NADP+-specific 2-oxoglutarate dehydrogenase in denitrifying Pseudomonas species (original) (raw)

Abstract

Several denitrifying Pseudomonas strains contained an NADP+-specific 2-oxoglutarate dehydrogenase, in contrast to an NAD+-specific pyruvate dehydrogenase, if the cells were grown anaerobically with aromatic compounds. With non-aromatic substrates or after aerobic growth the coenzyme specificity of 2-oxoglutarate dehydrogenase changed to NAD+-specificity. The reaction stoichiometry and the apparent K m-values of the enriched enzymes were determined: pyruvate 0.5 mM, coenzyme A 0.05 mM, NAD+ 0.25 mM; 2-oxoglutarate 0.6 mM, coenzyme A 0.05 mM, NADP+ 0.03 mM. Isocitrate dehydrogenase was NADP+-specific. The findings suggest that these strains contained at least two lipoamide dehydrogenases, one NAD+-specific, the other NADP+-specific.

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1. Abteilung Angewandte Mikrobiologie, Universität Ulm, P. O. Box 4066, D-7900, Ulm, Federal Republic of Germany
   Christa Lochmeyer & Georg Fuchs

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1. Christa Lochmeyer
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2. Georg Fuchs
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Lochmeyer, C., Fuchs, G. NADP+-specific 2-oxoglutarate dehydrogenase in denitrifying Pseudomonas species.Arch. Microbiol. 153, 226–229 (1990). https://doi.org/10.1007/BF00249072

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• Received: 04 September 1989
• Accepted: 07 October 1989
• Issue Date: February 1990
• DOI: https://doi.org/10.1007/BF00249072

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