Purification of glutaryl-CoA dehydrogenase from Pseudomonas sp., an enzyme involved in the anaerobic degradation of benzoate View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-02

AUTHORS

Ulrich Härtel, Elke Eckel, Jürgen Koch, Georg Fuchs, Dietmar Linder, Wolfgang Buckel

ABSTRACT

Cell-free extracts of Pseudomonas sp. strains KB 740 and K 172 both contained high levels of glutaryl-CoA dehydrogenase when grown anaerobically on benzoate or other aromatic compounds and with nitrate as electron acceptor. These aromatic compounds have in common benzoyl-CoA as the central aromatic intermediate of anaerobic metabolism. The enzymatic activity was almost absent in cells grown aerobically on benzoate regardless whether nitrate was present. Glutaryl-CoA dehydrogenase activity was also detected in cell-free extracts of Rhodopseudomonas, Rhodomicrobium and Rhodocyclus after phototrophic growth on benzoate. Parallel to the induction of glutaryl-CoA dehydrogenase as measured with ferricenium ion as electron acceptor, an about equally high glutaconyl-CoA decarboxylase activity was detected in cell-free extracts. The latter activity was measured with the NAD-dependent assay, as described for the biotin-containing sodium ion pump glutaconyl-CoA decarboxylase from glutamate fermenting bacteria. Glutaryl-CoA dehydrogenase was purified to homogeneity from both Pseudomonas strains. The enzymes catalyse the decarboxylation of glutaconyl-CoA at about the same rate as the oxidative decarboxylation of glutaryl-CoA. The green enzymes are homotetramers (m = 170 kDa) and contain 1 mol FAD per subunit. No inhibition was observed with avidin indicating the absence of biotin. The N-terminal sequences of the enzymes from both strains are similar (65%). More... »

PAGES

174-181

References to SciGraph publications

Journal

TITLE

Archives of Microbiology

ISSUE

2

VOLUME

159

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/bf00250279

    DOI

    http://dx.doi.org/10.1007/bf00250279

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1025300827

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/8439237


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