Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Bacterial Proteins
Share to Enzyme Activation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Pseudomonas aeruginosa

Share to Serine Endopeptidases

Share to Substrate Specificity

Source

Identifiers

PMID: 1588815
DOI: 10.1111/j.1365-2958.1992.tb01554.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Further studies on Pseudomonas aeruginosa LasA: analysis of specificity.PMID 1588815Read ↗

lasA and lasB genes of Pseudomonas aeruginosa: analysis of transcription and gene product activity.Semantic proximity Read ↗

Secreted LasA of Pseudomonas aeruginosa is a staphylolytic protease.Semantic proximity Read ↗

Pseudomonas aeruginosa lasB1 mutants produce an elastase, substituted at active-site His-223, that is defective in activity, processing, and secretion.Semantic proximity Read ↗

A substitution at His-120 in the LasA protease of Pseudomonas aeruginosa blocks enzymatic activity without affecting propeptide processing or extracellular secretion.Semantic proximity Read ↗

Pseudomonas aeruginosa elastase provides an escape from phagocytosis by degrading the pulmonary surfactant protein-A.Semantic proximity Read ↗

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.Semantic proximity Read ↗

Pseudomonas aeruginosa possesses two putative type I signal peptidases, LepB and PA1303, each with distinct roles in physiology and virulence.Semantic proximity Read ↗

Quorum sensing-dependent post-secretional activation of extracellular proteases in Pseudomonas aeruginosa.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.