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Literature summary extracted from

  • Da Costa, A.; Pauli, I.; Dorn, M.; Schroeder, E.; Zhan, C.; De Souza, O.
    Conformational changes in 2-trans-enoyl-ACP (CoA) reductase (InhA) from M. tuberculosis induced by an inorganic complex A molecular dynamics simulation study (2012), J. Mol. Model., 18, 1779-1790 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.3.1.9 I21V isoniazid-resistant mutant Mycobacterium tuberculosis
1.3.1.118 I21V isoniazid-resistant mutant Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.9 isoniazid prodrug which is biologically activated by the Mycobacterium tuberculosis catalase-peroxidase KatG enzyme. The activation reaction promotes the formation of an isonicotinyl-NAD adduct which inhibits the InhA enzyme, resulting in reduction of mycolic acid biosynthesis Mycobacterium tuberculosis
1.3.1.9 pentacyano(isoniazid)ferrate(II) the inorganic complex inhibits both wild-type and isoniazid-resistant Ile21Val mutants of InhA and this inactivation did not require activation by KatG. Molecular dynamics simulations show that the interaction of pentacyano(isoniazid)ferrate(II) with InhA leads to macromolecular instabilities reflected in the long time necessary for simulation convergence. These instabilities are mainly due to perturbation of the substrate binding loop, particularly the partial denaturation of helices alpha6 and alpha7 Mycobacterium tuberculosis
1.3.1.118 isoniazid prodrug which is biologically activated by the Mycobacterium tuberculosis catalase-peroxidase KatG enzyme. The activation reaction promotes the formation of an isonicotinyl-NAD adduct which inhibits the InhA enzyme, resulting in reduction of mycolic acid biosynthesis Mycobacterium tuberculosis
1.3.1.118 pentacyano(isoniazid)ferrate(II) the inorganic complex inhibits both wild-type and isoniazid-resistant Ile21Val mutants of InhA and this inactivation did not require activation by KatG. Molecular dynamics simulations show that the interaction of pentacyano(isoniazid)ferrate(II) with InhA leads to macromolecular instabilities reflected in the long time necessary for simulation convergence. These instabilities are mainly due to perturbation of the substrate binding loop, particularly the partial denaturation of helices alpha6 and alpha7 Mycobacterium tuberculosis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.9 Mycobacterium tuberculosis P9WGR1
-
-
1.3.1.9 Mycobacterium tuberculosis ATCC 25618 P9WGR1
-
-
1.3.1.118 Mycobacterium tuberculosis P9WGR1
-
-
1.3.1.118 Mycobacterium tuberculosis ATCC 25618 P9WGR1
-
-

Synonyms

EC Number Synonyms Comment Organism
1.3.1.9 2-trans-enoyl-ACP reductase
-
 Mycobacterium tuberculosis
1.3.1.9 InhA
-
 Mycobacterium tuberculosis
1.3.1.118 2-trans-enoyl-ACP reductase
-
 Mycobacterium tuberculosis
1.3.1.118 InhA
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
1.3.1.9 metabolism the enzyme is involved in the biosynthesis of mycolic acids Mycobacterium tuberculosis
1.3.1.118 metabolism the enzyme is involved in the biosynthesis of mycolic acids Mycobacterium tuberculosis