[Structure, properties and regulation of acetyl-CoA-carboxylase activity].
The paper deals with the analysis of data available in literature and those of the authors' own investigations concerning the structure, properties and regulation of acetyl-CoA-carboxylase. Nicotinic acid is one of the factors regulating the enzyme activity in the animal liver. It inhibits the acetyl-CoA-carboxylase activity through two mechanisms--allosteric regulation and covalent modification. A comparative characteristic of the studied enzyme preparations has shown that administration of nicotinic acid to animals leads to phosphorylation of acetyl-CoA-carboxylase which affects its structure. A complex with homogenic acetyl-CoA-carboxylase is found to contain cAMP-independent and cAMP-dependent protein kinase. The phosphorylation is controlled by citrate competing with nicotinic acid for the coupling sites.
D000105:Acetyl Coenzyme A / Q000378:metabolism; D000103:Acetyl-CoA Carboxylase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D000494:Allosteric Regulation; D000818:Animals; D002645:Chickens; D002951:Citrates / Q000378:metabolism; D005227:Fatty Acids / Q000096:biosynthesis; D008025:Ligases / Q000378:metabolism*; D008055:Lipids / Q000096:biosynthesis; D008099:Liver / Q000201:enzymology* / Q000378:metabolism; D009525:Niacin / Q000494:pharmacology; D010766:Phosphorylation; D013379:Substrate Specificity
D002951:Citrates; D005227:Fatty Acids; D008055:Lipids; D009525:Niacin; D000105:Acetyl Coenzyme A; D008025:Ligases; D000103:Acetyl-CoA Carboxylase
Struktura, svoĭstva i reguliatsiia aktivnosti atsetil-CoA-karboksilazy.