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Sensitivity to pH, product inhibition, and inhibition by NAD+ of 1,3-propanediol dehydrogenase purified from Enterobacter agglomerans CNCM 1210

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Abstract

Because of its key role in the metabolism of glycerol during fermentation, 1,3-propanediol dehydrogenase (EC 1.1.1.202) of Enterobacter agglomerans CNCM 1210 was purified to homogeneity and studied with respect to its sensitivity to pH and to nucleotide and 1,3-propanediol concentrations. Enzyme activity was optimal at pH 7.8. The enzyme was competitively inhibited by NAD+ (Ki of 0.29 mM), and 1,3-propanediol exerted a strong inhibitory effect according to a mixed-type inhibition with a Ki of 13.7 mM and an a-factor of 9.0. It is proposed that these dehydrogenase properties be extended to the dehydrogenases of Citrobacter freundii and Klebsiella pneumoniae, which exhibited numerous similar physical properties.

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Authors and Affiliations

  1. Institut National de la Recherche Agronomique, Laboratoire de Biotechnologie de l’Environnement, Avenue des étangs, F-11100 Narbonne, France, , , , , , FR

    Fabien Barbirato, Anne Larguier, Thierry Conte, Suzette Astruc & A. Bories

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  1. Fabien Barbirato
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  2. Anne Larguier
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  3. Thierry Conte
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  4. Suzette Astruc
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  5. A. Bories
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Received: 4 December 1996 / Accepted: 24 March 1997

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Barbirato, F., Larguier, A., Conte, T. et al. Sensitivity to pH, product inhibition, and inhibition by NAD+ of 1,3-propanediol dehydrogenase purified from Enterobacter agglomerans CNCM 1210. Arch Microbiol 168, 160–163 (1997). https://doi.org/10.1007/s002030050482

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  • DOI: https://doi.org/10.1007/s002030050482

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