1994
DOI: 10.1099/13500872-140-2-409
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Anaerobic degradation of pimelate by newly isolated denitrifying bacteria

Abstract: A C, dicarboxylic (pimelic) acid derivative is postulated as an intermediate in anaerobic degradation of benzoate. Four strains of Gram-negative, nitratereducing bacteria capable of growth with both pimelate and benzoate as sole carbon and energy source were isolated. The metabolism of strain LP-1, which was enriched from activated sludge with pimelate as substrate, was studied in detail. This strain grew only with oxygen or with oxidized nitrogen compounds as electron acceptor. In the presence of nitrate, a w… Show more

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Cited by 30 publications
(25 citation statements)
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“…The pimelyl-CoA dehydrogenase activity, which was demonstrated for the first time in a benzoate-grown anaerobic microorganism, was not detected in a nitrate-reducing isolate when it was grown with benzoate (16), probably because benzoate degradation in the isolate proceeds via transformation of cyclohex-1,5-diene carboxyl-CoA to 3-hydroxypimelate without the formation of pimelyl-CoA. The dehydrogenase activity was detected, however, when the same isolate was grown on pimelate (16). It could also be argued that the observed cyclohex-1-ene carboxyl-CoA hydratase activity is due to the action of an enoyl-CoA hydratase, which acts primarily on short-chain unsaturated fatty acids (28).…”
Section: Discussionmentioning
confidence: 89%
“…The pimelyl-CoA dehydrogenase activity, which was demonstrated for the first time in a benzoate-grown anaerobic microorganism, was not detected in a nitrate-reducing isolate when it was grown with benzoate (16), probably because benzoate degradation in the isolate proceeds via transformation of cyclohex-1,5-diene carboxyl-CoA to 3-hydroxypimelate without the formation of pimelyl-CoA. The dehydrogenase activity was detected, however, when the same isolate was grown on pimelate (16). It could also be argued that the observed cyclohex-1-ene carboxyl-CoA hydratase activity is due to the action of an enoyl-CoA hydratase, which acts primarily on short-chain unsaturated fatty acids (28).…”
Section: Discussionmentioning
confidence: 89%
“…A glutaryl-CoA dehydrogenase was significantly produced in crude extracts of bacteria growing anaerobically in aromatic compounds (and cyclohexane carboxylate), which suggests that glutaryl-CoA was indeed an intermediate formed during the catabolism of these compounds via the pimelyl-CoA/3-hydroxypimelyl-CoA ␤-oxidation pathway (28,106,118,140,141,153,328). Recently, the gcdH gene, encoding the bifunctional glutaryl-CoA dehydrogenase enzyme, has been identified and characterized for Azoarcus sp.…”
Section: Benzoate Catabolism: the Benzoyl-coa Degradation Pathwaymentioning
confidence: 99%
“…The further degradation of the aliphatic C 7 -dicarboxyl-CoA derivative generates three acetyl-CoAs and CO 2 ( Fig. 3) (118,140). Usually, bacteria contain many genes that might participate in the metabolism of the dicarboxyl-CoA intermediates formed during the anaerobic metabolism of aromatic (and alicyclic) acids as well as in the catabolism of dicarboxylic acids.…”
Section: Benzoate Catabolism: the Benzoyl-coa Degradation Pathwaymentioning
confidence: 99%
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“…Succinate and sugars were quantified by HPLC with an Interaction ORH-801 organic acids column packed with a cation-exchange polymer (Interaction Chemicals, Mountain View, USA) and refractive-index detection (Gallus and Schink 1994). Production of surface-active substances was first checked half-quantitatively following the unmixing process of The original publication is available at www.springerlink.com First publ.…”
Section: Methodsmentioning
confidence: 99%