Article
Aspartate aminotransferase with the pyridoxal-5'-phosphate-binding lysine residue replaced by histidine retains partial catalytic competence.
European journal of biochemistry - 26 Jan 1990
Ziak M, Jaussi R, Gehring H, Christen P
Abstract excerpt
The active site residue lysine 258 of chicken mitochondrial aspartate aminotransferase was replaced with a histidine residue by means of site-directed mutagenesis. The mutant protein was expressed in Escherichia coli and purified to homogeneity. Addition of 2-oxoglutarate to its pyridoxamine form...
Topics
- Animals
- Aspartate Aminotransferases
- Binding Sites
- Binding, Competitive
- Catalysis
- Chickens
- Circular Dichroism
- Escherichia coli
- Gene Expression Regulation, Enzymologic
- Histidine
- Lysine
- Mutation
- Plasmids
- Protein Engineering
- Pyridoxal Phosphate
- Recombinant Proteins