Evidence map›Paper›PMID 26858729›Full record

ArticleFrontiers in plant science2015

In vitro Biochemical Characterization of All Barley Endosperm Starch Synthases.

Jose A Cuesta-Seijo, Morten M Nielsen, Christian Ruzanski, Katarzyna Krucewicz, Sophie R Beeren, Maja G Rydhal, Yayoi Yoshimura, Alexander Striebeck, Mohammed S Motawia, William G T Willats and 1 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.0field-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

32 citing papers in PubMed, 55 citations in OpenAlex.

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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

11 authors at 2 institutions in 1 country.

Jose A Cuesta-SeijoCarlsberg Research Laboratory Copenhagen, Denmark.
Morten M NielsenCarlsberg Research Laboratory Copenhagen, Denmark.
Christian RuzanskiCarlsberg Research Laboratory Copenhagen, Denmark.
Katarzyna KrucewiczCarlsberg Research Laboratory Copenhagen, Denmark.
Sophie R BeerenCarlsberg Research Laboratory Copenhagen, Denmark.
Maja G RydhalDepartment of Plant and Environmental Sciences, University of Copenhagen Frederiksberg, Copenhagen, Denmark.
Yayoi YoshimuraCarlsberg Research Laboratory Copenhagen, Denmark.
Alexander StriebeckCarlsberg Research Laboratory Copenhagen, Denmark.
Mohammed S MotawiaDepartment of Plant and Environmental Sciences, University of Copenhagen Frederiksberg, Copenhagen, Denmark.
William G T WillatsDepartment of Plant and Environmental Sciences, University of Copenhagen Frederiksberg, Copenhagen, Denmark.
Monica M PalcicCarlsberg Research Laboratory Copenhagen, Denmark.
Carlsberg Laboratory · DKUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Starch is the main storage polysaccharide in cereals and the major source of calories in the human diet. It is synthesized by a panel of enzymes including five classes of starch synthases (SSs). While the overall starch synthase (SS) reaction is known, the functional differences between the five SS classes are poorly understood. Much of our knowledge comes from analyzing mutant plants with altered SS activities, but the resulting data are often difficult to interpret as a result of pleitropic effects, competition between enzymes, overlaps in enzyme activity and disruption of multi-enzyme complexes. Here we provide a detailed biochemical study of the activity of all five classes of SSs in barley endosperm. Each enzyme was produced recombinantly in E. coli and the properties and modes of action in vitro were studied in isolation from other SSs and other substrate modifying activities. Our results define the mode of action of each SS class in unprecedented detail; we analyze their substrate selection, temperature dependence and stability, substrate affinity and temporal abundance during barley development. Our results are at variance with some generally accepted ideas about starch biosynthesis and might lead to the reinterpretation of results obtained in planta. In particular, they indicate that granule bound SS is capable of processive action even in the absence of a starch matrix, that SSI has no elongation limit, and that SSIV, believed to be critical for the initiation of starch granules, has maltoligosaccharides and not polysaccharides as its preferred substrates.

Indexed as

affinitybarleybiochemical characterizationexpression levelskineticsstabilitystarch synthasessubstrate specificity

Identifiers

PMID26858729
PMCPMC4730117
OpenAlexW2277370993

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.