Evidence map›Paper›PMID 17496125›Full record

ArticleEukaryotic cell2007

Two novel, putatively cell wall-associated and glycosylphosphatidylinositol-anchored alpha-glucanotransferase enzymes of Aspergillus niger.

R M van der Kaaij, X-L Yuan, A Franken, A F J Ram, P J Punt, M J E C van der Maarel, L Dijkhuizen

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

17 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Novel Design of an α-Amylase with an N-Terminal CBM20 inMolecules (Basel, Switzerland) · 2023
    Article
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  7. Deletion of theMicroorganisms · 2020
    Article
  8. Review
  9. Function and Biosynthesis of Cell Wall α-1,3-Glucan in Fungi.Journal of fungi (Basel, Switzerland) · 2017
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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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

7 authors at 2 institutions in 1 country.

R M van der KaaijCentre for Carbohydrate Bioprocessing, TNO-University of Groningen, Haren, The Netherlands.
X-L Yuan
A Franken
A F J Ram
P J Punt
M J E C van der Maarel
L Dijkhuizen
Leiden University · NLUniversity of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the genome sequence of Aspergillus niger CBS 513.88, three genes were identified with high similarity to fungal alpha-amylases. The protein sequences derived from these genes were different in two ways from all described fungal alpha-amylases: they were predicted to be glycosylphosphatidylinositol anchored, and some highly conserved amino acids of enzymes in the alpha-amylase family were absent. We expressed two of these enzymes in a suitable A. niger strain and characterized the purified proteins. Both enzymes showed transglycosylation activity on donor substrates with alpha-(1,4)-glycosidic bonds and at least five anhydroglucose units. The enzymes, designated AgtA and AgtB, produced new alpha-(1,4)-glycosidic bonds and therefore belong to the group of the 4-alpha-glucanotransferases (EC 2.4.1.25). Their reaction products reached a degree of polymerization of at least 30. Maltose and larger maltooligosaccharides were the most efficient acceptor substrates, although AgtA also used small nigerooligosaccharides containing alpha-(1,3)-glycosidic bonds as acceptor substrate. An agtA knockout of A. niger showed an increased susceptibility towards the cell wall-disrupting compound calcofluor white, indicating a cell wall integrity defect in this strain. Homologues of AgtA and AgtB are present in other fungal species with alpha-glucans in their cell walls, but not in yeast species lacking cell wall alpha-glucan. Possible roles for these enzymes in the synthesis and/or maintenance of the fungal cell wall are discussed.

Indexed as

Aspergillus nigerAmino Acid SequenceBase SequenceCell WallFungal ProteinsGlycogen Debranching Enzyme SystemGlycosylphosphatidylinositolsIsoenzymesMolecular Sequence DataOligosaccharidesPhylogenyRecombinant Fusion ProteinsSequence AlignmentSequence Homology, Amino Acid4 alpha-glucanotransferaseFungal ProteinsGlycogen Debranching Enzyme SystemGlycosylphosphatidylinositolsIsoenzymesmaltooligosaccharidesOligosaccharidesRecombinant Fusion Proteins

Identifiers

PMID17496125
PMCPMC1951109
OpenAlexW2146564683

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.