Article
Yeast allosteric chorismate mutase is locked in the activated state by a single amino acid substitution.
Biochemistry - 17 Apr 1990
Schmidheini T, Mösch H U, Evans J N, Braus G
Abstract excerpt
Chorismate mutase, a branch-point enzyme in the aromatic amino acid pathway of Saccharomyces cerevisiae, and also a mutant chorismate mutase with a single amino acid substitution in the C-terminal part of the protein have been purified approximately 20-fold and 64-fold from overproducing strains, respectively. The wild-type enzyme is activated by tryptophan and subject to feedback inhibition by tyrosine, whereas...
Topics
- Amino Acid Sequence
- Binding Sites
- Chorismate Mutase
- Enzyme Activation
- Hydrogen-Ion Concentration
- Isomerases
- Kinetics
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Molecular Weight
- Mutation