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Arch Biochem Biophys. 2012 Mar 15;519(2):81-90. doi: 10.1016/j.abb.2011.10.024. Epub 2011 Dec 16.

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase.

Author information

1
Department of Chemistry, Boston College, Merkert Chemistry Center, Chestnut Hill, MA 02467, USA. evan.kantrowitz@bc.edu

Abstract

The allosteric enzyme aspartate transcarbamoylase (ATCase) from Escherichia coli has been the subject of investigations for approximately 50 years. This enzyme controls the rate of pyrimidine nucleotide biosynthesis by feedback inhibition, and helps to balance the pyrimidine and purine pools by competitive allosteric activation by ATP. The catalytic and regulatory components of the dodecameric enzyme can be separated and studied independently. Many of the properties of the enzyme follow the Monod, Wyman Changeux model of allosteric control thus E. coli ATCase has become the textbook example. This review will highlight kinetic, biophysical, and structural studies which have provided a molecular level understanding of how the allosteric nature of this enzyme regulates pyrimidine nucleotide biosynthesis.

PMID:
22198283
PMCID:
PMC3393099
DOI:
10.1016/j.abb.2011.10.024
[Indexed for MEDLINE]
Free PMC Article

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