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

Exploring the structure and function of the mycobacterial KatG protein using trans-dominant mutants.

Antimicrobial agents and chemotherapy - 1 Jan 2003

DeVito Joseph A, Morris Sheldon

Abstract excerpt

In order to probe the structure and function of the mycobacterial catalase-peroxidase enzyme (KatG), we employed a genetic approach using dominant-negative analysis of katG merodiploids. Transformation of Mycobacterium bovis BCG with various katG point mutants (expressed from low-copy-number plasmids) resulted in reductions in peroxidase and catalase activities as measured in cell extracts. These reductions in...

Read the complete abstract on PubMed

Topics

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

Share to Catalase
Share to Electrophoresis, Agar Gel
Share to Escherichia coli Proteins

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

Share to Microbial Sensitivity Tests

Share to Mutation

Share to Mycobacterium tuberculosis

Share to Peroxidase

Share to Phenotype

Source

Open in PubMed Open full text

Identifiers

PMID: 12499190
DOI: 10.1128/AAC.47.1.188-195.2003
PMCID: PMC148984

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Exploring the structure and function of the mycobacterial KatG protein using trans-dominant mutants.PMID 12499190Read ↗

Isoniazid activation defects in recombinant Mycobacterium tuberculosis catalase-peroxidase (KatG) mutants evident in InhA inhibitor production.Semantic proximity Read ↗

Three-dimensional model and molecular mechanism of Mycobacterium tuberculosis catalase-peroxidase (KatG) and isoniazid-resistant KatG mutants.Semantic proximity Read ↗

Roles of the three Mycobacterium smegmatis katG genes for peroxide detoxification and isoniazid susceptibility.Semantic proximity Read ↗

Mutation of katG in a clinical isolate of Mycobacterium tuberculosis: effects on catalase-peroxidase for isoniazid activation.Semantic proximity Read ↗

Virulence of Mycobacterium tuberculosis after Acquisition of Isoniazid Resistance: Individual Nature of katG Mutants and the Possible Role of AhpC.Semantic proximity Read ↗

Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis.Semantic proximity Read ↗

Comparative study of enzymatic activities of new KatG mutants from low- and high-level isoniazid-resistant clinical isolates of Mycobacterium tuberculosis.Semantic proximity Read ↗

Molecular Analysis of katG Encoding Catalase-Peroxidase from Clinical Isolate of Isoniazid-Resistant Mycobacterium tuberculosis.Semantic proximity Read ↗

Molecular mechanisms of isoniazid resistance in Mycobacterium tuberculosis and Mycobacterium bovis.Semantic proximity Read ↗

Mutations in the catalase-peroxidase gene from isoniazid-resistant Mycobacterium tuberculosis isolates.Semantic proximity Read ↗

Involvement of the N- and C-terminal domains of Mycobacterium tuberculosis KatG in the protection of mutant Escherichia coli against DNA-damaging agents.Semantic proximity Read ↗

<b>Site‐directed mutagenesis of the <i>katG</i> gene of <i>Mycobacterium tuberculosis</i>: effects on catalase–peroxidase activities and isoniazid resistance</b>Semantic proximity Read ↗

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