Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 23 December 1966:
Vol. 154. no. 3756, pp. 1572 - 1573
DOI: 10.1126/science.154.3756.1572

Articles

Control of the Activity of Escherichia coli Carbamoyl Phosphate Synthetase by Antagonistic Allosteric Effectors

André Piérard 1

1 Institut de Recherches du Centre d'Enseignement et de Recherches des Industries Alimentaires et Chimiques (C.E.R.I.A.), Bruxelles 7, Belgium

The synthesis of carbamoyl phosphate required in both arginine and pyrimidine biosyntheses is carried out by a single enzyme in Escherichia coli. Opposed effects of pyrimidine nucleotides and of ornithine on the activity of the enzyme ensure a proper supply of carbamoyl phosphate according to the needs of the two biosynthetic sequences.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Arginine Biosynthesis in Escherichia coli: EXPERIMENTAL PERTURBATION AND MATHEMATICAL MODELING.
M. Caldara, G. Dupont, F. Leroy, A. Goldbeter, L. De Vuyst, and R. Cunin (2008)
J. Biol. Chem. 283, 6347-6358
   Abstract »    Full Text »    PDF »
Unmasking a Functional Allosteric Domain in an Allosterically Nonresponsive Carbamoyl-phosphate Synthetase.
B. Eroglu and S. G. Powers-Lee (2002)
J. Biol. Chem. 277, 45466-45472
   Abstract »    Full Text »    PDF »



ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)