[Interaction of acetyl-CoA carboxylase from the rat liver with analogs of activated carbon dioxide and ATP].
The interaction of rat liver Ac-CoA-carboxylase with reactive and stable analogs of carbon dioxide and phosphoric acid mixed anhydrides--hypothetic intermediate of the enzyme reaction--has been studied. Carbamoylphosphate showed substrate properties, whereas phosphonacetic acid and beta-oxopropyl-alpha, alpha-diphosphonate inhibited this enzyme (Ki 3.0 and 3.5 mM correspondingly). The analog of another possible intermediate in the reaction of ATP and carbon dioxide, Appp (CH2COOH) also inhibited Ac-CoA-carboxylase (Ki = 0.7 mM).
D000106:Acetate-CoA Ligase / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism*; D000818:Animals; D002221:Carbamyl Phosphate / Q000378:metabolism; D002245:Carbon Dioxide / Q000378:metabolism*; D003066:Coenzyme A Ligases / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D051381:Rats
D002245:Carbon Dioxide; D002221:Carbamyl Phosphate; D000255:Adenosine Triphosphate; D003066:Coenzyme A Ligases; D000106:Acetate-CoA Ligase
Vzaimodeĭstvie atsetil-CoA-karboksilazy pecheni krys s analogami aktivirovannoĭ uglekisloty i ATP.