Abstract
Tuberculosis is considered a worldwide health problem mainly due to co-infection with HIV and proliferation of multi-drugresistant strains. The enzymes of the shikimate pathway are potential targets for the development of new therapies because they are essential for bacteria, but absent from mammals. The last step in this pathway is performed by chorismate synthase (CS), which catalyzes the conversion of 5-enolpyruvylshikimate-3-phosphate (EPSP) to chorismate. The aim of this article is to review the available information on chorismate synthase from Mycobacterium tuberculosis.
Keywords: Chorismate synthase, Mycobacterium tuberculosis, shikimate pathway, inhibition, HIV, Genetic products, antiretroviral agents, polypeptide, bacteria, antimycobacterial agents
Current Medicinal Chemistry
Title: Understanding the Structure, Activity and Inhibition of Chorismate Synthase from Mycobacterium tuberculosis
Volume: 18 Issue: 9
Author(s): H. A. Arcuri and M. S. Palma
Affiliation:
Keywords: Chorismate synthase, Mycobacterium tuberculosis, shikimate pathway, inhibition, HIV, Genetic products, antiretroviral agents, polypeptide, bacteria, antimycobacterial agents
Abstract: Tuberculosis is considered a worldwide health problem mainly due to co-infection with HIV and proliferation of multi-drugresistant strains. The enzymes of the shikimate pathway are potential targets for the development of new therapies because they are essential for bacteria, but absent from mammals. The last step in this pathway is performed by chorismate synthase (CS), which catalyzes the conversion of 5-enolpyruvylshikimate-3-phosphate (EPSP) to chorismate. The aim of this article is to review the available information on chorismate synthase from Mycobacterium tuberculosis.
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Cite this article as:
A. Arcuri H. and S. Palma M., Understanding the Structure, Activity and Inhibition of Chorismate Synthase from Mycobacterium tuberculosis, Current Medicinal Chemistry 2011; 18 (9) . https://dx.doi.org/10.2174/092986711795029528
DOI https://dx.doi.org/10.2174/092986711795029528 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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