The delta6 desaturation of unsaturated acyl-CoA is the first reaction involved in the normal biosynthesis of all polyunsaturated fatty acids families in animal microsomes. Due to this key position it can regulate the biosynthesis of the fatty acids of the series. The reaction is modified by competition with substrates and products, ATP, and acyl-CoA acceptors. Dietary glucose and fructose inhibit the enzyme whereas protein diets and essential fatty acid deficient diets enhance the reaction independently of hormonal effects. The enzyme is sensitive to hormones concentration. Insulin enhance the reaction but the effect is eliminated by protein synthesis inhibition. Hyperglucemic hormones as glucagon, and epinephrine depress the activity of the delta6 desaturase by reactions triggers by an increase of cAMP concentration. The lateral relation of linoleic or alpha-linolenic microsomal elongation is insensitive to insulin, glucagon, epinephrine and protein. All these effects have been proved by either in vivo experiments or cell culture using linoleic or alpha-linolenic acids as substrates.
CITATION STYLE
Brenner, R. R. (1977). Regulatory function of delta6 desaturate -- key enzyme of polyunsaturated fatty acid synthesis. Advances in Experimental Medicine and Biology, 83, 85–101. https://doi.org/10.1007/978-1-4684-3276-3_8
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