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

Identification of the missing trans-acting enoyl reductase required for phthiocerol dimycocerosate and phenolglycolipid biosynthesis in Mycobacterium tuberculosis.

Journal of bacteriology - 1 Jul 2007

Siméone Roxane, Constant Patricia, Guilhot Christophe, Daffé Mamadou, Chalut Christian

Abstract excerpt

Phthiocerol dimycocerosates (DIM) and phenolglycolipids (PGL) are functionally important surface-exposed lipids of Mycobacterium tuberculosis. Their biosynthesis involves the products of several genes clustered in a 70-kb region of the M. tuberculosis chromosome. Among these products is PpsD, one of the modular type I polyketide synthases responsible for the synthesis of the lipid core common to DIM and PGL....

Read the complete abstract on PubMed

Topics

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

Share to Chromatography, Thin Layer
Share to Computational Biology

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

Share to Glycolipids

Share to Lipids

Share to Magnetic Resonance Spectroscopy

Share to Molecular Structure

Share to Mycobacterium tuberculosis

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Source

Open in PubMed Open full text

Identifiers

PMID: 17468241
DOI: 10.1128/JB.00169-07
PMCID: PMC1913427

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

Identification of the missing trans-acting enoyl reductase required for phthiocerol dimycocerosate and phenolglycolipid biosynthesis in Mycobacterium tuberculosis.PMID 17468241Read ↗

Molecular dissection of the role of two methyltransferases in the biosynthesis of phenolglycolipids and phthiocerol dimycoserosate in the Mycobacterium tuberculosis complex.Semantic proximity Read ↗

Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosisSemantic proximity Read ↗

Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosisSemantic proximity Read ↗

Analysis of the Phthiocerol Dimycocerosate Locus ofMycobacterium tuberculosisSemantic proximity Read ↗

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

A lipid profile typifies the Beijing strains of Mycobacterium tuberculosis: identification of a mutation responsible for a modification of the structures of phthiocerol dimycocerosates and phenolic glycolipids.Semantic proximity Read ↗

Gene knockout reveals a novel gene cluster for the synthesis of a class of cell wall lipids unique to pathogenic mycobacteria.Semantic proximity Read ↗

Both phthiocerol dimycocerosates and phenolic glycolipids are required for virulence of Mycobacterium marinum.Semantic proximity Read ↗

Role of the pks15/1 Gene in the Biosynthesis of Phenolglycolipids in the Mycobacterium tuberculosisComplexSemantic proximity Read ↗

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

p-Hydroxybenzoic acid synthesis in Mycobacterium tuberculosis.Semantic proximity Read ↗

Multiple deletions in the polyketide synthase gene repertoire of<i>Mycobacterium tuberculosis</i>reveal functional overlap of cell envelope lipids in host-pathogen interactionsSemantic proximity Read ↗

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