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 β-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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Mercaldi GF,Dawson A,Hunter WN,Cordeiro ATdoi
10.1002/1873-3468.12276subject
Has Abstractpub_date
2016-08-01 00:00:00pages
2776-86issue
16eissn
0014-5793issn
1873-3468journal_volume
590pub_type
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