Article
L-aspartate association contributes to rate limitation and induction of the T-->R transition in Escherichia coli aspartate transcarbamoylase. Equilibrium exchanges and kinetic isotope effects with a Vmax-enhanced mutant, Asp-236-->Ala.
The Journal of biological chemistry - 28 Apr 1995
Wedler F C, Ley B W, Lee B H, O'Leary M H, Kantrowitz E R
Abstract excerpt
Equilibrium isotope exchange kinetics (EIEK) and kinetic isotope effects have been used to determine the mechanistic basis for the altered kinetic characteristics of a mutant version of Escherichia coli aspartate transcarbamylase in which Asp-236 of the catalytic chain is replaced by alanine (Asp-236-->Ala). The [14C]Asp<--> N-carbamyl-L-aspartate (CAsp) and [14C]CP<-->CAsp exchange rates, observed as a function...
Topics
- Alanine
- Aspartate Carbamoyltransferase
- Aspartic Acid
- Escherichia coli
- Isotopes
- Kinetics
- Ligands
- Mutation
- Point Mutation