ArticleScientific reports2020
Demystifying the catalytic pathway of Mycobacterium tuberculosis isocitrate lyase.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Homology Modeling and Pharmacophore Based Inhibitor Design Targeting Isocitrate Lyase of Madurella mycetomatis-A Novel Approach Against Eumycetoma.Chemistry & biodiversity · 2026Article
- Physiological, genetical and morphological alterations in Mycobacterium avium subsp. paratuberculosis mutants generated with the CRISPRi system.BMC microbiology · 2026Article
- Functional analysis of the intracellular survival ofJournal of bacteriology · 2025Article
- Datasets comprising the quality validations of simulated protein-ligand complexes and SYBYL docking scores of bioactive natural compounds as inhibitors ofData in brief · 2022Article
- Discovery of a Novel Inhibitor Structure ofMolecules (Basel, Switzerland) · 2022Article
- Article
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pulmonary tuberculosis, caused by Mycobacterium tuberculosis, is one of the most persistent diseases leading to death in humans. As one of the key targets during the latent/dormant stage of M. tuberculosis, isocitrate lyase (ICL) has been a subject of interest for new tuberculosis therapeutics. In this work, the cleavage of the isocitrate by M. tuberculosis ICL was studied using quantum mechanics/molecular mechanics method at M06-2X/6-31+G(d,p): AMBER level of theory. The electronic embedding approach was applied to provide a better depiction of electrostatic interactions between MM and QM regions. Two possible pathways (pathway I that involves Asp108 and pathway II that involves Glu182) that could lead to the metabolism of isocitrate was studied in this study. The results suggested that the core residues involved in isocitrate catalytic cleavage mechanism are Asp108, Cys191 and Arg228. A water molecule bonded to Mg
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