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Literature summary extracted from

  • Pan, P.; Tonge, P.
    Targeting InhA, the FASII enoyl-ACP reductase SAR studies on novel inhibitor scaffolds (2012), Curr. Top. Med. Chem., 12, 672-693 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.118 additional information SAR studies on novel inhibitor scaffolds. Inhibitor scaffolds include the diaryl ethers, pyrrolidine carboxamides, piperazine indoleformamides, pyrazoles, arylamides, fatty acids, and imidazopiperidines, all of which form ternary complexes with InhA and the NAD cofactor, as well as isoniazid and the diazaborines which covalently modify the cofactor. Analysis of the structural data has enabled the development of a common binding mode for the ternary complex inhibitors, which includes a hydrogen bond network, a large hydrophobic pocket and a third size-limited binding area comprised of both polar and non-polar groups. A critical factor in InhA inhibition involves ordering of the substrate binding loop, located close to the active site, and a direct link is proposed between loop ordering and slow onset enzyme inhibition. Slow onset inhibitors have long residence times on the enzyme target, a property that is of critical importance for in vivo activity Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.118 Mycobacterium tuberculosis
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Synonyms

EC Number Synonyms Comment Organism
1.3.1.118 FASII enoyl-ACP reductase
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 Mycobacterium tuberculosis
1.3.1.118 InhA
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 Mycobacterium tuberculosis