Literature summary for 1.3.1.9 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 .

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Protein Variants

Protein Variants	Comment	Organism
I21V	isoniazid-resistant mutant	Mycobacterium tuberculosis

Inhibitors

Inhibitors	Comment	Organism	Structure
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
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

Organism

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

Synonyms

Synonyms	Comment	Organism
2-trans-enoyl-ACP reductase	-	Mycobacterium tuberculosis
InhA	-	Mycobacterium tuberculosis

General Information

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

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Release 2023.1 (January 2023)