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

Substrate specificity of MarP, a periplasmic protease required for resistance to acid and oxidative stress in Mycobacterium tuberculosis.

The Journal of biological chemistry - 3 May 2013

Small Jennifer L, O'Donoghue Anthony J, Boritsch Eva C, Tsodikov Oleg V, Knudsen Giselle M, Vandal Omar, Craik Charles S, Ehrt Sabine

Abstract excerpt

The transmembrane serine protease MarP is important for pH homeostasis in Mycobacterium tuberculosis (Mtb). Previous structural studies revealed that MarP contains a chymotrypsin fold and a disulfide bond that stabilizes the protease active site in the substrate-bound conformation. Here, we determined that MarP is located in the Mtb periplasm and showed that this localization is essential for function. Using the...

Read the complete abstract on PubMed

Topics

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

Share to Hydrogen-Ion Concentration
Share to Mycobacterium tuberculosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxidative Stress

Share to Peptide Hydrolases

Share to Periplasmic Proteins

Share to Protein Folding

Share to Protein Structure, Secondary

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 23504313
DOI: 10.1074/jbc.M113.456541
PMCID: PMC3642297

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

Substrate specificity of MarP, a periplasmic protease required for resistance to acid and oxidative stress in Mycobacterium tuberculosis.PMID 23504313Read ↗

Mutations of key substrate binding residues of leishmanial peptidase T alter its functional and structural dynamics.Semantic proximity Read ↗

Structural insight into serine protease Rv3671c that Protects M. tuberculosis from oxidative and acidic stress.Semantic proximity Read ↗

Structural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity.Semantic proximity Read ↗

<i>mspms</i> : A Comprehensive R Package and Graphic Interface for Multiplex Substrate Profiling by Mass Spectrometry AnalysisSemantic proximity Read ↗

Comprehensive exploration of the translocation, stability and substrate recognition requirements in VIM-2 lactamaseSemantic proximity Read ↗

Comprehensive exploration of the translocation, stability and substrate recognition requirements in VIM-2 lactamase.Semantic proximity Read ↗

Antibacterial Activity of and Resistance to Small Molecule Inhibitors of the ClpP PeptidaseSemantic proximity Read ↗

Targeted protein degradation in mycobacteria uncovers antibacterial effects and potentiates antibiotic efficacySemantic proximity Read ↗

Toxin-based screening of C-terminal tags in <i>Escherichia coli</i> reveals the exceptional potency of ssrA-like degronsSemantic proximity Read ↗

Mycobacterium tuberculosis Rv0198c, a putative matrix metalloprotease is involved in pathogenicity.Semantic proximity Read ↗

The structural basis for catalysis and substrate specificity of a rhomboid protease.Semantic proximity Read ↗

Distinct specificities of Mycobacterium tuberculosis and mammalian proteasomes for N-acetyl tripeptide substrates.Semantic proximity Read ↗

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