Evidence map›Paper›PMID 21257776›Full record

ArticleJournal of bacteriology2011

Corynebacterium glutamicum as a host for synthesis and export of D-Amino Acids.

Norma Stäbler, Tadao Oikawa, Michael Bott, Lothar Eggeling

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.7field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. l-Alanine Exporter AlaE Functions as One of the d-Alanine Exporters inInternational journal of molecular sciences · 2023
    Article
  6. Customized chitooligosaccharide production-controlling their lengthFrontiers in bioengineering and biotechnology · 2022
    Article
  7. Review
  8. Recent Advances of L-ornithine Biosynthesis in Metabolically EngineeredFrontiers in bioengineering and biotechnology · 2019
    Review
  9. Metabolite secretion in microorganisms: the theory of metabolic overflow put to the test.Metabolomics : Official journal of the Metabolomic Society · 2018
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Norma StäblerInstitut für Bio- und Geowissenschaften, IBG-1: Biotechnologie, Forschungszentrum Jülich, D-52425 Jülich, Germany. l.eggeling@fz-juelich.de
Tadao Oikawa
Michael Bott
Lothar Eggeling
Forschungszentrum Jülich · DEKansai University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A number of d-amino acids occur in nature, and there is growing interest in their function and metabolism, as well as in their production and use. Here we use the well-established l-amino-acid-producing bacterium Corynebacterium glutamicum to study whether d-amino acid synthesis is possible and whether mechanisms for the export of these amino acids exist. In contrast to Escherichia coli, C. glutamicum tolerates d-amino acids added extracellularly. Expression of argR (encoding the broad-substrate-specific racemase of Pseudomonas taetrolens) with its signal sequence deleted results in cytosolic localization of ArgR in C. glutamicum. The isolated enzyme has the highest activity with lysine (100%) but also exhibits activity with serine (2%). Upon overexpression of argR in an l-arginine, l-ornithine, or l-lysine producer, equimolar mixtures of the d- and l-enantiomers accumulated extracellularly. Unexpectedly, argR overexpression in an l-serine producer resulted in extracellular accumulation of a surplus of d-serine (81 mM d-serine and 37 mM l-serine) at intracellular concentrations of 125 mM d-serine plus 125 mM l-serine. This points to a nonlimiting ArgR activity for intracellular serine racemization and to the existence of a specific export carrier for d-serine. Export of d-lysine relies fully on the presence of lysE, encoding the exporter for l-lysine, which is apparently promiscuous with respect to the chirality of lysine. These data show that d-amino acids can also be produced with C. glutamicum and that in special cases, due to specific carriers, even a preferential extracellular accumulation of this enantiomer is possible.

Indexed as

Amino Acid IsomerasesAmino AcidsBacterial ProteinsCorynebacterium glutamicumCulture MediaCytosolGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicLysineProtein TransportPseudomonasSerineAmino Acid IsomerasesAmino AcidsBacterial ProteinsCulture MediaLysineSerine

Identifiers

PMID21257776
PMCPMC3067661
OpenAlexW2048422381

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.