Evidence map›Paper›PMID 26520834›Full record

ArticlePlant molecular biology2016

New insight into the catalytic properties of rice sucrose synthase.

Yu-Chiao Huang, Erh-Chieh Hsiang, Chien-Chih Yang, Ai-Yu Wang

Abstract read
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In one paragraph

Article in Plant molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

13 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Molecular identification and expression analysis of five sucrose synthase genes inPhysiology and molecular biology of plants : an international journal of functional plant biology · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. An Overview of Sucrose Synthases in Plants.Frontiers in plant science · 2019
    Review
  12. Thermo-responsive allele ofBreeding science · 2018
    Article
  13. 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

4 authors at 1 institution in 1 country.

Yu-Chiao HuangDepartment of Biochemical Science and Technology, National Taiwan University, No. 1, Sec. 4, Roosevelt Road, Taipei, 10617, Taiwan.
Erh-Chieh HsiangDepartment of Biochemical Science and Technology, National Taiwan University, No. 1, Sec. 4, Roosevelt Road, Taipei, 10617, Taiwan.
Chien-Chih YangDepartment of Biochemical Science and Technology, National Taiwan University, No. 1, Sec. 4, Roosevelt Road, Taipei, 10617, Taiwan. ccyang@ntu.edu.tw.
Ai-Yu WangDepartment of Biochemical Science and Technology, National Taiwan University, No. 1, Sec. 4, Roosevelt Road, Taipei, 10617, Taiwan. aywang@ntu.edu.tw.
National Taiwan University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sucrose synthase (SuS), which catalyzes the reversible conversion of sucrose and uridine diphosphate (UDP) into fructose and UDP-glucose, is a key enzyme in sucrose metabolism in higher plants. SuS belongs to family 4 of the glycosyltransferases (GT4) and contains an E-X7-E motif that is conserved in members of GT4 and two other GT families. To gain insight into the roles of this motif in rice sucrose synthase 3 (RSuS3), the two conserved glutamate residues (E678 and E686) in this motif and a phenylalanine residue (F680) that resides between the two glutamate residues were changed by site-directed mutagenesis. All mutant proteins maintained their tetrameric conformation. The mutants E686D and F680Y retained partial enzymatic activity and the mutants E678D, E678Q, F680S, and E686Q were inactive. Substrate binding assays indicated that UDP and fructose, respectively, were the leading substrates in the sucrose degradation and synthesis reactions of RSuS3. Mutations on E678, F680, and E686 affected the binding of fructose, but not of UDP. The results indicated that E678, F680, and E686 in the E-X7-E motif of RSuS3 are essential for the activity of the enzyme and the sequential binding of substrates. The sequential binding of the substrates implied that the reaction catalyzed by RSuS can be controlled by the availability of fructose and UDP, depending on the metabolic status of a tissue.

Indexed as

Models, MolecularAmino Acid SequenceAmino Acid SubstitutionBiocatalysisFructoseGlucosyltransferasesKineticsMolecular Sequence DataMutagenesis, Site-DirectedOryzaPlant ProteinsProtein Structure, TertiaryRecombinant ProteinsSequence AlignmentSubstrate SpecificitySucroseFructoseGlucosyltransferasesPlant ProteinsRecombinant ProteinsSucrosesucrose synthaseUridine DiphosphateUridine Diphosphate GlucoseEnzyme kineticsMolecular modelingSite-directed mutagenesisSubstrate bindingSucrose synthase

Identifiers

PMID26520834
OpenAlexW1961686464

What OpenQuestion holds

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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.