Structural basis for the variation in triclosan affinity to enoyl reductases.
J Mol Biol
; 343(1): 147-55, 2004 Oct 08.
Article
em En
| MEDLINE
| ID: mdl-15381426
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 analysis reveals that the conformation of this flexible loop and the binding affinities of triclosan to each of these enzymes are strongly correlated.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oxirredutases
/
Triclosan
/
Variação Genética
Idioma:
En
Revista:
J Mol Biol
Ano de publicação:
2004
Tipo de documento:
Article