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  • Title: Exploring the interaction energies for the binding of hydroxydiphenyl ethers to enoyl-acyl carrier protein reductases.
    Author: Muralidharan J, Suguna K, Surolia A, Surolia N.
    Journal: J Biomol Struct Dyn; 2003 Feb; 20(4):589-94. PubMed ID: 12529157.
    Abstract:
    It is now well established that the potent anti-microbial compound, triclosan, interrupts the type II fatty acid synthesis by inhibiting the enzyme enoyl-ACP reductase in a number of organisms. Existence of a high degree of similarity between the recently discovered enoyl-ACP reductase from P. falciparum and B. napus enzyme permitted building of a satisfactory model for the former enzyme that explained some of the key aspects of the enzyme such as its specificity for binding to the cofactor and the inhibitor. We now report the interaction energies between triclosan and other hydroxydiphenyl ethers with the enzymes from B. napus, E. coli and P. falciparum. Examination of the triclosan-enzyme interactions revealed that subtle differences exist in the ligand binding sites of the enzymes from different sources i.e., B. napus, E. coli and P. falciparum. A comparison of their binding propensities thus determined should aid in the design of effective inhibitors for the respective enzymes.
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