Evidence map›Paper›PMID 26881499›Full record

ArticleOrganic & biomolecular chemistry2016

One-pot multienzyme (OPME) systems for chemoenzymatic synthesis of carbohydrates.

Hai Yu, Xi Chen

Abstract read
In one paragraph

Article in Organic & biomolecular chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
16.1field-weighted citation impact, top 1% 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

49 citing papers in PubMed, 142 citations in OpenAlex.

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  17. Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.International journal of molecular sciences · 2022
    Review
  18. Cell-Free Multi-Enzyme Synthesis and Purification of Uridine Diphosphate Galactose.Chembiochem : a European journal of chemical biology · 2022
    Article
  19. Article
  20. Review
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

2 authors at 2 institutions in 1 country.

Hai YuDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA. xiichen@ucdavis.edu.
Xi ChenDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA. xiichen@ucdavis.edu.
University of California, Davis · USUniversity of California System · US

Funding

Oligosaccharides as antimicrobials and prebioticsR01HD065122 · NICHD · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI · 2010 to 2013
$1.8M
New chemoenzymatic methods for synthesizing complex carbohydratesR01GM094523 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI · 2013 to 2016
$1.2M
NICHD NIH HHS R01 HD065122NICHD NIH HHS R01HD065122NIGMS NIH HHS R01 GM094523NIGMS NIH HHS R01GM094523
6 · The paper itself

Abstract

Glycosyltransferase-catalyzed enzymatic and chemoenzymatic syntheses are powerful approaches for the production of oligosaccharides, polysaccharides, glycoconjugates, and their derivatives. Enzymes involved in the biosynthesis of sugar nucleotide donors can be combined with glycosyltransferases in one pot for efficient production of the target glycans from simple monosaccharides and acceptors. The identification of enzymes involved in the salvage pathway of sugar nucleotide generation has greatly facilitated the development of simplified and efficient one-pot multienzyme (OPME) systems for synthesizing major glycan epitopes in mammalian glycomes. The applications of OPME methods are steadily gaining popularity mainly due to the increasing availability of wild-type and engineered enzymes. Substrate promiscuity of these enzymes and their mutants allows OPME synthesis of carbohydrates with naturally occurring post-glycosylational modifications (PGMs) and their non-natural derivatives using modified monosaccharides as precursors. The OPME systems can be applied in sequence for synthesizing complex carbohydrates. The sequence of the sequential OPME processes, the glycosyltransferase used, and the substrate specificities of the glycosyltransferases define the structures of the products. The OPME and sequential OPME strategies can be extended to diverse glycans in other glycomes when suitable enzymes with substrate promiscuity become available. This Perspective summarizes the work of the authors and collaborators on the development of glycosyltransferase-based OPME systems for carbohydrate synthesis. Future directions are also discussed.

Indexed as

CarbohydratesCarbohydrate SequenceEnzymesMolecular Sequence DataCarbohydratesEnzymes

Identifiers

PMID26881499
PMCPMC4795158
OpenAlexW2258747568

What OpenQuestion holds

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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.