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Article

Biochemical and genetic data suggest that InhA is not the primary target for activated isoniazid in Mycobacterium tuberculosis.

The Journal of infectious diseases - 1 Nov 1996

Mdluli K, Sherman D R, Hickey M J, Kreiswirth B N, Morris S, Stover C K, Barry C E

Abstract excerpt

An examination of the pattern of lipid biosynthetic responses to isoniazid (INH) treatment of Mycobacterium tuberculosis and Mycobacterium smegmatis suggests that the mode of action of activated INH differs between these 2 organisms. Transformation of M. smegmatis with inhA on a plasmid construct conferred high-level resistance to INH, while the same construct failed to confer resistance upon M. tuberculosis. The...

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Identifiers

PMID: 8896513
DOI: 10.1093/infdis/174.5.1085

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Biochemical and genetic data suggest that InhA is not the primary target for activated isoniazid in Mycobacterium tuberculosis.PMID 8896513Read ↗

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ahpC, a gene involved in isoniazid resistance of the Mycobacterium tuberculosis complex.Semantic proximity Read ↗

Genetic evidence that InhA of Mycobacterium smegmatis is a target for triclosan.Semantic proximity Read ↗

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Inactivation of the inhA-encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis.Semantic proximity Read ↗

NADH dehydrogenase defects confer isoniazid resistance and conditional lethality in Mycobacterium smegmatis.Semantic proximity Read ↗

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