Rat liver L-threonine dehydrogenase is a mitochondrial enzyme which transforms L-threonine either into aminoacetone or into acetyl-CoA. We show that it is inhibited by several fatty acids and their derivatives: short chain fatty acids, L-2-hydroxybutyrate and D-3-hydroxybutyrate, long chain fatty acids, such as lauric acid, myristic acid, palmitic and stearic acids, bicarboxylic acids such as malonic acid and its derivatives methyl- and hydroxymalonic acids. The inhibition occurs at low and physiological concentrations of such compounds, which are normally present and metabolized in mitochondria. It presumably plays a role in the physiology of acetyl-CoA-dependent formation of fatty acids and ketobodies, in L-threonine-dependent gluconeogenesis, and in the regulation of L-threonine metabolism by L-threonine dehydrogenase and L-threonine deaminase.
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|Titolo:||Inhibition and regulation of rat liver L-threonine dehydrogenase by different fatty acids and their derivatives|
|Citazione:||Guerranti, R., Pagani, R., Neri, S., Errico, S.V., Leoncini, R., & Marinello, E. (2001). Inhibition and regulation of rat liver L-threonine dehydrogenase by different fatty acids and their derivatives. BIOCHIMICA ET BIOPHYSICA ACTA, 1568(1), 45-52.|
|Appare nelle tipologie:||1.1 Articolo in rivista|