Article
Mutation of amino acids thought to polarize the oxaloacetate carbonyl in citrate synthase severely reduces but does not abolish activity of the enzyme.
Biochemistry and cell biology = Biochimie et biologie cellulaire - 1 Jan 2000
Anderson D H, Duckworth H W
Abstract excerpt
Oligonucleotide-directed mutagenesis has been used to alter two active site residues of Escherichia coli citrate synthase, histidine-305 and arginine-314. Both residues are thought to be involved in the polarization of the carbonyl group of oxaloacetate and thus facilitate attack at the carbonyl...
Topics
- Amino Acids
- Binding Sites
- Citrate (si)-Synthase
- Escherichia coli
- Kinetics
- Mutation
- Oxaloacetates
- Oxo-Acid-Lyases