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

The nonredundant roles of two 4'-phosphopantetheinyl transferases in vital processes of Mycobacteria.

Proceedings of the National Academy of Sciences of the United States of America - 30 May 2006

Chalut Christian, Botella Laure, de Sousa-D'Auria Célia, Houssin Christine, Guilhot Christophe

Abstract excerpt

Mycobacterium tuberculosis contains >20 enzymes that require activation by transfer of the 4'-phosphopantetheine moiety of CoA onto a conserved serine residue, a posttranslational modification catalyzed by 4'-phosphopantetheinyl transferases (PPTases). The modified proteins are involved in key me...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Colony Count, Microbial
Share to Corynebacterium glutamicum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fatty Acids

Share to Microbial Viability

Share to Molecular Structure

Share to Mycobacterium

Share to Transferases (Other Substituted Phosphate Groups)

Source

Open in PubMed Open full text

Identifiers

PMID: 16709676
DOI: 10.1073/pnas.0511129103
PMCID: PMC1570105

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-16709676-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The nonredundant roles of two 4'-phosphopantetheinyl transferases in vital processes of Mycobacteria.PMID 16709676Read ↗

4′-Phosphopantetheinyl Transferase PptT, a New Drug Target Required for Mycobacterium tuberculosis Growth and Persistence In VivoSemantic proximity Read ↗

The Molecular Genetics of Mycolic Acid BiosynthesisSemantic proximity Read ↗

Biosynthesis of mycobacterial lipids by polyketide synthases and beyondSemantic proximity Read ↗

The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue.Semantic proximity Read ↗

Serine threonine protein kinases of mycobacterial genus: phylogeny to functionSemantic proximity Read ↗

Characterization of key enzymes involved in triacylglycerol biosynthesis in mycobacteria.Semantic proximity Read ↗

Genetic and lipidomic identification of tuberculostearic acid as a controller of mycobacterial membrane compartmentalizationSemantic proximity Read ↗

The PE-PPE Family of Mycobacterium tuberculosis: Proteins in DisguiseSemantic proximity Read ↗

Mechanistic studies of mycobacterial glycolipid biosynthesis by the mannosyltransferase PimESemantic proximity Read ↗

Phylogeny to function: PE / PPE protein evolution and impact on M ycobacterium tuberculosis pathogenicitySemantic proximity Read ↗

Two Accessory Proteins Govern MmpL3 Mycolic Acid Transport in MycobacteriaSemantic proximity Read ↗

Biosynthesis of cell envelope-associated phenolic glycolipids in Mycobacterium marinum.Semantic proximity Read ↗

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