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. 2007 Aug 8;129(31):9582-3.
doi: 10.1021/ja073160k. Epub 2007 Jul 18.

New insight into the mechanism of action of and resistance to isoniazid: interaction of Mycobacterium tuberculosis enoyl-ACP reductase with INH-NADP

Argyrides Argyrou  1 , Matthew W Vetting, John S Blanchard
Affiliations

New insight into the mechanism of action of and resistance to isoniazid: interaction of Mycobacterium tuberculosis enoyl-ACP reductase with INH-NADP

Argyrides Argyrou et al. J Am Chem Soc. .
No abstract available

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Figures

Figure 1
Figure 1
Chemical structures of the INH-NAD and INH-NADP adducts. The adenosine diphosphoribose (for INH-NAD) and 2′-phosphoadenosine diphosphoribose (for INH-NADP) moieties of these molecules are abbreviated as ADPR(P). The acyclic forms are in equilibrium with the corresponding pair of diastereomeric, cyclic, hemiaminal forms.
Figure 2
Figure 2
Inhibition of M. tuberculosis InhA by INH-NADP. The solid lines represent the fit to v=VA∕[KmA(1+I∕Kiapp)+A], giving Kiapp=256±15nM. Assays contained 100 mM Pipes, pH 7.0, 10 % (v/v) glycerol, 10 nM M. tuberculosis InhA, 100 μM 2-trans-octenoyl-CoA, varied levels of NADH (2, 2.5, 3.3, 5, and 10 μM) at five fixed levels (0, 200, 400, 600, and 800 nM) of INH-NADP.
Figure 3
Figure 3
Structure of the InhA:INH-NADP complex. (A) Fo-Fc omit map for INH-NADP contoured at 3σ. (B) Superposition of the InhA:INH-NAD structure (PDBID:1ZID; colored yellow) and the InhA:INH-NADP structure (colored by atom type, grey carbons).
See this image and copyright information in PMC

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