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

Prevention of C-terminal autoprocessing of Lactococcus lactis SK11 cell-envelope proteinase by engineering of an essential surface loop.

The Biochemical journal - 15 Sept 1994

Bruinenberg P G, de Vos W M, Siezen R J

Abstract excerpt

The catalytic domain of the cell-envelope proteinase from Lactococcus lactis SK11 has various inserts, situated in external loops of the catalytic domain, compared with the related subtilisins. Protein engineering was employed to analyse the necessity and function of one of these extra loops (residues 205-219), that is predicted to be located in close proximity to the substrate-binding region and is susceptible...

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

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

Share to Base Sequence

Share to Cell Membrane

Share to Cloning, Molecular

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 7945226
DOI: 10.1042/bj3020957
PMCID: PMC1137323

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 · 12 closest

Prevention of C-terminal autoprocessing of Lactococcus lactis SK11 cell-envelope proteinase by engineering of an essential surface loop.PMID 7945226Read ↗

Multiple-peptidase mutants of Lactococcus lactis are severely impaired in their ability to grow in milk.Semantic proximity Read ↗

Reconstruction of the proteolytic pathway for use of beta-casein by Lactococcus lactis.Semantic proximity Read ↗

Structural and functional characterization of SplA, an exclusively specific protease of <i>Staphylococcus aureus</i>Semantic proximity Read ↗

Genetics of peptide degradation in Lactococcus: gene cloning, construction and analysis of peptidase negative mutants.Semantic proximity Read ↗

Improved autoprocessing efficiency of mutant subtilisins E with altered specificity by engineering of the pro-region.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 ↗

Identification of critical residues in the propeptide of LasA protease of Pseudomonas aeruginosa involved in the formation of a stable mature protease.Semantic proximity Read ↗

Crystal structure of the lytic CHAP(K) domain of the endolysin LysK from Staphylococcus aureus bacteriophage K.Semantic proximity Read ↗

Diversity of cell envelope proteinase specificity among strains of Lactococcus lactis and its relationship to charge characteristics of the substrate-binding region.Semantic proximity Read ↗

Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217.Semantic proximity Read ↗

Substitution of cysteine 192 in a highly conserved Streptococcus pyogenes extracellular cysteine protease (interleukin 1beta convertase) alters proteolytic activity and ablates zymogen processing.Semantic proximity Read ↗

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