Article
A substitution at His-120 in the LasA protease of Pseudomonas aeruginosa blocks enzymatic activity without affecting propeptide processing or extracellular secretion.
Journal of bacteriology - 1 Nov 1996
Gustin J K, Kessler E, Ohman D E
Abstract excerpt
The LasA protease of Pseudomonas aeruginosa can degrade elastin and is an important contributor to the pathogenesis of this organism. LasA (20 kDa) is a member of the beta-lytic endopeptidase family of extracellular bacterial proteases, and it shows high-level staphylolytic activity. We sequenced...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Bacteriolysis
- Base Sequence
- Binding Sites
- Enzyme Activation
- Enzyme Precursors
- Escherichia coli
- Histidine
- Membrane Proteins
- Metalloendopeptidases
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Protein Processing, Post-Translational