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

Extracellular production of active vibriolysin engineered by random mutagenesis in Escherichia coli.

Protein expression and purification - 1 Dec 2008

Sonoda Hiroyuki, Sugimura Atsushi

Abstract excerpt

Vibriolysin, an extracellular protease of Vibrio proteolyticus, is synthesized as a preproenzyme. The N-terminal propeptide functions as an intramolecular chaperone and an inhibitor of the mature enzyme. Extracellular production of recombinant vibriolysin has been achieved in Bacillus subtilis, but not in Escherichia coli, which is widely used as a host for the production of recombinant proteins. Vibriolysin is...

Read the complete abstract on PubMed

Topics

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

Share to Culture Media
Share to Enzyme Activation
Share to Extracellular Space

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Metalloendopeptidases

Share to Peptides

Share to Protein Engineering

Share to Protein Processing, Post-Translational

Share to Vibrio

Source

Identifiers

PMID: 18768160
DOI: 10.1016/j.pep.2008.08.001

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Extracellular production of active vibriolysin engineered by random mutagenesis in Escherichia coli.PMID 18768160Read ↗

Characterization of the glutamyl endopeptidase from Staphylococcus aureus expressed in Escherichia coli.Semantic proximity Read ↗

Improvement of extracellular production of a thermophilic subtilase expressed in Escherichia coli by random mutagenesis of its N-terminal propeptide.Semantic proximity Read ↗

Heterologous production of active form of beta-lytic protease by Bacillus subtilis and improvement of staphylolytic activity by protein engineering.Semantic proximity Read ↗

Molecular cloning of the gene encoding Vibrio metalloproteinase vimelysin and isolation of a mutant with high stability in organic solvents.Semantic proximity Read ↗

Intramembrane proteolytic cleavage of a membrane-tethered transcription factor by a metalloprotease depends on ATP.Semantic proximity Read ↗

Requirement for the COOH-terminal pro-sequence in the translocation of aqualysin I across the cytoplasmic membrane in Escherichia coli.Semantic proximity Read ↗

Over‐expression, secretion, biochemical characterisation, and structure analysis of Bacillus subtilis aminopeptidaseSemantic proximity Read ↗

Removal of N-terminal methionine from recombinant proteins by engineered E. coli methionine aminopeptidase.Semantic proximity Read ↗

A de novo designed signal peptide cleavage cassette functions in vivo.Semantic proximity Read ↗

Structure and protective efficacy of the Staphylococcus aureus autocleaving protease EpiP.Semantic proximity Read ↗

Selection of Streptomyces griseus protease B mutants with desired alterations in primary specificity using a library screening strategy.Semantic proximity Read ↗

Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants.Semantic proximity Read ↗

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