Article
The prosequence of thermolysin acts as an intramolecular chaperone when expressed in trans with the mature sequence in Escherichia coli.
Journal of molecular biology - 5 Feb 1999
Marie-Claire C, Ruffet E, Beaumont A, Roques B P
Abstract excerpt
The zinc metalloendopeptidase, thermolysin (EC 3.4.24.27) produced by Bacillus thermoproteolyticus serves as a model of important physiological enzymes such as neprilysin, angiotensin converting enzyme and endothelin converting enzyme. Thermolysin is synthesised as a pre-proenzyme, with an N-term...
Topics
- Blotting, Western
- Cell Division
- Enzyme Precursors
- Escherichia coli
- Gene Expression Regulation, Bacterial
- Genetic Vectors
- Isopropyl Thiogalactoside
- Molecular Chaperones
- Mutagenesis, Site-Directed
- Mutation
- Recombinant Proteins
- Thermolysin