Regulation of the structure and activity of pyruvate carboxylase by acetyl CoA.

@article{Adinazada2012RegulationOT,
  title={Regulation of the structure and activity of pyruvate carboxylase by acetyl CoA.},
  author={A Adina-zada and Tonya N Zeczycki and Paul V. Attwood},
  journal={Archives of biochemistry and biophysics},
  year={2012},
  volume={519 2},
  pages={118-30}
}
In this review we examine the effects of the allosteric activator, acetyl CoA on both the structure and catalytic activities of pyruvate carboxylase. We describe how the binding of acetyl CoA produces gross changes to the quaternary and tertiary structures of the enzyme that are visible in the electron microscope. These changes serve to stabilize the tetrameric structure of the enzyme. The main locus of activation of the enzyme by acetyl CoA is the biotin carboxylation domain of the enzyme… CONTINUE READING
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