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

Mycobacterium tuberculosis Is a Natural Ornithine Aminotransferase (rocD) Mutant and Depends on Rv2323c for Growth on Arginine.

PloS one - 1 Jan 2015

Hampel Annegret, Huber Claudia, Geffers Robert, Spona-Friedl Marina, Eisenreich Wolfgang, Bange Franz-Christoph

Abstract excerpt

Mycobacterium tuberculosis (Mtb) possesses a genetic repertoire for metabolic pathways, which are specific and fit to its intracellular life style. Under in vitro conditions, Mtb is known to use arginine as a nitrogen source, but the metabolic pathways for arginine utilization have not been identified. Here we show that, in the presence of arginine, Mtb upregulates a gene cluster which includes an ornithine...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Bacterial Proteins

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

Share to Mutation

Share to Mycobacterium tuberculosis

Source

Open in PubMed Open full text

Identifiers

PMID: 26368558
DOI: 10.1371/journal.pone.0136914
PMCID: PMC4569260

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

Mycobacterium tuberculosis Is a Natural Ornithine Aminotransferase (rocD) Mutant and Depends on Rv2323c for Growth on Arginine.PMID 26368558Read ↗

Rv3722c governs aspartate-dependent nitrogen metabolism in <i>Mycobacterium tuberculosis</i>Semantic proximity Read ↗

CcpA regulates arginine biosynthesis in Staphylococcus aureus through repression of proline catabolism.Semantic proximity Read ↗

The prrAB two-component system is essential for Mycobacterium tuberculosis viability and is induced under nitrogen-limiting conditions.Semantic proximity Read ↗

A Genomic View on Nitrogen Metabolism and Nitrogen Control in MycobacteriaSemantic proximity Read ↗

Construction and phenotypic characterization of an auxotrophic mutant of Mycobacterium tuberculosis defective in L-arginine biosynthesis.Semantic proximity Read ↗

Assessment of Metabolic Changes in Mycobacterium smegmatis Wild-Type and alr Mutant Strains: Evidence of a New Pathway of d-Alanine Biosynthesis.Semantic proximity Read ↗

Catabolic Ornithine Carbamoyltransferase Activity Facilitates Growth of Staphylococcus aureus in Defined Medium Lacking Glucose and ArginineSemantic proximity Read ↗

Arginine homeostasis in J774.1 macrophages in the context of Mycobacterium bovis BCG infection.Semantic proximity Read ↗

Isolation and characterization of Pseudomonas putida mutants affected in arginine, ornithine and citrulline catabolism: function of the arginine oxidase and arginine succinyltransferase pathways.Semantic proximity Read ↗

Staphylococcus aureus Does Not Synthesize Arginine from Proline under Physiological Conditions.Semantic proximity Read ↗

<i>Staphylococcus aureus</i> does not synthesize arginine from proline under physiological conditionsSemantic proximity Read ↗

Arginine Auxotrophy Affects Siderophore Biosynthesis and Attenuates Virulence of Aspergillus fumigatus.Semantic proximity Read ↗

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