[Citrate influence on acetyl-CoA-carboxylase activation and phosphorylation in chicken liver with lipogenesis inhibited by nicotinic acid].
Nicotinic acid in vivo affects the citrate demand for acetyl-CoA-carboxylase activation in the chicken liver under conditions of alimentary lipogenesis stimulation. Stoichiometry of the citrate binding with the dissociation constant of the enzyme-allosteric activator complex is determined under experimental conditions. Endogenic phosphorylation of acetyl-CoA-carboxylase completely correlates with its inactivation and depends on the citrate level. cAMP is established to have an activating effect on phosphorylation of acetyl-CoA-carboxylase of test animals.
Fomenko
A I
AI
Khalmuradov
A G
AG
Khustochka
L N
LN
Pozharum
S V
SV
Stepanenko
S P
SP
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism*; D000818:Animals; D002645:Chickens; D002951:Citrates / Q000378:metabolism*; D019343:Citric Acid; D000242:Cyclic AMP / Q000502:physiology; D004789:Enzyme Activation; D008025:Ligases / Q000378:metabolism*; D008055:Lipids / Q000096:biosynthesis; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D009525:Niacin / Q000494:pharmacology*; D010766:Phosphorylation
D002951:Citrates; D008055:Lipids; D009525:Niacin; D019343:Citric Acid; D000242:Cyclic AMP; D008025:Ligases; D000103:Acetyl-CoA Carboxylase
Vliianie tsitrata na aktivatsiiu i stepen' fosforilirovaniia atsetil CoA-karboksilazy pecheni tsypliat pri ingibirovanii lipogeneza nikotinovoĭ kislotoĭ.