Article
Altered nucleotide cofactor-dependent properties of the mutant [S240K]RecA protein.
Biochemical and biophysical research communications - 11 May 2012
Steffen Scott E, Bryant Floyd R
Abstract excerpt
Two mutant Escherichia coli RecA proteins were prepared in which the ATP active site residue, Ser240, was replaced with asparagine and lysine (these amino acids are found in the corresponding positions in other bacterial RecA proteins). The S240N mutation had no discernible effect on the ATP-dependent activities of the RecA protein, indicating that serine and asparagine are functionally interchangeable at...
Topics
- Adenosine Triphosphate
- Amino Acid Substitution
- Bacterial Proteins
- Deoxyadenine Nucleotides
- Escherichia coli
- Hydrolysis
- Lysine
- Mutation
- Nucleotides
- Proteolysis
- Rec A Recombinases