Article
Dissection of the functional domains of Escherichia coli carbamoyl phosphate synthetase by site-directed mutagenesis.
The Journal of biological chemistry - 15 May 1990
Post L E, Post D J, Raushel F M
Abstract excerpt
The catalytic functions of the amino-terminal and carboxyl-terminal halves of the large subunit of carbamoyl phosphate synthetase from Escherichia coli have been identified using site-directed mutagenesis. Glycine residues at positions 176, 180, and 722 within the putative mononucleotide-binding...
Topics
- Adenosine Diphosphate
- Adenosine Triphosphate
- Amino Acid Sequence
- Binding Sites
- Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)
- Carbamyl Phosphate
- Escherichia coli
- Glycine
- Isoleucine
- Kinetics
- Molecular Sequence Data
- Mutation
- Sequence Homology, Nucleic Acid
- Transformation, Bacterial