| Autor: |
Guerranti R; Institute of Biochemistry and Enzymology, University of Siena, Via A. Moro 2, 53100 Siena, Italy., Pagani R, Neri S, Errico SV, Leoncini R, Marinello E |
| Jazyk: |
angličtina |
| Zdroj: |
Biochimica et biophysica acta [Biochim Biophys Acta] 2001 Nov 07; Vol. 1568 (1), pp. 45-52. |
| DOI: |
10.1016/s0304-4165(01)00197-0 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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