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 In Vitro Redundant Enzymes PurN and PurT Are Both Essential for Systemic Infection of Mice in Salmonella enterica Serovar Typhimurium.

Infection and immunity - 1 Jul 2016

Jelsbak Lotte, Mortensen Mie I B, Kilstrup Mogens, Olsen John E

Abstract excerpt

Metabolic enzymes show a high degree of redundancy, and for that reason they are generally ignored in searches for novel targets for anti-infective substances. The enzymes PurN and PurT are redundant in vitro in Salmonella enterica serovar Typhimurium, in which they perform the third step of purine synthesis. Surprisingly, the results of the current study demonstrated that single-gene deletions of each of the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Bacterial Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Carbon

Share to Macrophages

Share to Microbial Viability

Share to Salmonella Infections

Share to Salmonella typhimurium

Share to Virulence

Source

Open in PubMed Open full text

Identifiers

PMID: 27113361
DOI: 10.1128/IAI.00182-16
PMCID: PMC4936368

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

The In Vitro Redundant Enzymes PurN and PurT Are Both Essential for Systemic Infection of Mice in Salmonella enterica Serovar Typhimurium.PMID 27113361Read ↗

A metabolic intermediate of the fructose-asparagine utilization pathway inhibits growth of a Salmonella fraB mutant.Semantic proximity Read ↗

Mechanisms ofSalmonellapathogenesis in animal modelsSemantic proximity Read ↗

Synthesis of thiamine in Salmonella typhimurium independent of the purF function.Semantic proximity Read ↗

Phosphoribosylpyrophosphate synthetase (PrsA) variants alter cellular pools of ribose 5-phosphate and influence thiamine synthesis in Salmonella enterica.Semantic proximity Read ↗

Analysis of virulence and inflammatory potential of Shigella flexneri purine biosynthesis mutants.Semantic proximity Read ↗

Defects in pyruvate kinase cause a conditional increase of thiamine synthesis in Salmonella typhimurium.Semantic proximity Read ↗

Extensive in vivo resilience of persistent Salmonella.Semantic proximity Read ↗

Glucose and Glycolysis Are Required for the Successful Infection of Macrophages and Mice by Salmonella enterica Serovar TyphimuriumSemantic proximity Read ↗

Amplification of adenine phosphoribosyltransferase suppresses the conditionally lethal growth and virulence phenotype of Leishmania donovani mutants lacking both hypoxanthine-guanine and xanthine phosphoribosyltransferases.Semantic proximity Read ↗

Genetic analysis of metabolic crosstalk and its impact on thiamine synthesis in Salmonella typhimurium.Semantic proximity Read ↗

Perturbations in histidine biosynthesis uncover robustness in the metabolic network of Salmonella enterica.Semantic proximity Read ↗

Intracellular multiplication and virulence of Shigella flexneri auxotrophic mutants.Semantic proximity Read ↗

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