Abstract
The resistance of the emerging human pathogenStenotrophomonas maltophiliato tetracycline antibiotics mainly depends on multidrug efflux pumps and ribosomal protection enzymes. However, the genomes of several strains of this Gram-negative bacterium code for a FAD-dependent monooxygenase (SmTetX) homologous to tetracycline destructases. This protein was recombinantly produced and its structure and function were investigated. Activity assays usingSmTetX showed its ability to modify oxytetracycline with a catalytic rate comparable to those of other destructases.SmTetX shares its fold with the tetracycline destructase TetX fromBacteroides thetaiotaomicron; however, its active site possesses an aromatic region that is unique in this enzyme family. A docking study confirmed tetracycline and its analogues to be the preferred binders amongst various classes of antibiotics.
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