ArticleThe Journal of biological chemistry2013
Substrate specificity of MarP, a periplasmic protease required for resistance to acid and oxidative stress in Mycobacterium tuberculosis.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- An unusual genetic switch controlsbioRxiv : the preprint server for biology · 2025Article
- Enhancing schistosomiasis drug discovery approaches with optimized proteasome substrates.Protein science : a publication of the Protein Society · 2025Article
- Multiplex substrate profiling by mass spectrometry for proteases.Methods in enzymology · 2023Article
- Novel inhibitors and activity-based probes targeting serine proteases.Frontiers in chemistry · 2022Article
- Expression of recombinant protease MarP from Mycobacterium tuberculosis in Pichia pastoris and its effect on human monocytes.Biotechnology letters · 2021Article
- AC2P20 selectively killsRSC advances · 2021Article
- Mycobacterium tuberculosis infection of host cells in space and time.FEMS microbiology reviews · 2019Review
- The Cell Wall Hydrolytic NlpC/P60 Endopeptidases in Mycobacterial Cytokinesis: A Structural Perspective.Cells · 2019Review
- Identification of Compounds with pH-Dependent Bactericidal Activity against Mycobacterium tuberculosis.ACS infectious diseases · 2019Article
- PhoPR Positively RegulatesJournal of bacteriology · 2018Article
- Global Protease Activity Profiling Provides Differential Diagnosis of Pancreatic Cysts.Clinical cancer research : an official journal of the American Association for Cancer Research · 2017Article
- Article
- Integrated Activity and Genetic Profiling of Secreted Peptidases in Cryptococcus neoformans Reveals an Aspartyl Peptidase Required for Low pH Survival and Virulence.PLoS pathogens · 2016Article
- Design of Selective Substrates and Activity-Based Probes for Hydrolase Important for Pathogenesis 1 (HIP1) from Mycobacterium tuberculosis.ACS infectious diseases · 2016Article
- Magnetite Biomineralization in Magnetospirillum magneticum Is Regulated by a Switch-like Behavior in the HtrA Protease MamE.The Journal of biological chemistry · 2016Article
- Mycobacterial Acid Tolerance Enables Phagolysosomal Survival and Establishment of Tuberculous Infection In Vivo.Cell host & microbe · 2016Article
- Excretion/secretion products from Schistosoma mansoni adults, eggs and schistosomula have unique peptidase specificity profiles.Biochimie · 2016Article
- Systematic Survey of Serine Hydrolase Activity in Mycobacterium tuberculosis Defines Changes Associated with Persistence.Cell chemical biology · 2016Article
- A Mycobacterium avium subsp. paratuberculosis Predicted Serine Protease Is Associated with Acid Stress and Intraphagosomal Survival.Frontiers in cellular and infection microbiology · 2016Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
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 recombinant protease domain of MarP, we identified its substrate specificity using two independent assays: positional-scanning synthetic combinatorial library profiling and multiplex substrate profiling by mass spectrometry. These methods revealed that MarP prefers bulky residues at P4, tryptophan or leucine at P2, arginine or hydrophobic residues at P1, and alanine or asparagine at P1'. Guided by these data, we designed fluorogenic peptide substrates and characterized the kinetic properties of MarP. Finally, we tested the impact of mutating MarP cysteine residues on the peptidolytic activity of recombinant MarP and its ability to complement phenotypes of Mtb ΔMarP. Taken together, our studies provide insight into the enzymatic properties of MarP, its substrate preference, and the importance of its transmembrane helices and disulfide bond.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.