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

Alanyl-phosphatidylglycerol synthase: mechanism of substrate recognition during tRNA-dependent lipid modification in Pseudomonas aeruginosa.

Molecular microbiology - 1 May 2011

Hebecker Stefanie, Arendt Wiebke, Heinemann Ilka U, Tiefenau Jana H J, Nimtz Manfred, Rohde Manfred, Söll Dieter, Moser Jürgen

Abstract excerpt

Bacterial lipid homeostasis plays an important role for the adaptation to changing environments and under conditions of antimicrobial treatment. The tRNA-dependent aminoacylation of the phospholipid phosphatidylglycerol catalysed by aminoacyl-phosphatidylglycerol synthases was shown to render various organisms less susceptible to antibacterial agents. Therefore, this type of enzyme might provide a new target to...

Read the complete abstract on PubMed

Topics

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

Share to Aminoacyltransferases
Share to Lipid Metabolism

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

Share to Mass Spectrometry

Share to Phosphatidylglycerols

Share to Phospholipids

Share to Pseudomonas aeruginosa

Share to RNA, Transfer

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 21392131
DOI: 10.1111/j.1365-2958.2011.07621.x
PMCID: PMC3111014

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

Alanyl-phosphatidylglycerol synthase: mechanism of substrate recognition during tRNA-dependent lipid modification in Pseudomonas aeruginosa.PMID 21392131Read ↗

Adaptation of Pseudomonas aeruginosa to various conditions includes tRNA-dependent formation of alanyl-phosphatidylglycerol.Semantic proximity Read ↗

The phosphatidylglycerol phosphate synthase PgsA utilizes a trifurcated amphipathic cavity for catalysis at the membrane-cytosol interfaceSemantic proximity Read ↗

A divergent Pseudomonas aeruginosa palmitoyltransferase essential for cystic fibrosis-specific lipid A.Semantic proximity Read ↗

Phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) of Escherichia coli has seven transmembrane segments, and its essential residues are embedded in the membrane.Semantic proximity Read ↗

Topology and active site of PlsY: the bacterial acylphosphate:glycerol-3-phosphate acyltransferase.Semantic proximity Read ↗

Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinaseSemantic proximity Read ↗

Unravelling the mechanisms causing murepavadin resistance in Pseudomonas aeruginosa: lipopolysaccharide alterations and its consequences.Semantic proximity Read ↗

Cardiolipin biosynthesis in Streptococcus mutans is regulated in response to external pHSemantic proximity Read ↗

Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycinSemantic proximity Read ↗

The Role of Lipids in Legionella-Host Interaction.Semantic proximity Read ↗

A Staphylococcus aureus ypfP mutant with strongly reduced lipoteichoic acid (LTA) content: LTA governs bacterial surface properties and autolysin activity.Semantic proximity Read ↗

Host-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues.Semantic proximity Read ↗

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