The structure of a Trypanosoma cruzi glucose-6-phosphate dehydrogenase reveals differences from the mammalian enzyme.
FEBS Lett
; 590(16): 2776-86, 2016 08.
Article
em En
| MEDLINE
| ID: mdl-27391210
ABSTRACT
The enzyme glucose-6-phosphate dehydrogenase from Trypanosoma cruzi (TcG6PDH) catalyses the first step of the pentose phosphate pathway (PPP) and is considered a promising target for the discovery of a new drug against Chagas diseases. In the present work, we describe the crystal structure of TcG6PDH obtained in a ternary complex with the substrate ß-d-glucose-6-phosphate (G6P) and the reduced 'catalytic' cofactor NADPH, which reveals the molecular basis of substrate and cofactor recognition. A comparison with the homologous human protein sheds light on differences in the cofactor-binding site that might be explored towards the design of new NADP(+) competitive inhibitors targeting the parasite enzyme.
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Base de dados:
MEDLINE
Assunto principal:
Conformação Proteica
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Trypanosoma cruzi
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Doença de Chagas
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Coenzimas
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Glucosefosfato Desidrogenase
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article