Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Inhibition of InhA activity, but not KasA activity, induces formation of a KasA-containing complex in mycobacteria.

The Journal of biological chemistry - 6 Jun 2003

Kremer Laurent, Dover Lynn G, Morbidoni Hector R, Vilchèze Catherine, Maughan William N, Baulard Alain, Tu Shiao-Chun, Honoré Nadine, Deretic Vojo, Sacchettini James C, Locht Camille, Jacobs William R, Besra Gurdyal S

Abstract excerpt

Isoniazid (INH) remains one of the key drugs used to control tuberculosis, with the enoyl-AcpM reductase InhA being the primary target. However, based on the observation that INH-treated Mycobacterium tuberculosis overproduces KasA, an enzyme involved in the biosynthesis of mycolic acids, and induces the formation of a covalent complex consisting of AcpM, KasA, and INH, it has been proposed that KasA represents...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Oxidoreductases
Share to Antibodies

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Antitubercular Agents

Share to Bacterial Proteins

Share to Drug Resistance, Microbial

Share to Isoniazid

Share to Multienzyme Complexes

Share to Mycobacterium smegmatis

Source

Identifiers

PMID: 12654922
DOI: 10.1074/jbc.M302435200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Inhibition of InhA activity, but not KasA activity, induces formation of a KasA-containing complex in mycobacteria.PMID 12654922Read ↗

Inhibition of a Mycobacterium tuberculosis beta-ketoacyl ACP synthase by isoniazid.Semantic proximity Read ↗

Differential Sensitivity of Mycobacteria to Isoniazid Is Related to Differences in KatG-Mediated Enzymatic Activation of the DrugSemantic proximity Read ↗

Acetylation of Isoniazid Is a Novel Mechanism of Isoniazid Resistance in Mycobacterium tuberculosis.Semantic proximity Read ↗

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 ↗

A Novel Mechanism of Growth Phase-dependent Tolerance to Isoniazid in MycobacteriaSemantic proximity Read ↗

inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis.Semantic proximity Read ↗

The isoniazid analog IQG-607 is not a direct substrate for the <i>Mycobacterium tuberculosis</i> catalase-peroxidase KatGSemantic proximity Read ↗

The role of KasA and KasB in the biosynthesis of meromycolic acids and isoniazid resistance in Mycobacterium tuberculosis.Semantic proximity Read ↗

Mycobacterium tuberculosis dihydrofolate reductase is not a target relevant to the antitubercular activity of isoniazid.Semantic proximity Read ↗

The mabA gene from the inhA operon of Mycobacterium tuberculosis encodes a 3-ketoacyl reductase that fails to confer isoniazid resistance.Semantic proximity Read ↗

Conditional depletion of KasA, a key enzyme of mycolic acid biosynthesis, leads to mycobacterial cell lysis.Semantic proximity Read ↗

Evidence towards the role of arylamine N-acetyltransferase in Mycobacterium smegmatis and development of a specific antiserum against the homologous enzyme of Mycobacterium tuberculosisSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.