Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase
- 作者：Evan R. Kantrowitz evan.kantrowitz@bc.edu
- 关键词：Allosteric enzyme ; Pyrimidine nucleotide biosynthesis ; Domain motions ; Concerted allosteric transition ; Feedback inhibition
- 刊名：Archives of Biochemistry and Biophysics
- 出版年：2012
- 期刊代码：116_00039861
- 类别：ch
- 出版时间：15 March, 2012
- 卷：519
- 期：2
- 页码：81-90
- 文件大小：2063 K
摘要
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.