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Stimulation of isocitrate lyase biosynthesis by hydroxylamine and hydrazine.
Mol Cell Biochem. 1977 Apr 12; 15(2):125-31.MC

Abstract

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 5 mM 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 nove" 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.

Authors

Vanni P
No affiliation info available
Vincenzini MT
No affiliation info available
Vincieri F
No affiliation info available
Baccari V
No affiliation info available

MeSH

Dose-Response Relationship, DrugEnzyme InductionEthanolaminesGlyoxylatesHydrazinesHydroxylaminesIsocitrate LyaseMalate SynthaseOxo-Acid-LyasesTime Factors

Pub Type(s)

Journal Article

Language

eng

PubMed ID

895730

Citation

Vanni, P, et al. "Stimulation of Isocitrate Lyase Biosynthesis By Hydroxylamine and Hydrazine." Molecular and Cellular Biochemistry, vol. 15, no. 2, 1977, pp. 125-31.
Vanni P, Vincenzini MT, Vincieri F, et al. Stimulation of isocitrate lyase biosynthesis by hydroxylamine and hydrazine. Mol Cell Biochem. 1977;15(2):125-31.
Vanni, P., Vincenzini, M. T., Vincieri, F., & Baccari, V. (1977). Stimulation of isocitrate lyase biosynthesis by hydroxylamine and hydrazine. Molecular and Cellular Biochemistry, 15(2), 125-31.
Vanni P, et al. Stimulation of Isocitrate Lyase Biosynthesis By Hydroxylamine and Hydrazine. Mol Cell Biochem. 1977 Apr 12;15(2):125-31. PubMed PMID: 895730.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Stimulation of isocitrate lyase biosynthesis by hydroxylamine and hydrazine. AU - Vanni,P, AU - Vincenzini,M T, AU - Vincieri,F, AU - Baccari,V, PY - 1977/4/12/pubmed PY - 1977/4/12/medline PY - 1977/4/12/entrez SP - 125 EP - 31 JF - Molecular and cellular biochemistry JO - Mol Cell Biochem VL - 15 IS - 2 N2 - 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 5 mM 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 nove" 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. SN - 0300-8177 UR - https://www.unboundmedicine.com/medline/citation/895730/Stimulation_of_isocitrate_lyase_biosynthesis_by_hydroxylamine_and_hydrazine_ DB - PRIME DP - Unbound Medicine ER -