Article
Conversion of citrate synthase into citryl-CoA lyase as a result of mutation of the active-site aspartic acid residue to glutamic acid.
The Biochemical journal - 1 Dec 1991
Man W J, Li Y, O'Connor C D, Wilton D C
Abstract excerpt
The active-site aspartic acid residue, Asp-362, of Escherichia coli citrate synthase was changed by site-directed mutagenesis to Glu-362, Asn-362 or Gly-362. Only very low catalytic activity could be detected with the Asp----Asn and Asp----Gly mutations. The Asp----Glu mutation produced an enzyme that expressed about 0.8% of the overall catalytic rate, and the hydrolysis step in the reaction, monitored as...
Topics
- Acetyl Coenzyme A
- Aspartic Acid
- Base Sequence
- Binding Sites
- Catalysis
- Citrate (si)-Synthase
- DNA
- Escherichia coli
- Glutamates
- Glutamic Acid
- Lyases
- Molecular Sequence Data