Article
Introduction of a stabilizing 10 residue beta-hairpin in Bacillus subtilis neutral protease.
Protein engineering - 1 Mar 1992
Eijsink V G, Vriend G, van den Burg B, van der Zee J R, Veltman O R, Stulp B K, Venema G
Abstract excerpt
A 10 residue beta-hairpin, which is characteristic of thermostable Bacillus neutral proteases, was engineered into the thermolabile neutral protease of Bacillus subtilis. The recipient enzyme remained fully active after introduction of the loop. However, the mutant protein exhibited autocatalytic nicking and a 0.4 degree C decrease in thermostability. Two additional point mutations designed to improve the...
Topics
- Amino Acid Sequence
- Bacillus subtilis
- Enzyme Stability
- Genetic Engineering
- Hydrogen Bonding
- Metalloendopeptidases
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis
- Mutation
- Protein Conformation