Abstract
The causative agent of tuberculosis (TB), Mycobacterium tuberculosis, infects one-third of the world population. TB remains the leading cause of mortality due to a single bacterial pathogen. The worldwide increase in incidence of M. tuberculosis has been attributed to the high proliferation rates of multi and extensively drug-resistant strains, and to co-infection with the human immunodeficiency virus. There is thus a continuous requirement for studies on mycobacterial metabolism to identify promising targets for the development of new agents to combat TB. Singular characteristics of this pathogen, such as functional and structural features of enzymes involved in fundamental metabolic pathways, can be evaluated to identify possible targets for drug development. Enzymes involved in the pyrimidine salvage pathway might be attractive targets for rational drug design against TB, since this pathway is vital for all bacterial cells, and is composed of enzymes considerably different from those present in humans. Moreover, the enzymes of the pyrimidine salvage pathway might have an important role in the mycobacterial latent state, since M. tuberculosis has to recycle bases and/or nucleosides to survive in the hostile environment imposed by the host. The present review describes the enzymes of M. tuberculosis pyrimidine salvage pathway as attractive targets for the development of new antimycobacterial agents. Enzyme functional and structural data have been included to provide a broader knowledge on which to base the search for compounds with selective biological activity.
Keywords: Enzyme functional features, enzyme structural features, Mycobacterium tuberculosis, pyrimidine salvage pathway, rational drug design, tuberculosis, BCG vaccination, drug resistance, HIV, macrophages
Current Medicinal Chemistry
Title: Pyrimidine Salvage Pathway in Mycobacterium tuberculosis
Volume: 18 Issue: 9
Author(s): A. D. Villela, Z. A. Sanchez-Quitian, R. G. Ducati, D. S. Santos and L. A. Basso
Affiliation:
Keywords: Enzyme functional features, enzyme structural features, Mycobacterium tuberculosis, pyrimidine salvage pathway, rational drug design, tuberculosis, BCG vaccination, drug resistance, HIV, macrophages
Abstract: The causative agent of tuberculosis (TB), Mycobacterium tuberculosis, infects one-third of the world population. TB remains the leading cause of mortality due to a single bacterial pathogen. The worldwide increase in incidence of M. tuberculosis has been attributed to the high proliferation rates of multi and extensively drug-resistant strains, and to co-infection with the human immunodeficiency virus. There is thus a continuous requirement for studies on mycobacterial metabolism to identify promising targets for the development of new agents to combat TB. Singular characteristics of this pathogen, such as functional and structural features of enzymes involved in fundamental metabolic pathways, can be evaluated to identify possible targets for drug development. Enzymes involved in the pyrimidine salvage pathway might be attractive targets for rational drug design against TB, since this pathway is vital for all bacterial cells, and is composed of enzymes considerably different from those present in humans. Moreover, the enzymes of the pyrimidine salvage pathway might have an important role in the mycobacterial latent state, since M. tuberculosis has to recycle bases and/or nucleosides to survive in the hostile environment imposed by the host. The present review describes the enzymes of M. tuberculosis pyrimidine salvage pathway as attractive targets for the development of new antimycobacterial agents. Enzyme functional and structural data have been included to provide a broader knowledge on which to base the search for compounds with selective biological activity.
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Cite this article as:
D. Villela A., A. Sanchez-Quitian Z., G. Ducati R., S. Santos D. and A. Basso L., Pyrimidine Salvage Pathway in Mycobacterium tuberculosis, Current Medicinal Chemistry 2011; 18 (9) . https://dx.doi.org/10.2174/092986711795029555
DOI https://dx.doi.org/10.2174/092986711795029555 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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