Article
Further studies on Pseudomonas aeruginosa LasA: analysis of specificity.
Molecular microbiology - 1 May 1992
Peters J E, Park S J, Darzins A, Freck L C, Saulnier J M, Wallach J M, Galloway D R
Abstract excerpt
Full elastolytic activity in Pseudomonas aeruginosa is a result of the combined activities of elastase, alkaline proteinase, and the lasA gene product, LasA. The results of this study demonstrate that an active fragment of the LasA protein which is isolated from the culture supernatant fraction is capable of degrading elastin in the absence of elastase, thus showing that LasA is a second elastase produced by this...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Caseins
- Elastin
- Enzyme Activation
- Metalloendopeptidases
- Molecular Sequence Data
- Mutation
- Pancreatic Elastase
- Pseudomonas aeruginosa
- Serine Endopeptidases