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   [25]Structural Basis for the Variation in Triclosan Affinit...
   Journal of Molecular Biology

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   [26]Structural Basis for the Variation in Triclosan Affinity to Enoyl
   Reductases  Original Research Article
   Journal of Molecular Biology, Volume 343, Issue 1, 8 October 2004,
   Pages 147-155
   Lakshmi Swarnamukhi Pidugu, Mili Kapoor, Namita Surolia, Avadhesha
   Surolia, Kaza Suguna
   Abstract
   Bacteria synthesize fatty acids in a dissociated type pathway different
   from that in humans. Enoyl acyl carrier protein reductase, which
   catalyzes the final step of fatty acid elongation, has been validated
   as a potential anti-microbial drug target. Triclosan is known to
   inhibit this enzyme effectively. Precise characterization of the mode
   of triclosan binding is required to develop highly specific inhibitors.
   With this in view, interactions between triclosan, the cofactor
   NADH/NAD^+ and the enzyme from five different species, one plant and
   four of microbial origin, have been examined in the available crystal
   structures. A comparison of these structures shows major structural
   differences at the substrate/inhibitor/cofactor-binding loop. The