Article
Enhancement of the thermostability of subtilisin E by introduction of a disulfide bond engineered on the basis of structural comparison with a thermophilic serine protease.
The Journal of biological chemistry - 25 Apr 1990
Takagi H, Takahashi T, Momose H, Inouye M, Maeda Y, Matsuzawa H, Ohta T
Abstract excerpt
Sites for Cys substitutions to form a disulfide bond were chosen in subtilisin E from Bacillus subtilis, a cysteine-free bacterial serine protease, based on the structure of aqualysin I of Thermus aquaticus YT-1 (a thermophilic subtilisin-type protease containing two disulfide bonds). Cys residue...
Topics
- Amino Acid Sequence
- Bacillus subtilis
- Base Sequence
- Calorimetry, Differential Scanning
- Disulfides
- Enzyme Stability
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Oligonucleotide Probes
- Protein Conformation
- Protein Denaturation
- Sequence Homology, Nucleic Acid
- Serine Endopeptidases