Sandbox Reserved 1073: Difference between revisions
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The InhA gene encodes for the InhA protein. InhA catalyzes the NADH-dependent reduction of the trans double bond between positions C2-C3 of fatty acyl substrates. InhA prefers fatty acyl substrates of C16 or longer, which is consistent of the protein being a member of the FAS-II system. The longer chain length specificity of InhA distinguishes the enzyme from other enoyl-ACP reductase analogues. | The InhA gene encodes for the InhA protein. InhA catalyzes the NADH-dependent reduction of the trans double bond between positions C2-C3 of fatty acyl substrates. InhA prefers fatty acyl substrates of C16 or longer, which is consistent of the protein being a member of the FAS-II system. The longer chain length specificity of InhA distinguishes the enzyme from other enoyl-ACP reductase analogues. | ||
[[Image:Mechanism-InhA.JPG|thumb| | [[Image:Mechanism-InhA.JPG|thumb|1000px|center|Figure 1. Mechanism of InhA protein]] | ||
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Isoniazid is a first-line antibiotic that has been used to treat tuberculosis infections for over 50 years. Isoniazid is known to inhibit mycolic acid biosnthesis, which is the function of InhA. The activated form of isoniazid is covalently attached to the [http://en.wikipedia.org/wiki/Nicotinamide nicotinamide] ring of NADH. However, Isoniazid is still not an ideal antibiotic because many drug-resistant strains of tuberculosis have shown resistance to this inhibitor. Specifically, the mutation Ser<sup>94</sup> to Ala of InhA was sufficient enough to have isoniazid resistance. | Isoniazid is a first-line antibiotic that has been used to treat tuberculosis infections for over 50 years. Isoniazid is known to inhibit mycolic acid biosnthesis, which is the function of InhA. The activated form of isoniazid is covalently attached to the [http://en.wikipedia.org/wiki/Nicotinamide nicotinamide] ring of NADH. However, Isoniazid is still not an ideal antibiotic because many drug-resistant strains of tuberculosis have shown resistance to this inhibitor. Specifically, the mutation Ser<sup>94</sup> to Ala of InhA was sufficient enough to have isoniazid resistance. | ||
[[Image:Isoniazid.JPG|thumb| | [[Image:Isoniazid.JPG|thumb|700px|center|Figure 5. Isoniazid Mechanism of Action]] | ||
=== Other Inhibitors === | === Other Inhibitors === | ||