Evidence map›Paper›PMID 15240254›Full record

ArticleApplied and environmental microbiology2004

Impact of heterologous expression of Escherichia coli UDP-glucose pyrophosphorylase on trehalose and glycogen synthesis in Corynebacterium glutamicum.

Leandro Padilla, Susanne Morbach, Reinhard Krämer, Eduardo Agosin

Abstract read
In one paragraph

Article in Applied and environmental microbiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

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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

14 citing papers in PubMed.

  1. Article
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  4. Review
  5. Article
  6. Two Homologous Enzymes of the GalU Family inInternational journal of molecular sciences · 2019
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  11. 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.

Leandro PadillaDepartmento de Ingeniería y Bioprocesos, Escuela de Ingeniería, Pontificia Universidad Católica de Chile, Casilla 306 Correo 22, Santiago, Chile.
Susanne Morbach
Reinhard Krämer
Eduardo Agosin

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trehalose is a disaccharide with a wide range of applications in the food industry. We recently proposed a strategy for trehalose production based on improved strains of the gram-positive bacterium Corynebacterium glutamicum. This microorganism synthesizes trehalose through two major pathways, OtsBA and TreYZ, by using UDP-glucose and ADP-glucose, respectively, as the glucosyl donors. In this paper we describe improvement of the UDP-glucose supply through heterologous expression in C. glutamicum of the UDP-glucose pyrophosphorylase gene from Escherichia coli, either expressed alone or coexpressed with the E. coli ots genes (galU otsBA synthetic operon). The impact of such expression on trehalose accumulation and excretion, glycogen accumulation, and the growth pattern of new recombinant strains is described. Expression of the galU otsBA synthetic operon resulted in a sixfold increase in the accumulated and excreted trehalose relative to that in a wild-type strain. Surprisingly, single expression of galU also resulted in an increase in the accumulated trehalose. This increase in trehalose synthesis was abolished upon deletion of the TreYZ pathway. These results proved that UDP-glucose has an important role not only in the OtsBA pathway but also in the TreYZ pathway.

Indexed as

CorynebacteriumEscherichia coliEscherichia coli ProteinsGlucosyltransferasesGlycogenOperonPhosphoric Monoester HydrolasesTrehaloseUridine Diphosphate GlucoseUTP-Glucose-1-Phosphate UridylyltransferaseEscherichia coli ProteinsgalU protein, E coliGlucosyltransferasesGlycogenPhosphoric Monoester HydrolasesTrehalosetrehalose-6-phosphate synthasetrehalose-phosphataseUridine Diphosphate GlucoseUTP-Glucose-1-Phosphate Uridylyltransferase

Identifiers

PMID15240254
PMCPMC444832

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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.