Article
Importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamoylase.
Biochemistry - 24 Apr 1990
Stebbins J W, Zhang Y, Kantrowitz E R
Abstract excerpt
Site-specific mutagenesis has been used to create two mutant versions of aspartate transcarbamoylase. Arg-167 and Gln-231, both previously identified as interacting with the portion of the bisubstrate analogue N-(phosphonoacetyl)-L-aspartate (PALA) that corresponds to aspartate [Krause, K. L., Vo...
Topics
- Adenosine Triphosphate
- Allosteric Regulation
- Aspartate Carbamoyltransferase
- Aspartic Acid
- Binding Sites
- Catalysis
- Cytidine Triphosphate
- Escherichia coli
- Glutamine
- Kinetics
- Mutation
- Phosphonoacetic Acid
- Protein Conformation