Article
Characterization of the leader peptide of an endo-type cellulase produced by an alkalophilic Streptomyces strain.
Agricultural and biological chemistry - 1 Jul 1991
Park J S, Horinouchi S, Beppu T
Abstract excerpt
An endo-type semi-alkaline cellulase (CMCase I) produced by an alkalophilic Streptomyces strain has an extraordinarily long leader peptide of about 70 amino acids (aa), which can be grouped into four distinct regions, an NH2-terminal region (13 aa), an Arg-cluster region (13 aa), a hydrophobic region (23 aa), and an Ala/Pro-repeat region (12 aa). For identification of the function of each part of the leader...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Base Sequence
- Cellulase
- Glycoside Hydrolases
- Hydrogen-Ion Concentration
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Plasmids
- Protein Sorting Signals