ArticleThe Journal of biological chemistry2014
Mycobacterium tuberculosis phosphoenolpyruvate carboxykinase is regulated by redox mechanisms and interaction with thioredoxin.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 39 citations in OpenAlex.
- H-NOX and NosP Regulate Flagellar Protein and Virulence Factor Production in Vibrio Cholerae.Molecular & cellular proteomics : MCP · 2026Article
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- Mycobacterium tuberculosis curli pili facilitates pathogenicity by modulating central carbon metabolism.Metabolomics : Official journal of the Metabolomic Society · 2025Article
- Lineage-specific energy and carbon metabolism of sponge symbionts and contributions to the host carbon pool.The ISME journal · 2022Article
- Central carbon metabolism remodeling as a mechanism to develop drug tolerance and drug resistance inFrontiers in cellular and infection microbiology · 2022Review
- Phosphoenolpyruvate depletion mediates both growth arrest and drug tolerance ofProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Phosphofructokinases A and B fromInternational journal of molecular sciences · 2021Article
- Bedaquiline reprograms central metabolism to reveal glycolytic vulnerability in Mycobacterium tuberculosis.Nature communications · 2020Article
- Metabolic principles of persistence and pathogenicity in Mycobacterium tuberculosis.Nature reviews. Microbiology · 2018Review
- Understanding the role of interactions between host and Mycobacterium tuberculosis under hypoxic condition: an in silico approach.BMC genomics · 2018Article
- The anaplerotic node is essential for the intracellular survival ofThe Journal of biological chemistry · 2018Article
- Metabolic Perspectives on Persistence.Microbiology spectrum · 2017Review
- EthA/R-Independent Killing ofFrontiers in microbiology · 2017Article
- The Role of Cysteine Residues in Catalysis of Phosphoenolpyruvate Carboxykinase from Mycobacterium tuberculosis.PloS one · 2017Article
- Mycobacterium tuberculosis has diminished capacity to counteract redox stress induced by elevated levels of endogenous superoxide.Free radical biology & medicine · 2015Article
- Structural and functional studies of phosphoenolpyruvate carboxykinase from Mycobacterium tuberculosis.PloS one · 2015Article
Corrections and comments
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Authors and funding
10 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tuberculosis remains a major health concern worldwide. Eradication of its causative agent, the bacterial pathogen Mycobacterium tuberculosis, is particularly challenging due to a vast reservoir of latent carriers of the disease. Despite the misleading terminology of a so-called dormant state associated with latent infections, the bacteria have to maintain basic metabolic activities. Hypoxic conditions have been widely used as an in vitro system to study this dormancy. Such studies identified a rearrangement of central carbon metabolism to exploit fermentative processes caused by the lack of oxygen. Phosphoenolpyruvate carboxykinase (Pck; EC 4.1.1.32) is the enzyme at the center of these metabolic rearrangements. Although Pck is associated with gluconeogenesis under standard growth conditions, the enzyme can catalyze the reverse reaction, supporting anaplerosis of the tricarboxylic acid cycle, under conditions leading to slowed or stopped bacterial replication. To study the mechanisms that regulate the switch between two Pck functions, we systematically investigated factors influencing the gluconeogenic and anaplerotic reaction kinetics. We demonstrate that a reducing environment, as found under hypoxia-triggered non-replicating conditions, accelerates the reaction in the anaplerotic direction. Furthermore, we identified proteins that interact with Pck. The interaction between Pck and the reduced form of mycobacterial thioredoxin, gene expression of which is increased under hypoxic conditions, also increased the Pck anaplerotic activity. We thus propose that a reducing environment and the protein-protein interaction with thioredoxin in particular enable the Pck anaplerotic function under fermentative growth conditions.
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