Article
Allosteric activation in Bacillus stearothermophilus lactate dehydrogenase investigated by an X-ray crystallographic analysis of a mutant designed to prevent tetramerization of the enzyme.
Journal of molecular biology - 13 May 1994
Cameron A D, Roper D I, Moreton K M, Muirhead H, Holbrook J J, Wigley D B
Abstract excerpt
The crystal structure of a mutant Bacillus stearothermophilus lactate dehydrogenase, into which an additional loop has been engineered in order to prevent tetramerization of the enzyme, has been solved and refined at 2.4 A. The minimal repeat unit in the crystal is a dimer and the tetramer cannot...
Topics
- Allosteric Regulation
- Amino Acids
- Binding Sites
- Crystallography, X-Ray
- Fructosediphosphates
- Geobacillus stearothermophilus
- L-Lactate Dehydrogenase
- Models, Molecular
- Mutation
- NAD
- Protein Conformation