| Literature DB >> 11239932 |
R McLeod1, S P Muench, J B Rafferty, D E Kyle, E J Mui, M J Kirisits, D G Mack, C W Roberts, B U Samuel, R E Lyons, M Dorris, W K Milhous, D W Rice.
Abstract
Fab I, enoyl acyl carrier protein reductase (ENR), is an enzyme used in fatty acid synthesis. It is a single chain polypeptide in plants, bacteria, and mycobacteria, but is part of a complex polypeptide in animals and fungi. Certain other enzymes in fatty acid synthesis in apicomplexan parasites appear to have multiple forms, homologous to either a plastid, plant-like single chain enzyme or more like the animal complex polypeptide chain. We identified a plant-like Fab I in Plasmodium falciparum and modelled the structure on the Brassica napus and Escherichia coli structures, alone and complexed to triclosan (5-chloro-2-[2,4 dichlorophenoxy] phenol]), which confirmed all the requisite features of an ENR and its interactions with triclosan. Like the remarkable effect of triclosan on a wide variety of bacteria, this compound markedly inhibits growth and survival of the apicomplexan parasites P. falciparum and Toxoplasma gondii at low (i.e. IC50 congruent with150-2000 and 62 ng/ml, respectively) concentrations. Discovery and characterisation of an apicomplexan Fab I and discovery of triclosan as lead compound provide means to rationally design novel inhibitory compounds.Entities:
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Year: 2001 PMID: 11239932 DOI: 10.1016/s0020-7519(01)00111-4
Source DB: PubMed Journal: Int J Parasitol ISSN: 0020-7519 Impact factor: 3.981