Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
Mycobacterium tuberculosis enolase is an essential glycolytic enzyme that catalyzes the conversion of 2, phosphoglycerate (PGA) to phosphoenol pyruvate (PEP). It is also a crucial link between glycolysis and the tricarboxylic acid (TCA) pathway. The depletion of PEP has recently been associated with the emergence of non-replicating drug resistant bacteria. Enolase is also known to exhibit multiple alternate functions, such as promoting tissue invasion via its role as a plasminogen (Plg) receptor. In addition, proteomic studies have identified the presence of enolase in the Mtb degradosome and in biofilms. However, the precise role in these processes has not been elaborated. The enzyme was recently identified as a target for 2-amino thiazoles - a novel class of anti-mycobacterials. In vitro assays and characterization of this enzyme were unsuccessful due to the inability to obtain functional recombinant protein. In the present study, we report the expression and characterization of enolase using Mtb H37Ra as a host strain. Our study demonstrates that the enzyme activity and alternate functions of this protein are significantly impacted by the choice of expression host (Mtb H37Ra or E. coli). Detailed analysis of the protein from each source revealed subtle differences in the post-translational modifications. Lastly, our study confirms the role of enolase in Mtb biofilm formation and describes the potential for inhibiting this process.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.biochi.2023.06.012 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Transcriptomic and proteomic analyses of strains isolated from tuberculous meningitis patients.
Int J Mycobacteriol
December 2023
Department of Microbiology, Jawaharlal Institute of Postgraduate Medical Education and Research, Puducherry, India.
Background: Tuberculous meningitis (TBM) is caused by the dissemination of Mycobacterium tuberculosis (MTB) from the primary site of infection to the central nervous system. However, the bacterial factors associated with the pathogenesis of TBM remain unclear. This study employed transcriptomic and proteomic methods to comprehensively analyze the changes in genes and proteins and their associated pathways in MTB strains isolated from cerebrospinal fluid (CSF) of TBM and sputum of pulmonary TB (PTB) cases.
View Article and Find Full Text PDFStructural snapshots of Mycobacterium tuberculosis enolase reveal dual mode of 2PG binding and its implication in enzyme catalysis.
IUCrJ
November 2023
Structural and Functional Biology Laboratory, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067, India.
Article Synopsis
- - Enolase is an enzyme that helps convert 2-phosphoglycerate (2PG) to phosphoenolpyruvate (PEP) in glycolysis, but the reverse reaction (PEP to 2PG) hasn't been fully understood until now.
- - This research provides structural insights into Mycobacterium tuberculosis enolase, revealing how 2PG can exist in both a common and an alternate conformation during the conversion process.
- - Key findings suggest that, unlike in the forward reaction, magnesium is not essential for the reverse reaction, and the alternate conformation of 2PG enhances its release from the enzyme's active site, indicating a new mechanism for this conversion.
Mycobacterium tuberculosis H37Rv enolase (Rv1023)- expression, characterization and effect of host dependent modifications on protein functionality.
Biochimie
November 2023
Department of Biotechnology National Institute of Pharmaceutical Education and Research (NIPER), Phase X, Sector 67, SAS Nagar, Punjab, 160062, India. Electronic address:
Mycobacterium tuberculosis enolase is an essential glycolytic enzyme that catalyzes the conversion of 2, phosphoglycerate (PGA) to phosphoenol pyruvate (PEP). It is also a crucial link between glycolysis and the tricarboxylic acid (TCA) pathway. The depletion of PEP has recently been associated with the emergence of non-replicating drug resistant bacteria.
View Article and Find Full Text PDFCost-effectiveness analysis of multimodal prognostication in cardiac arrest with EEG monitoring.
Neurology
August 2020
From Harvard Medical School (E.A., S.S.M., S.S.C., M.T.B., M.B.W.); Department of Neurology (E.A., S.S.C., M.T.B., M.B.W.), Massachusetts General Hospital, Boston; Department of Neurology (E.A.), University of California, San Francisco; and Computer Science and Artificial Intelligence Laboratory (E.
Objective: To determine cost-effectiveness parameters for EEG monitoring in cardiac arrest prognostication.
Methods: We conducted a cost-effectiveness analysis to estimate the cost per quality-adjusted life-year (QALY) gained by adding continuous EEG monitoring to standard cardiac arrest prognostication using the American Academy of Neurology Practice Parameter (AANPP) decision algorithm: neurologic examination, somatosensory evoked potentials, and neuron-specific enolase. We explored lifetime cost-effectiveness in a closed system that incorporates revenue back into the medical system (return) from payers who survive a cardiac arrest with good outcome and contribute to the health system during the remaining years of life.
Exploring the interaction between Mycobacterium tuberculosis enolase and human plasminogen using computational methods and experimental techniques.
J Cell Biochem
February 2018
Laboratory of Molecular Biology and Genetic Engineering, School of Biotechnology, Jawaharlal Nehru University, New Delhi, India.
Surface localized microbial enolases' binding with human plasminogen has been increasingly proven to have an important role in initial infection cycle of several human pathogens. Likewise, surface localized Mycobacterium tuberculosis (Mtb) enolase also binds to human plasminogen, and this interaction may entail crucial consequences for granuloma stability. The current study is the first attempt to explore the plasminogen interacting residues of enolase from Mtb.
View Article and Find Full Text PDF