Structural highlights
Function
Q4E0B2_TRYCC Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis.[RuleBase:RU362120]
Publication Abstract from PubMed
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 beta-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.
The structure of a Trypanosoma cruzi glucose-6-phosphate dehydrogenase reveals differences from the mammalian enzyme.,Mercaldi GF, Dawson A, Hunter WN, Cordeiro AT FEBS Lett. 2016 Jul 8. doi: 10.1002/1873-3468.12276. PMID:27391210[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mercaldi GF, Dawson A, Hunter WN, Cordeiro AT. The structure of a Trypanosoma cruzi glucose-6-phosphate dehydrogenase reveals differences from the mammalian enzyme. FEBS Lett. 2016 Jul 8. doi: 10.1002/1873-3468.12276. PMID:27391210 doi:http://dx.doi.org/10.1002/1873-3468.12276
