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1. [Interaction of acetyl-CoA carboxylase from the rat liver with analogs of activated carbon dioxide and ATP].

Author

Amontov SV, Rabinkov AG, Tyrtysh TV, Tarusova NB, and Goriachenkova EV

Subjects
Adenosine Triphosphate analogs & derivatives, Animals, Carbamyl Phosphate metabolism, Rats, Acetate-CoA Ligase metabolism, Adenosine Triphosphate metabolism, Carbon Dioxide metabolism, Coenzyme A Ligases metabolism, Liver enzymology
Abstract

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).

Published
1988

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