ArticleScientific reports2018
The crystal structure of monoacylglycerol lipase from M. tuberculosis reveals the basis for specific inhibition.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Prioritization of chemical scaffolds using the TDR Targets database: An integrative workflow for Trypanosoma cruzi drug discovery.PLoS neglected tropical diseases · 2026Article
- Plants lipases: challenges, recent advances, and future prospects - a review.Bioprocess and biosystems engineering · 2025Review
- Metabolite dynamics over the course of anti-tuberculosis treatment in individuals with mild and severe tuberculosis.PLOS global public health · 2025Article
- TheJournal of bacteriology · 2024Article
- A putative lipase affectsmSphere · 2023Article
- Feruloyl Esterase (International journal of molecular sciences · 2023Article
- Emerging mechanisms by which endocannabinoids and their derivatives modulate bacterial populations within the gut microbiome.Advances in drug and alcohol research · 2023Review
- Review
- Identification of cell wall synthesis inhibitors active against Mycobacterium tuberculosis by competitive activity-based protein profiling.Cell chemical biology · 2022Article
- Characterization of Polymer Degrading Lipases, LIP1 and LIP2 FromFrontiers in bioengineering and biotechnology · 2022Article
- Structural Changes in the Cap of Rv0183/mtbMGL Modulate the Shape of the Binding Pocket.Biomolecules · 2021Article
- Elucidating the Antimycobacterial Mechanism of Action of Ciprofloxacin Using Metabolomics.Microorganisms · 2021Article
- Structure and Dynamics of an Archeal Monoglyceride Lipase fromBiomolecules · 2021Article
- Anti-tubercular derivatives of rhein require activation by the monoglyceride lipase Rv0183.Cell surface (Amsterdam, Netherlands) · 2020Article
- Directed Evolution ofFrontiers in bioengineering and biotechnology · 2020Article
- A Thermostable Monoacylglycerol Lipase from MarineInternational journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Monoacylglycerol lipases (MGLs) are enzymes that hydrolyze monoacylglycerol into a free fatty acid and glycerol. Fatty acids can be used for triacylglycerol synthesis, as energy source, as building blocks for energy storage, and as precursor for membrane phospholipids. In Mycobacterium tuberculosis, fatty acids also serve as precursor for polyketide lipids like mycolic acids, major components of the cellular envelope associated to resistance for drug. We present the crystal structure of the MGL Rv0183 from Mycobacterium tuberculosis (mtbMGL) in open conformation. The structure reveals remarkable similarities with MGL from humans (hMGL) in both, the cap region and the α/β core. Nevertheless, mtbMGL could not be inhibited with JZL-184, a known inhibitor of hMGL. Docking studies provide an explanation why the activity of mtbMGL was not affected by the inhibitor. Our findings suggest that specific inhibition of mtbMGL from Mycobacterium tuberculosis, one of the oldest recognized pathogens, is possible without influencing hMGL.
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