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Dynamics of Activity of the Key Enzymes of Polyhydroxyalkanoate Metabolism in Ralstonia eutropha B5786

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Abstract

The dynamics of accumulation of polyhydroxybutyrate (PHB) and the activities of key enzymes of PHB metabolism (β-ketothiolase, acetoacetyl-CoA reductase, PHB synthase, D-hydroxybutyrate dehydrogenase, and PHB depolymerase) in the hydrogen bacterium Ralstonia eutropha B5786 were studied under various conditions of carbon nutrition and substrate availability. The highest activities of β-ketothiolase, acetoacetyl-CoA reductase, and PHB synthase were recorded during acceleration of PHB synthesis. The activities of enzymes catalyzing PHB depolymerization (PHB depolymerase and D-hydroxybutyrate dehydrogenase) were low, being expressed only upon stimulated endogenous PHB degradation. The change of carbon source (CO2 or fructose) did not affect the time course of the enzyme activity significantly.

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Authors and Affiliations

  1. Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russia

    T. G. Volova, G. S. Kalacheva, O. V. Gorbunova & N. O. Zhila

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  1. T. G. Volova
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  2. G. S. Kalacheva
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  3. O. V. Gorbunova
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  4. N. O. Zhila
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Volova, T.G., Kalacheva, G.S., Gorbunova, O.V. et al. Dynamics of Activity of the Key Enzymes of Polyhydroxyalkanoate Metabolism in Ralstonia eutropha B5786. Applied Biochemistry and Microbiology 40, 170–177 (2004). https://doi.org/10.1023/B:ABIM.0000018921.04863.d5

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