The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa

Keyphrases

• Elastase 100%
• Pseudomonas Aeruginosa (P. aeruginosa) 100%
• Propeptide 100%
• Elastase Activity 100%
• Intramolecular Chaperone 100%
• Enzymatic Activity 21%
• LasB 15%
• Protease 10%
• Supernatant 10%
• Protein Activity 10%
• Direct Interaction 10%
• Co-precipitated 10%
• Chaperone-like 10%
• Culture Media 5%
• Escherichia Coli 5%
• Co-expression 5%
• Active Enzyme 5%
• Bacterial Membrane 5%
• Hydrolytic Activity 5%
• Zinc Metalloprotease 5%

Biochemistry, Genetics and Molecular Biology

• Secretion (Process) 100%
• Elastase 100%
• Pseudomonas aeruginosa 100%
• Enzyme Activity 22%
• Allele 11%
• Supernatant 11%
• Protease 11%
• Enzyme 5%
• Wild Type 5%
• Maturation 5%
• Escherichia coli 5%
• Precursor 5%
• Metalloproteinase 5%
• Hydrolase 5%
• Metalloendopeptidase 5%
• Bacterial Outer Membrane 5%