Binding of catalase-peroxidase-activated isoniazid to wild-type and mutant Mycobacterium tuberculosis enoyl-ACP reductases

Journal of the American Chemical Society

Volumn 118, Issue 6, 1996, Pages 1561-1562

  Quernard, Annaik ^b   Dessen, Andrea ^a   Sugantino, Michelle ^a   Jacobs Jr , William R ^a   Sacchettini, James C ^a   Blanchard, John S ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ISONIAZID; OXIDOREDUCTASE;

ARTICLE; DRUG ACTIVATION; ENZYME BINDING; MUTANT; MYCOBACTERIUM TUBERCULOSIS;

EID: 0038492810     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja950998b     Document Type: Article

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24. In 20 mM Hepes. pH 7.3, either in the presence or in the absence of 100 μM NADH, μ6 uM InhA was titrated with 25 successive injections of 4 μL of 5.6 mM ligand (isonicotinic acid, isonicotinamide, or pyridine-4-carboxaldehyde) in the same buffer in an Omega microcalorimeter (Microcal, Inc.) at 25°C.
25. 14C]Isoniazid had a specific radioactivity of 13 mCi/mmol.
26. 14C]isoniazid, and 1.9 μM KatG, 9 μM InhA was incubated. The InhA activity was reduced by 82% after incubation.
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