ArticleScientific reports2017
Distant Phe345 mutation compromises the stability and activity of Mycobacterium tuberculosis isocitrate lyase by modulating its structural flexibility.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 64 citations in OpenAlex.
- Exploring the molecular basis ofBioinformatics advances · 2026Article
- Computational studies on the functional and structural impact of pathogenic mutations in enzymes.Protein science : a publication of the Protein Society · 2025Review
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- Identification and characterization of cytosolic malate dehydrogenase from the liver fluke Fasciola gigantica.Scientific reports · 2020Article
- Recent Progress in the Understanding and Engineering of Coenzyme BFrontiers in bioengineering and biotechnology · 2020Review
- A novel mutation alters the stability of PapA2 resulting in the complete abrogation of sulfolipids in clinical mycobacterial strains.FASEB bioAdvances · 2019Article
- Identification and characterization of glyceraldehyde 3-phosphate dehydrogenase from Fasciola gigantica.Parasitology research · 2019Article
- Bacterial flagellar switching: a molecular mechanism directed by the logic of an electric motor.Journal of molecular modeling · 2018Article
- Comprehensive analysis of the catalytic and structural properties of a mu-class glutathione s-transferase from Fasciola gigantica.Scientific reports · 2017Article
- Exploring Leishmania secretory proteins to design B and T cell multi-epitope subunit vaccine using immunoinformatics approach.Scientific reports · 2017Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Isocitrate lyase (ICL), a potential anti-tubercular drug target, catalyzes the first step of the glyoxylate shunt. In the present investigation, we studied the conformational flexibility of MtbICL to better understand its stability and catalytic activity. Our biochemical results showed that a point mutation at Phe345, which is topologically distant (>10 Å) to the active site signature sequence (
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