Article
Mutation of an essential glutamate residue in folylpolyglutamate synthetase and activation of the enzyme by pteroate binding.
Archives of biochemistry and biophysics - 1 Jun 2002
Sheng Yi, Cross Jennifer A, Shen Yang, Smith Clyde A, Bognar Andrew L
Abstract excerpt
Site-directed mutagenesis was performed on Glu143, an essential amino acid in Lactobacillus casei folylpolyglutamate synthetase (FPGS) and the structurally equivalent residue, Glu146, in Escherichia coli FPGS. Glu143 is positioned near the P-loop and interacts with the Mg(2+) of Mg NTP-binding proteins. We have solved the structure of the E143A mutant of L. casei FPGS in the presence of AMPPCP and Mg(2+). The...
Topics
- Adenosine Diphosphate
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Amino Acid Sequence
- Amino Acid Substitution
- Binding Sites
- Chromatography, Thin Layer
- Enzyme Activation
- Escherichia coli
- Glutamic Acid
- Lacticaseibacillus casei
- Models, Molecular
- Molecular Sequence Data