Evidence map›Paper›PMID 28922469›Full record

ArticleBiotechnology and bioengineering2018

One pot synthesis of GDP-mannose by a multi-enzyme cascade for enzymatic assembly of lipid-linked oligosaccharides.

Thomas F T Rexer, Anna Schildbach, Jan Klapproth, Angelika Schierhorn, Reza Mahour, Markus Pietzsch, Erdmann Rapp, Udo Reichl

Open access · hybridAbstract read
In one paragraph

Article in Biotechnology and bioengineering, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Cell-freeFrontiers in molecular biosciences · 2023
    Article
  8. Article
  9. Cell-Free Multi-Enzyme Synthesis and Purification of Uridine Diphosphate Galactose.Chembiochem : a European journal of chemical biology · 2022
    Article
  10. Review
  11. Article
  12. Enzymatic Synthesis of Glycans and Glycoconjugates.Advances in biochemical engineering/biotechnology · 2021
    Review
  13. Biospektrum : Zeitschrift der Gesellschaft fur Biologishe Chemie (GBCH) und der Vereinigung fur Allgemeine und Angewandte Mikrobiologie (VAAM) · 2021
    Review
  14. Cell-Free Glycoengineering of the Recombinant SARS-CoV-2 Spike Glycoprotein.Frontiers in bioengineering and biotechnology · 2021
    Article
  15. Article
  16. Nucleotide Sugars in Chemistry and Biology.Molecules (Basel, Switzerland) · 2020
    Review
  17. Review
  18. Article
  19. Article
  20. Article
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

8 authors at 2 institutions in 1 country.

Thomas F T RexerMax Planck Institute for Dynamics of Complex Technical Systems, Bioprocess Engineering, Magdeburg, Germany.ORCID http://orcid.org/0000-0002-2105-1283
Anna SchildbachDepartment of Downstream Processing, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Jan KlapprothDepartment of Downstream Processing, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Angelika SchierhornInstitute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Reza MahourMax Planck Institute for Dynamics of Complex Technical Systems, Bioprocess Engineering, Magdeburg, Germany.
Markus PietzschDepartment of Downstream Processing, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.
Erdmann RappMax Planck Institute for Dynamics of Complex Technical Systems, Bioprocess Engineering, Magdeburg, Germany.
Udo ReichlMax Planck Institute for Dynamics of Complex Technical Systems, Bioprocess Engineering, Magdeburg, Germany.
Martin Luther University Halle-Wittenberg · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation of proteins is a key function of the biosynthetic-secretory pathway in the endoplasmic reticulum (ER) and Golgi apparatus. Glycosylated proteins play a crucial role in cell trafficking and signaling, cell-cell adhesion, blood-group antigenicity, and immune response. In addition, the glycosylation of proteins is an important parameter in the optimization of many glycoprotein-based drugs such as monoclonal antibodies. In vitro glycoengineering of proteins requires glycosyltransferases as well as expensive nucleotide sugars. Here, we present a designed pathway consisting of five enzymes, glucokinase (Glk), phosphomannomutase (ManB), mannose-1-phosphate-guanyltransferase (ManC), inorganic pyrophosphatase (PmPpA), and 1-domain polyphosphate kinase 2 (1D-Ppk2) expressed in E. coli for the cell-free production and regeneration of GDP-mannose from mannose and polyphosphate with catalytic amounts of GDP and ADP. It was shown that GDP-mannose is produced at various conditions, that is pH 7-8, temperature 25-35°C and co-factor concentrations of 5-20 mM MgCl

Indexed as

CoenzymesEnzymesEscherichia coliGene ExpressionGuanosine Diphosphate MannoseHydrogen-Ion ConcentrationLipopolysaccharidesMagnesium ChlorideMannosePolyphosphatesRecombinant ProteinsTemperatureCoenzymesEnzymesGuanosine Diphosphate Mannoselipid-linked oligosaccharidesLipopolysaccharidesMagnesium ChlorideMannosePolyphosphatesRecombinant Proteinscell-free synthesisenzymatic catalysisin vitro N-glycoengineeringkinetic modelingnucleotide sugar regeneration

Identifiers

PMID28922469
PMCPMC5765510
OpenAlexW2754055217

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.