Article
Long range effects of amino acid substitutions in the catalytic chain of aspartate transcarbamoylase. Localized replacements in the carboxyl-terminal alpha-helix cause marked alterations in allosteric properties and intersubunit interactions.
The Journal of biological chemistry - 5 Feb 1992
Peterson C B, Schachman H K
Abstract excerpt
A single alpha-helical polypeptide segment of 21 amino acids near the carboxyl terminus of the catalytic chain of aspartate transcarbamoylase from Escherichia coli has been shown recently to be important for the in vivo folding of the chains and assembly of the enzyme (Peterson, C. B., and Schach...
Topics
- Allosteric Regulation
- Amino Acids
- Aspartate Carbamoyltransferase
- Aspartic Acid
- Catalysis
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Kinetics
- Mutation
- Phosphonoacetic Acid
- Protein Conformation