ArticleBiological chemistry2013
The Staphylococcus aureus leucine aminopeptidase is localized to the bacterial cytosol and demonstrates a broad substrate range that extends beyond leucine.
Article in Biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Aminopeptidase M17 in bacteria: insights into structure, function, and potential as a drug target.Journal of bacteriology · 2026Review
- Chemical probes for enzyme imaging: challenges in design, synthesis and biomedical applications.Chemical science · 2025Review
- Real-time fluorescent monitoring of phase I xenobiotic-metabolizing enzymes.RSC advances · 2024Review
- Review
- Recent Progress of Activity-Based Fluorescent Probes for Imaging Leucine Aminopeptidase.Biosensors · 2023Review
- The identification of two M20B family peptidases required for full virulence inFrontiers in cellular and infection microbiology · 2023Article
- Using microbial metalo-aminopeptidases as targets in human infectious diseases.Microbial cell (Graz, Austria) · 2021Review
- Mapping the substrate specificity of the Plasmodium M1 and M17 aminopeptidases.The Biochemical journal · 2021Article
- An M29 Aminopeptidase fromMicroorganisms · 2020Article
- Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis.Scientific reports · 2017Article
- Leucine aminopeptidase may contribute to the intrinsic resistance of cancer cells toward cisplatin as revealed by an ultrasensitive fluorescent probe.Chemical science · 2016Article
- Investigating the genetic regulation of the ECF sigma factor σS in Staphylococcus aureus.BMC microbiology · 2014Article
- The lone S41 family C-terminal processing protease in Staphylococcus aureus is localized to the cell wall and contributes to virulence.Microbiology (Reading, England) · 2014Article
- Active site metals mediate an oligomeric equilibrium in Plasmodium M17 aminopeptidases.The Journal of biological chemistryArticle
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Staphylococcus aureus is a potent pathogen of humans exhibiting a broad disease range, in part due to an extensive repertoire of secreted virulence factors, including proteases. Recently, we identified the first example of an intracellular protease (leucine aminopeptidase, LAP) that is required for virulence in S. aureus. Disruption of pepZ, the gene encoding LAP, had no affect on the growth rate of bacteria; however, in systemic and localized infection models the pepZ mutant had significantly attenuated virulence. Recently, a contradictory report was published suggesting that LAP is an extracellular enzyme and it is required for growth in S. aureus. Here, we investigate these results and confirm our previous findings that LAP is localized to the bacterial cytosol and is not required for growth. In addition, we conduct a biochemical investigation of purified recombinant LAP, identifying optimal conditions for enzymatic activity and substrate preference for hydrolysis. Our results show that LAP has a broad substrate range, including activity against the dipeptide cysteine-glycine, and that leucine is not the primary target of LAP.
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