Article
Specific suppression of heterotropic interactions in phosphofructokinase by the mutation of leucine 178 into tryptophan.
The Journal of biological chemistry - 25 Jul 1990
Serre M C, Teschner W, Garel J R
Abstract excerpt
The leucine residue at position 178 in the allosteric phosphofructokinase from Escherichia coli has been changed into a tryptophan residue by oligonucleotide-directed mutagenesis. The modified enzyme has been purified to homogeneity, and its enzymatic properties show that this single mutation suppresses the heterotropic interactions without affecting the homotropic ones. The mutant has the same saturation curve...
Topics
- Allosteric Regulation
- DNA Mutational Analysis
- Escherichia coli
- Guanosine Diphosphate
- Hot Temperature
- Kinetics
- Leucine
- Mutation
- Phosphoenolpyruvate
- Phosphofructokinase-1
- Protein Denaturation