Evidence map›Paper›PMID 23610417›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Broadening the scope of glycosyltransferase-catalyzed sugar nucleotide synthesis.

Richard W Gantt, Pauline Peltier-Pain, Shanteri Singh, Maoquan Zhou, Jon S Thorson

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
–field-weighted citation impact
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

41 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Synthesis of triazole bridgedRSC advances · 2024
    Article
  8. Article
  9. Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023
    Review
  10. Article
  11. Rethinking Biosynthesis of Aclacinomycin A.Molecules (Basel, Switzerland) · 2023
    Review
  12. Structure-function and engineering of plant UDP-glycosyltransferase.Computational and structural biotechnology journal · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

5 authors.

Richard W GanttPharmaceutical Sciences Division, School of Pharmacy, Wisconsin Center for Natural Products Research, University of Wisconsin, Madison, WI 53705-2222, USA.
Pauline Peltier-Pain
Shanteri Singh
Maoquan Zhou
Jon S Thorson

Funding

Kentucky Center for Clinical and Translational ScienceUL1TR000117 · NCATS · UNIVERSITY OF KENTUCKY · PI KERN, PHILIP A · 2012 to 2015
$13.3M
In Vitro Glycorandomization of Natural ProductsR37AI052218 · NIAID · UNIVERSITY OF KENTUCKY · PI THORSON, JON SCOTT · 2012 to 2021
$4.0M
In Vitro Glycorandomization of Natural ProductsR01AI052218 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI THORSON, JON SCOTT · 2002 to 2011
$3.8M
NCATS NIH HHS UL1 TR000117NCATS NIH HHS UL1TR000117NIAID NIH HHS AI52218NIAID NIH HHS R01 AI052218NIAID NIH HHS R37 AI052218
6 · The paper itself

Abstract

We described the integration of the general reversibility of glycosyltransferase-catalyzed reactions, artificial glycosyl donors, and a high throughput colorimetric screen to enable the engineering of glycosyltransferases for combinatorial sugar nucleotide synthesis. The best engineered catalyst from this study, the OleD Loki variant, contained the mutations P67T/I112P/T113M/S132F/A242I compared with the OleD wild-type sequence. Evaluated against the parental sequence OleD TDP16 variant used for screening, the OleD Loki variant displayed maximum improvements in k(cat)/K(m) of >400-fold and >15-fold for formation of NDP-glucoses and UDP-sugars, respectively. This OleD Loki variant also demonstrated efficient turnover with five variant NDP acceptors and six variant 2-chloro-4-nitrophenyl glycoside donors to produce 30 distinct NDP-sugars. This study highlights a convenient strategy to rapidly optimize glycosyltransferase catalysts for the synthesis of complex sugar nucleotides and the practical synthesis of a unique set of sugar nucleotides.

Indexed as

CatalysisGenetic VariationGlycomicsGlycosyltransferasesHigh-Throughput Screening AssaysMolecular ConformationMutationNitrophenolsNucleoside Diphosphate SugarsProtein EngineeringRecombination, GeneticUridine Diphosphate Sugars4-nitrophenylGlycosyltransferasesNitrophenolsNucleoside Diphosphate SugarsUridine Diphosphate Sugarscarbohydrateenzymeglycobiologyprotein engineering

Identifiers

PMID23610417
PMCPMC3651490

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.