[Role of pyruvate dehydrogenase and ATP-citrate (pro-3S)lyase in inhibition of the biosynthesis of fatty acids by nicotinic acid].
The pyruvate dehydrogenase and ATP-citrate(pro-3S)lyase activity in the liver after administration of nicotinic acid to chickens against a background of stimulated lypogenesis is shown to increase in the period of maximum fall of the acetyl-CoA-carboxylase activity. Affinity of ATP-citrate (pro-3S)-lyase to citrate at this time is lowered, the content of citrate and isocitrate is elevated and CoASac is decreased to some extent. A conclusion is made on the absence of substrate limitation of acetyl-CoA-carboxylase with administration of nicotinic acid to chickens under conditions of the fatty acid biosynthesis intensification.
D001275:ATP Citrate (pro-S)-Lyase / Q000378:metabolism*; D000818:Animals; D002645:Chickens; D005227:Fatty Acids / Q000096:biosynthesis*; D007700:Kinetics; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D009525:Niacin / Q000494:pharmacology*; D011768:Pyruvate Dehydrogenase Complex / Q000378:metabolism*
D005227:Fatty Acids; D011768:Pyruvate Dehydrogenase Complex; D009525:Niacin; D001275:ATP Citrate (pro-S)-Lyase
Rol' piruvatdegidrogenazy i ATP-tsitrat(pro-3S)liazy v ingivirovanii biosinteza zhirnykh kislot nikotinovoĭ kislotoĭ.