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

Functional and structural characterization of a thiol peroxidase from Mycobacterium tuberculosis.

Journal of molecular biology - 1 Sept 2006

Rho Beom-Seop, Hung Li-Wei, Holton James M, Vigil Dominico, Kim Su-Il, Park Min S, Terwilliger Thomas C, Pédelacq Jean-Denis

Abstract excerpt

A thiol peroxidase (Tpx) from Mycobacterium tuberculosis was functionally analyzed. The enzyme shows NADPH-linked peroxidase activity using a thioredoxin-thioredoxin reductase system as electron donor, and anti-oxidant activity in a thiol-dependent metal-catalyzed oxidation system. It reduces H2O2, t-butyl hydroperoxide, and cumene hydroperoxide, and is inhibited by sulfhydryl reagents. Mutational studies...

Read the complete abstract on PubMed

Topics

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

Share to Dimerization
Share to Molecular Weight

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutant Proteins

Share to Peroxidases

Share to Protein Structure, Quaternary

Share to Serine

Share to Solutions

Source

Identifiers

PMID: 16884737
DOI: 10.1016/j.jmb.2006.05.076

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Functional and structural characterization of a thiol peroxidase from Mycobacterium tuberculosis.PMID 16884737Read ↗

The role of thioredoxin proteins in <i>Mycobacterium tuberculosis</i> probed by proteome-wide target profilingSemantic proximity Read ↗

Microbial 2-Cys Peroxiredoxins: Insights into Their Complex Physiological Roles.Semantic proximity Read ↗

The cytosolic tryparedoxin peroxidase from Trypanosoma cruzi induces a pro-inflammatory Th1 immune response in a peroxidatic cysteine-dependent manner.Semantic proximity Read ↗

The Oxidative Stress Network of Mycobacterium tuberculosis Reveals Coordination between Radical Detoxification Systems.Semantic proximity Read ↗

The structure of an orthorhombic crystal form of a 'forced reduced' thiol peroxidase reveals lattice formation aided by the presence of the affinity tag.Semantic proximity Read ↗

Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61.Semantic proximity Read ↗

Structural insights into the catalytic mechanism of Trypanosoma cruzi GPXI (glutathione peroxidase-like enzyme I).Semantic proximity Read ↗

<i>Mycobacterium tuberculosis</i> Rv0991c is a redox-regulated molecular chaperoneSemantic proximity Read ↗

Tryparedoxin peroxidase of Leishmania donovani: molecular cloning, heterologous expression, specificity, and catalytic mechanism.Semantic proximity Read ↗

Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria.Semantic proximity Read ↗

Site-directed mutagenesis reveals a novel catalytic mechanism of Mycobacterium tuberculosis alkylhydroperoxidase C.Semantic proximity Read ↗

The oxidation-sensing regulator (MosR) is a new redox-dependent transcription factor in Mycobacterium tuberculosis.Semantic proximity Read ↗

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