ArticleThe Journal of biological chemistry2010
Tetrahydrolipstatin inhibition, functional analyses, and three-dimensional structure of a lipase essential for mycobacterial viability.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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Who cites it
17 citing papers in PubMed, 36 citations in OpenAlex.
- Article
- Disulfide bonds are required for cell division, cell envelope biogenesis and antibiotic resistance proteins in mycobacteria.bioRxiv : the preprint server for biology · 2025Article
- Article
- Roles of Lipolytic enzymes inFrontiers in microbiology · 2024Review
- Biochemical and microbiological evaluation ofMedChemComm · 2019Article
- Microbial esterases and ester prodrugs: An unlikely marriage for combating antibiotic resistance.Drug development research · 2019Review
- Characterization of Tetrahydrolipstatin and Stereoderivatives on the Inhibition of Essential Mycobacterium tuberculosis Lipid Esterases.Biochemistry · 2018Article
- Structural basis for lipid binding and mechanism of theThe Journal of biological chemistry · 2018Article
- Structural Basis for the Strict Substrate Selectivity of the Mycobacterial Hydrolase LipW.Biochemistry · 2016Article
- Effects of Lipid-Lowering Drugs on Vancomycin Susceptibility of Mycobacteria.Antimicrobial agents and chemotherapy · 2016Article
- Bacterial Sphingomyelinases and Phospholipases as Virulence Factors.Microbiology and molecular biology reviews : MMBR · 2016Review
- Systematic Survey of Serine Hydrolase Activity in Mycobacterium tuberculosis Defines Changes Associated with Persistence.Cell chemical biology · 2016Article
- Adherence and invasive properties of Corynebacterium diphtheriae strains correlates with the predicted membrane-associated and secreted proteome.BMC genomics · 2015Article
- Article
- Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis.The Journal of biological chemistry · 2012Article
- Article
- Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The highly complex and unique mycobacterial cell wall is critical to the survival of Mycobacteria in host cells. However, the biosynthetic pathways responsible for its synthesis are, in general, incompletely characterized. Rv3802c from Mycobacterium tuberculosis is a partially characterized phospholipase/thioesterase encoded within a genetic cluster dedicated to the synthesis of core structures of the mycobacterial cell wall, including mycolic acids and arabinogalactan. Enzymatic assays performed with purified recombinant proteins Rv3802c and its close homologs from Mycobacterium smegmatis (MSMEG_6394) and Corynebacterium glutamicum (NCgl2775) show that they all have significant lipase activities that are inhibited by tetrahydrolipstatin, an anti-obesity drug that coincidently inhibits mycobacterial cell wall biosynthesis. The crystal structure of MSMEG_6394, solved to 2.9 Å resolution, revealed an α/β hydrolase fold and a catalytic triad typically present in esterases and lipases. Furthermore, we demonstrate direct evidence of gene essentiality in M. smegmatis and show the structural consequences of loss of MSMEG_6394 function on the cellular integrity of the organism. These findings, combined with the predicted essentiality of Rv3802c in M. tuberculosis, indicate that the Rv3802c family performs a fundamental and indispensable lipase-associated function in mycobacteria.
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