Targeting the histidine pathway in Mycobacterium tuberculosis.
Curr Top Med Chem
; 13(22): 2866-84, 2013.
Article
em En
| MEDLINE
| ID: mdl-24111909
Worldwide, tuberculosis is the leading cause of morbidity and mortality due to a single bacterial pathogen, Mycobacterium tuberculosis (Mtb). The increasing prevalence of this disease, the emergence of multi-, extensively, and totally drug-resistant strains, complicated by co-infection with the human immunodeficiency virus, and the length of tuberculosis chemotherapy have led to an urgent and continued need for the development of new and more effective antitubercular drugs. Within this context, the L-histidine biosynthetic pathway, which converts 5-phosphoribosyl 1-pyrophosphate to L-histidine in ten enzymatic steps, has been reported as a promising target of antimicrobial agents. This pathway is found in bacteria, archaebacteria, lower eukaryotes, and plants but is absent in mammals, making these enzymes highly attractive targets for the drug design of new antimycobacterial compounds with selective toxicity. Moreover, the biosynthesis of L-histidine has been described as essential for Mtb growth in vitro. Accordingly, a comprehensive overview of Mycobacterium tuberculosis histidine pathway enzymes as attractive targets for the development of new antimycobacterial agents is provided, mainly summarizing the previously reported inhibition data for Mtb or orthologous proteins.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Enzimas
/
Histidina
/
Mycobacterium tuberculosis
/
Antituberculosos
Tipo de estudo:
Risk_factors_studies
Idioma:
En
Revista:
Curr Top Med Chem
Assunto da revista:
QUIMICA
Ano de publicação:
2013
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Emirados Árabes Unidos