construction of tetracysteine-tagged enzyme variants carrying the tag at the N-terminus, C-terminus, or both N- and C-terminus. All the tetracysteine-tagged FabI enzymes have high enzyme activities while the enhanced green fluorescent protein-tagged FabI exhaustively loses the activity. The binding between 4',5'-bis(1,3,2-dithioarsolan-2-yl)fuorescein, i.e. FlAsH reagent and tetracysteine motif is stable against high pressure, high field strength, high temperature, and ultrasound. A capillary zone electrophoresis system equipped with a laser-induced fluorescence detector has a detection limit of 10-16 M for the labeled proteins
development of a simple thermal shift assay, which does not use ACP-linked substrates, to determine the binding ability of triclosan to the enzyme's active site
Mycobacterium tuberculosis enoyl acyl carrier protein reductase represents a prospective drug target against tuberculosis, identified MtENR binders can be characterized as potential therapeutic targets laying a foundation for future lead identification and optimization studies
the results can be of primary importance in to elucidate the mechanism of action of isoniazid and to better understand the isoniazid-dependent resistances, and they can also prove useful in the design of a new generation of antitubercular drugs
de novo fatty acid biosynthetic components encoded in Francisella tularensis are transcriptionally active during infection in the mouse model of tularemia
de novo fatty acid biosynthetic components encoded in Francisella tularensis are transcriptionally active during infection in the mouse model of tularemia
the results can be of primary importance in to elucidate the mechanism of action of isoniazid and to better understand the isoniazid-dependent resistances, and they can also prove useful in the design of a new generation of antitubercular drugs
Mycobacterium tuberculosis enoyl acyl carrier protein reductase represents a prospective drug target against tuberculosis, identified MtENR binders can be characterized as potential therapeutic targets laying a foundation for future lead identification and optimization studies
the enzyme is a target for the antitubercular drug isoniazid. InhA inhibitors targeted at the enoyl substrate binding site may be effective against existing isoniazid-resistant strains of Mycobacterium tuberculosis
the enzyme is a target for the antitubercular drug isoniazid. InhA inhibitors targeted at the enoyl substrate binding site may be effective against existing isoniazid-resistant strains of Mycobacterium tuberculosis