Crystal Structure and Function of the Isoniazid Target of Mycobacterium tuberculosis

Resistance to isoniazid in Mycobacterium tuberculosis can be mediated by substitution of alanine for serine 94 in the InhA protein, the drug's primary target. InhA was shown to catalyze the β-nicotinamide adenine dinucleotide (NADH)-specific reduction of 2-trans-enoyl-acyl carrier protein, an e...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 1995-03, Vol.267 (5204), p.1638-1641
Hauptverfasser:	Dessen, Andréa, Quémard, Annaïk, Blanchard, John S., Jacobs, William R., Sacchettini, James C.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids Antibacterial agents Antibiotics. Antiinfectious agents. Antiparasitic agents Atoms Bacteria Bacterial Proteins - chemistry Bacterial Proteins - drug effects Bacterial Proteins - genetics Bacterial Proteins - physiology Binding Sites Biochemistry Biological and medical sciences Computer Graphics Crystallization Crystallography, X-Ray Crystals Drug resistance Drug Resistance, Microbial Drugs Enzymes Hydrogen Bonding Hydrogen bonds Isoniazid - pharmacology Kinetics Medical sciences Models, Molecular Molecules Mycobacterium tuberculosis Mycobacterium tuberculosis - chemistry Mycobacterium tuberculosis - drug effects NAD - metabolism Oxidation-Reduction Oxidoreductases Pharmacology. Drug treatments Protein Conformation Protein Folding Protein Structure, Secondary Proteins Scientific Concepts Tuberculosis Water
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