Article
Allosteric signal transmission involves synergy between discrete structural units of the regulatory subunit of aspartate transcarbamoylase.
Archives of biochemistry and biophysics - 15 Jan 2000
Liu L, Wales M E, Wild J R
Abstract excerpt
Previous studies have shown that the S5' beta-strand (r93-r97) of the regulatory polypeptides of the aspartate transcarbamoylases (ATCases) from Serratia marcescens and Escherichia coli are responsible for their diverged allosteric regulatory patterns, including conversion of CTP from an inhibitor in E. coli to an activator in S. marcescens. Similarly, mutation of residues located in the interface between the...
Topics
- Adenosine Triphosphate
- Allosteric Regulation
- Aspartate Carbamoyltransferase
- Cytidine Triphosphate
- Dimerization
- Escherichia coli
- Kinetics
- Models, Molecular
- Mutation
- Protein Binding
- Protein Structure, Secondary
- Recombinant Proteins
- Serratia marcescens
- Zinc