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Stimulation of isocitrate lyase biosynthesis by hydroxylamine and hydrazine

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Summary

Recently it has been demonstrated that hydroxylamine is an activator of triglyceride catabolism. We have studied the effect of hydroxylamine on isocitrate lyase activity and lipid catabolism and have noted a stimulation of isocitrate lyase biosynthesis by 5mm hydroxylamine. The specificity of this effect was tested with a number of representative enzymes of other metabolic pathways.

In an attempt to study the possible mechanism of action of hydroxylamine we have also tested the effects of two substances that are structural or functional analogues of hydroxylamine, namely, ethanolamine and hydrazine, both on the enzyme level in plant cultures and on the activity of enzyme preparations.

From our data we may conclude that “de novo” biosynthesis of isocitrate lyase depends on the reaction of hydroxylamine or hydrazine with glyoxylate to give the corresponding oxime and hydrazone. The removal of glyoxylate from the biological equilibrium in this way could cause extra formation of isocitrate lyase.

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Authors and Affiliations

  1. Institute of Biochemistry and Pharmaceutical Chemistry, University of Florence, Italy

    P. Vanni, M. T. Vincenzini, F. Vincieri & V. Baccari

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  1. P. Vanni
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  2. M. T. Vincenzini
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  3. F. Vincieri
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  4. V. Baccari
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Vanni, P., Vincenzini, M.T., Vincieri, F. et al. Stimulation of isocitrate lyase biosynthesis by hydroxylamine and hydrazine. Mol Cell Biochem 15, 125–131 (1977). https://doi.org/10.1007/BF01793334

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  • DOI: https://doi.org/10.1007/BF01793334

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