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

Oxidized and Met358-->Leu mutated alpha 1-proteinase inhibitor as substrates of Pseudomonas aeruginosa elastase.

Biochimica et biophysica acta - 21 Apr 1993

Padrines M, Bieth J G

Abstract excerpt

This paper investigates the catalytic activity of Pseudomonas aeruginosa elastase using the bait region of the alpha 1-proteinase inhibitor as a substrate. The bacterial enzyme cleaves the Pro357-Met358 bond of the wild-type inhibitor and the recombinant Met358 inhibitor and the Pro357-Leu358 bon...

Topics

Amino Acid Sequence
Hydrogen-Ion Concentration
Kinetics
Leucine
Methionine
Molecular Sequence Data
Mutation
Oxidation-Reduction
Pancreatic Elastase
Protease Inhibitors
Pseudomonas aeruginosa
Recombinant Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Substrate Specificity

Source

Identifiers

PMID: 8476930
DOI: 10.1016/0167-4838(93)90279-z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8476930-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Oxidized and Met358-->Leu mutated alpha 1-proteinase inhibitor as substrates of Pseudomonas aeruginosa elastase.PMID 8476930Read ↗

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

Human pre-elafin inhibits a Pseudomonas aeruginosa-secreted peptidase and prevents its proliferation in complex media.Semantic proximity Read ↗

The streptococcal lipoprotein rotamase A (SlrA) is a functional peptidyl-prolyl isomerase involved in pneumococcal colonization.Semantic proximity Read ↗

Substrate Recognition Properties of Oligopeptidase B fromSalmonella entericaSerovar TyphimuriumSemantic proximity Read ↗

Structure-function relationship of type-IV prepilin peptidase of Pseudomonas aeruginosa--a review.Semantic proximity Read ↗

The BapF protein from Pseudomonas aeruginosa is a β-peptidyl aminopeptidaseSemantic proximity Read ↗

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

Converting trypsin to elastase: substitution of the S1 site and adjacent loops reconstitutes esterase specificity but not amidase activity.Semantic proximity Read ↗

Alkaline proteinase inhibitor of Pseudomonas aeruginosa: a mutational and molecular dynamics study of the role of N-terminal residues in the inhibition of Pseudomonas alkaline proteinase.Semantic proximity Read ↗

Inhibitory characteristics and oxidant resistance of site specific variants of recombinant human antileukoproteinase (ALP).Semantic proximity Read ↗

Mutation of active site serine residue with cysteine displays change in acyl-acceptor preference of β-peptidyl aminopeptidase from Pseudomonas aeruginosa PAO1.Semantic proximity Read ↗

Alteration of inhibitory properties of Pleurotus ostreatus proteinase A inhibitor 1 by mutation of its C-terminal region.Semantic proximity Read ↗

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