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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.)

The structure of a Trypanosoma cruzi glucose-6-phosphate dehydrogenase reveals differences from the mammalian enzyme

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Author(s):
Mercaldi, Gustavo F. ; Dawson, Alice ; Hunter, Willian N. ; Cordeiro, Artur T.
Total Authors: 4
Document type: Journal article
Source: FEBS Letters; v. 590, n. 16, p. 2776-2786, AUG 2016.
Web of Science Citations: 5
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 -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. (AU)

FAPESP's process: 13/03983-5 - Functional and structural studies of the enzymes related to the NADPH production in trypanosomatids
Grantee:Artur Torres Cordeiro
Support Opportunities: Regular Research Grants
FAPESP's process: 14/07533-7 - Biophysical studies of glucose-6-phosphate dehydrogenase inhibitors complexes
Grantee:Gustavo Fernando Mercaldi
Support Opportunities: Scholarships abroad - Research Internship - Doctorate