Evidence map›Paper›PMID 14525539›Full record

ArticleThe Biochemical journal2004

Functional characterization of alpha-glucan,water dikinase, the starch phosphorylating enzyme.

René Mikkelsen, Lone Baunsgaard, Andreas Blennow

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
10.4field-weighted citation impact, top 2% 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

33 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. A structural perspective on α-glucan catabolism in oxygenic phototrophs.The Plant journal : for cell and molecular biology · 2026
    Review
  3. Article
  4. Article
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  11. Review
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  13. Article
  14. Repression ofFrontiers in plant science · 2018
    Article
  15. Article
  16. Article
  17. Incorporation of phosphate into glycogen by glycogen synthase.Archives of biochemistry and biophysics · 2016
    Article
  18. Article
  19. Article
  20. Glycogen phosphorylation and Lafora disease.Molecular aspects of medicine · 2015
    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

3 authors.

René MikkelsenCenter for Molecular Plant Physiology (PlaCe), Plant Biochemistry Laboratory, Department of Plant Biology, The Royal Veterinary and Agricultural University, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Copenhagen, Denmark.
Lone Baunsgaard
Andreas Blennow

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

GWD (alpha-glucan,water dikinase) is the enzyme that catalyses the phosphorylation of starch by a dikinase-type reaction in which the beta-phosphate of ATP is transferred to either the C-6 or the C-3 position of the glycosyl residue of amylopectin. GWD shows similarity in both sequence and reaction mechanism to bacterial PPS (pyruvate,water dikinase) and PPDK (pyruvate,phosphate dikinase). Amino acid sequence alignments identified a conserved histidine residue located in the putative phosphohistidine domain of potato GWD. Site-directed mutagenesis of this histidine residue resulted in an inactive enzyme and loss of autophosphorylation. Native GWD is a homodimer and shows a strict requirement for the presence of alpha-1,6 branch points in its polyglucan substrate, and exhibits a sharp 20-fold increase in activity when the degree of polymerization is increased from 27.8 to 29.5. In spite of the high variability in the degree of starch phosphorylation, GWD proteins are ubiquitous in plants. The overall reaction mechanism of GWD is similar to that of PPS and PPDK, but the GWD family appears to have arisen after divergence of the plant kingdom. The nucleotide-binding domain of GWD exhibits a closer phylogenetic relationship to prokaryotic PPSs than to PPDKs.

Indexed as

Amino Acid SequenceCatalytic DomainGlucansHistidineHydrogen-Ion ConcentrationMutationPhosphorylationPhosphotransferasesPhylogenyPlant ProteinsProtein Structure, QuaternarySolanum tuberosumStarchSubstrate SpecificityTemperatureGlucansHistidinePhosphotransferasesPlant ProteinsStarch

Identifiers

PMID14525539
PMCPMC1223868
OpenAlexW2091463893

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.