Article
Importance of domain closure for the catalysis and regulation of Escherichia coli aspartate transcarbamoylase.
The Journal of biological chemistry - 26 Jul 2002
Macol Christine P, Tsuruta Hiro, Kantrowitz Evan R
Abstract excerpt
Two hybrid versions of Escherichia coli aspartate transcarbamoylase were studied to determine the influence of domain closure on the homotropic and heterotropic properties of the enzyme. Each hybrid holoenzyme had one wild-type and one inactive catalytic subunit. In the first case the inactive catalytic subunit had Arg-54 replaced by alanine. The holoenzyme with this mutation in all six catalytic chains exhibits...
Topics
- Anions
- Aspartate Carbamoyltransferase
- Binding Sites
- Catalysis
- Chromatography, Ion Exchange
- Dose-Response Relationship, Drug
- Escherichia coli
- Kinetics
- Lysine
- Models, Molecular
- Mutation
- Protein Binding
- Protein Structure, Tertiary
- Scattering, Radiation
- Serine
- X-Rays