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Literature summary for 1.3.1.118 extracted from

  • Argyrou, A.; Vetting, M.; Blanchard, J.
    New insight into the mechanism of action of and resistance to isoniazid Interaction of Mycobacterium tuberculosis enoyl-ACP reductase with INH-NADP (2007), J. Am. Chem. Soc., 129, 9582-9583 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization of InhA with isoniazid-NADP bound and the structure of the complex is solved Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
isoniazid a pro-drug, which is oxidatively activated in vivo by the katG-encoded mycobacterial catalase peroxidase to generate an isonicotinoyl radical. This highly reactive species then reacts nonenzymatically with the cellular pyridine nucleotide coenzymes, NAD+ and NADP+, to generate 12 isonicotinoyl-NAD(P)+ adducts. Of these, the acyclic 4S isomer of isoniazid-NAD+ and the acyclic 4R isomer of isoniazid-NADP+ inhibit the inhA-encoded enoyl-ACP reductase Mycobacterium tuberculosis
isoniazid-NAD+
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Mycobacterium tuberculosis
isoniazid-NADP competitive Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WGR1
-
-
Mycobacterium tuberculosis ATCC 25618 P9WGR1
-
-

Synonyms

Synonyms Comment Organism
InhA
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Mycobacterium tuberculosis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00013
-
isoniazid-NADP pH 7.0, temperature not specified in the publication Mycobacterium tuberculosis