ArticleMolecular biology reports2014
Characterization of an acid inducible lipase Rv3203 from Mycobacterium tuberculosis H37Rv.
Article in Molecular biology reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers, 1 of them a synthesis that pooled it.
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Who cites it
9 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 citations in OpenAlex.
- Recombinant expression of insoluble enzymes in Escherichia coli: a systematic review of experimental design and its manufacturing implications.Microbial cell factories · 2021Pooled it
- Roles of Lipolytic enzymes inFrontiers in microbiology · 2024Review
- Article
- Rv0646c, an esterase from M. tuberculosis, up-regulates the host immune response in THP-1 macrophages cells.Molecular and cellular biochemistry · 2018Article
- Rv1288, a Two Domain, Cell Wall Anchored, Nutrient Stress Inducible Carboxyl-Esterase ofFrontiers in cellular and infection microbiology · 2018Article
- Cyclipostins and Cyclophostin analogs as promising compounds in the fight against tuberculosis.Scientific reports · 2017Article
- Effects of Lipid-Lowering Drugs on Vancomycin Susceptibility of Mycobacteria.Antimicrobial agents and chemotherapy · 2016Article
- Article
- Far-red fluorogenic probes for esterase and lipase detection.Chembiochem : a European journal of chemical biology · 2015Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Rv3203 (LipV) of Mycobacterium tuberculosis (Mtb) H37Rv, is annotated as a member of Lip family based on the presence of characteristic consensus esterase motif ‘GXSXG’. In vitro culture studies of Mtb H37Ra indicated that expression of Rv3203 gene was up-regulated during acidic stress as compared to normal whereas no expression was observed under nutrient and oxidative stress conditions. Therefore, detailed characterization of Rv3203 was done by gene cloning and its further expression and purification as his-tagged protein in microbial expression system. The enzyme was purified to homogeneity by affinity chromatography. It demonstrated broad substrate specificity and preferentially hydrolyzed p-nitrophenyl myristate. The purified enzyme demonstrated an optimum activity at pH 8.0 and temperature 50 °C. The specific activity, K m and V max of enzyme was determined to be 21.29 U mg(-1) protein, 714.28 μM and 62.5 μmol ml(-1) min(-1), respectively. The pH stability assay and circular dichroism spectroscopic analysis revealed that Rv3203 protein is more stable in acidic condition. Tetrahydrolipstatin, a specific lipase inhibitor and RHC80267, a diacylglycerol lipase inhibitor abolished the activity of this enzyme. The catalytic triad residues were determined to be Ser50, Asp180 and His203 residues by site-directed mutagenesis.
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