exchange reaction was studied in vitro. The reaction was dependent on the substrates C 0 2 and 4-hydroxybenzoate and required K + and Mn2+. The actual substrate was C 0 2 rather than HCO,. The apparent K,,, values were 1 mM dissolved COz, 0.2 mM 4-hydroxybenzoate, 2 mM K', and 0.1 mM MnZ+. The cationic cocatalysts could be substituted by ions of similar ionic radius: K' could be replaced to some extent by Rb', but not by Li+, Na', Cs+, or NH:; Mn2+ could be replaced to some extent by Fe2+ >Mg2+, Co2', but not by Ni2+, Zn2+, CaZ+, or Cu2+. The exchange reaction was not strictly specific for 4-hydroxybenzoate, however it required a p-hydroxyl group : derivatives of 4-hydroxybenzoate with OH, CH3 or C1 substituents in m-position did react, whereas those with substitutions in the o-position were inactive or were inhibitory. The enzyme was induced when cells were grown on phenol, but not on 4-hydroxybenzoate. Comparison of SDSjPAGE protein patterns of cells grown on phenol or 4-hydroxybenzoate revealed several additional protein bands in phenolgrown cells. The possible role of similar enzymes in the anaerobic metabolism of phenolic compounds is discussed.Phenolic compounds are important plant constituents and phenol is formed by the activity of microorganisms from a variety of natural and synthetic substrates [l]. In addition phenol is one of the most prominent ground water contaminants. The aerobic metabolism of phenol has been studied extensively; as in all pathways of aerobic aromatic metabolism, oxygenases initiate the degradation of phenol [2].Evidence has recently been presented that phenol is metabolized to C 0 2 by pure bacterial cultures in the absence of molecular oxygen [3] (Fig.

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“…Acetate was determined by gas chromatography as previously described (Platen and Schink 1987). Formation of ammonia was analyzed according to Chaney and Marbach (1962).…”

Section: Chemical Analysesmentioning

confidence: 99%

Fermentative degradation of triethanolamine by a homoacetogenic bacterium

Frings

Wondrak

Schink

1994

Archives of Microbiology

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With triethanolamine as sole source of energy and organic carbon, a strictly anaerobic, gram-positive, rod-shaped bacterium, strain LuTria 3, was isolated from sewage sludge and was assigned to the genus Acetobacterium on the basis of morphological and physiological properties. The G + C content of the DNA was 34.9 + 1.0 mol %. The new isolate fermented triethanolamine to acetate and ammonia. In cell-free extracts, a triethanolaminedegrading enzyme activity was detected that formed acetaldehyde as reaction product. Triethanolamine cleavage was stimulated 30-fold by added adenosylcobalamin (coenzyme B12) and inhibited by cyanocobalamin or hydroxocobalamin. Ethanolamine ammonia lyase, acetaldehyde:acceptor oxidoreductase, phosphate acetyltransferase, acetate kinase, and carbon monoxide dehydrogenase were measured in cell-free extracts of this strain. Our results establish that triethanolamine is degraded by a corrinoid-dependent shifting of the terminal hydroxyl group to the subterminal carbon atom, analogous to a diol dehydratase reaction, to form an unstable intermediate that releases acetaldehyde. No anaerobic degradation of triethylamine was observed in similar enrichment assays.

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Methanogenic degradation of acetone by an enrichment culture

Cited by 129 publications

References 33 publications

Anaerobic degradation of acetone by Desulfococcus biacutus spec. nov.

Anaerobic degradation of acetone by Desulfococcus biacutus spec. nov.

Catalytic properties of phenol carboxylase In vitro study of CO₂: 4‐hydroxybenzoate isotope exchange reaction

Fermentative degradation of triethanolamine by a homoacetogenic bacterium

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Methanogenic degradation of acetone by an enrichment culture

Cited by 129 publications

References 33 publications

Anaerobic degradation of acetone by Desulfococcus biacutus spec. nov.

Anaerobic degradation of acetone by Desulfococcus biacutus spec. nov.

Catalytic properties of phenol carboxylase In vitro study of CO2: 4‐hydroxybenzoate isotope exchange reaction

Fermentative degradation of triethanolamine by a homoacetogenic bacterium

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Catalytic properties of phenol carboxylase In vitro study of CO₂: 4‐hydroxybenzoate isotope exchange reaction