| Literature DB >> 19796954 |
Tina S Skinner-Adams1, Colin M Stack, Katharine R Trenholme, Chris L Brown, Jolanta Grembecka, Jonathan Lowther, Artur Mucha, Marcin Drag, Pawel Kafarski, Sheena McGowan, James C Whisstock, Donald L Gardiner, John P Dalton.
Abstract
The neutral aminopeptidases M1 alanyl aminopeptidase (PfM1AAP) and M17 leucine aminopeptidase (PfM17LAP) of the human malaria parasite Plasmodium falciparum are targets for the development of novel anti-malarial drugs. Although the functions of these enzymes remain unknown, they are believed to act in the terminal stages of haemoglobin degradation, generating amino acids essential for parasite growth and development. Inhibitors of both enzymes are lethal to P. falciparum in culture and kill the murine malaria P. chabaudi in vivo. Recent biochemical, structural and functional studies provide the substrate specificity and mechanistic binding data needed to guide the development of more potent anti-malarial drugs. Together with biological studies, these data form the rationale for choosing PfM1AAP and PfM17LAP as targets for anti-malarial development. Copyright 2009 Elsevier Ltd. All rights reserved.Entities:
Mesh：
Substances：
Year: 2009 PMID： 19796954 DOI： 10.1016/j.tibs.2009.08.004
Source DB: PubMed Journal: Trends Biochem Sci ISSN： 0968-0004 Impact factor: 13.807