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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Understanding the Structure, Activity and Inhibition of Chorismate Synthase from Mycobacterium tuberculosis

Author(s):
Arcuri, H. A. [1, 2] ; Palma, M. S. [1, 3]
Total Authors: 2
Affiliation:
[1] Sao Paulo State Univ UNESP, CEIS, Dept Biol, Inst Biosci Rio Claro, BR-13506900 Rio Claro, SP - Brazil
[2] HC FMUSP, INCor, Discipline Allergy & Immunol, Sao Paulo - Brazil
[3] Natl Inst Sci & Technol Immunol INCT III, Alegre, RS - Brazil
Total Affiliations: 3
Document type: Review article
Source: Current Medicinal Chemistry; v. 18, n. 9, p. 1311-1317, MAR 2011.
Web of Science Citations: 7
Abstract

Tuberculosis is considered a worldwide health problem mainly due to co-infection with HIV and proliferation of multi-drug-resistant 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. (AU)

FAPESP's process: 06/57122-7 - Searching for lead compounds for rational development of new drugs and pesticides through bioprospecting in Brazilian arthropods
Grantee:Mario Sergio Palma
Support type: BIOTA-FAPESP Program - Thematic Grants