Substitution of active-site His-223 in Pseudomonas aeruginosa elastase and expression of the mutated lasB alleles in Escherichia coli show evidence for autoproteolytic processing of proelastase.

Abstract excerpt

The neutral metalloprotease elastase is one of the major proteins secreted into the culture medium by many Pseudomonas aeruginosa strains. Encoded by the lasB gene, the 33-kDa elastase is initially synthesized as a 53-kDa preproenzyme which is processed to the mature form via a 51-kDa proelastase intermediate. To facilitate studies on proteolytic processing of elastase precursors and on secretion, we developed...

Topics

• Alleles
• Base Sequence
• Binding Sites
• Cloning, Molecular
• DNA, Bacterial
• Enzyme Precursors
• Escherichia coli
• Gene Expression Regulation, Bacterial
• Histidine
• Immunoblotting