Article
Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase.
Biochemistry - 17 Apr 1990
Eisenstein E, Markby D W, Schachman H K
Abstract excerpt
The sigmoidal dependence of activity on substrate concentration exhibited by the regulatory enzyme aspartate transcarbamoylase (ATCase) of Escherichia coli is generally attributed to a ligand-promoted change in the quaternary structure of the enzyme. Although a global conformational change in ATC...
Topics
- Adenosine Triphosphate
- Allosteric Regulation
- Aspartate Carbamoyltransferase
- Aspartic Acid
- Binding Sites
- Carbamyl Phosphate
- Cytidine Triphosphate
- Escherichia coli
- Kinetics
- Mutation
- Phosphonoacetic Acid
- Protein Conformation
