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Modeling the Negative Feedback Mechanism in the Enzyme Carboxyltransferase

[+] Author Affiliations
Xiaoyu Cai, Marcio de Queiroz, Glen Meades, Jr., Grover Waldrop

Louisiana State University, Baton Rouge, LA

Paper No. DSCC2011-6171, pp. 531-536; 6 pages
doi:10.1115/DSCC2011-6171
From:
  • ASME 2011 Dynamic Systems and Control Conference and Bath/ASME Symposium on Fluid Power and Motion Control
  • ASME 2011 Dynamic Systems and Control Conference and Bath/ASME Symposium on Fluid Power and Motion Control, Volume 2
  • Arlington, Virginia, USA, October 31–November 2, 2011
  • Conference Sponsors: Dynamic Systems and Control Division
  • ISBN: 978-0-7918-5476-1
  • Copyright © 2011 by ASME

abstract

The enzyme acetyl-CoA carboxylase catalyzes the first committed step in fatty acid synthesis in all organisms. The E. coli form of the carboxyltransferase subunit was recently found to regulate its own activity and expression by binding its own mRNA. By binding acetyl-CoA or the mRNA encoding its own subunits, Carboxyltransferase is able to sense the metabolic state of the cell and attenuate its own translation and enzymatic activity using a negative feedback mechanism. In this paper, this network of interactions is modeled mathematically using mass action kinetics. Numerical simulations of the model show agreement with experimental results.

Copyright © 2011 by ASME

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