| Autor: |
de Medeiros PS; Instituto de Pesquisas em Patologias Tropicais (IPEPATRO), Rua da Beira 7671, Rodovia BR364 km 3.5, 76812-245 Porto Velho, RO, Brazil., Ducati RG, Basso LA, Santos DS, da Silva LH |
| Jazyk: |
angličtina |
| Zdroj: |
Enzyme research [Enzyme Res] 2011; Vol. 2011, pp. 642758. Date of Electronic Publication: 2011 Mar 22. |
| DOI: |
10.4061/2011/642758 |
| Abstrakt: |
Malaria continues to be a major cause of children's morbidity and mortality worldwide, causing nearly one million deaths annually. The human malaria parasite, Plasmodium falciparum, synthesizes fatty acids employing the Type II fatty acid biosynthesis system (FAS II), unlike humans that rely on the Type I (FAS I) pathway. The FAS II system elongates acyl fatty acid precursors of the cell membrane in Plasmodium. Enoyl reductase (ENR) enzyme is a member of the FAS II system. Here we present steady-state kinetics, pre-steady-state kinetics, and equilibrium fluorescence spectroscopy data that allowed proposal of P. falciparum ENR (PfENR) enzyme mechanism. Moreover, building on previous results, the present study also evaluates the PfENR inhibition by the pentacyano(isoniazid)ferrateII compound. This inorganic complex represents a new class of lead compounds for the development of antimalarial agents focused on the inhibition of PfENR. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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