Article
Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants.
The Journal of biological chemistry - 20 Oct 1995
Li Y, Hu Z, Jordan F, Inouye M
Abstract excerpt
The amino-terminal propeptide, consisting of 77 amino acid residues, is known to be required as an intramolecular chaperone to guide the folding of mature subtilisin E, a serine protease, into active mature enzyme. Many mutations within the pro-sequence have been shown to abolish the production of active subtilisin E (Kobayashi, T., and Inouye, M. (1992) J. Mol. Biol. 226, 931-933). Here we report...
Topics
- Amino Acid Sequence
- Base Sequence
- Enzyme Precursors
- Molecular Chaperones
- Molecular Sequence Data
- Mutation
- Protein Folding
- Structure-Activity Relationship
- Subtilisins