Evidence map›Paper›PMID 27137180›Full record

ReviewCellular and molecular life sciences : CMLS2016

Structure and function of α-glucan debranching enzymes.

Marie Sofie Møller, Anette Henriksen, Birte Svensson

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2016. 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
8.5field-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

32 citing papers in PubMed, 88 citations in OpenAlex.

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  11. Origin and evolution of the main starch biosynthetic enzymes.Synthetic and systems biotechnology · 2023
    Article
  12. BoGH13ACellular and molecular life sciences : CMLS · 2023
    Article
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  18. Aspects and Recent Trends in Microbial α-Amylase: a Review.Applied biochemistry and biotechnology · 2021
    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

3 authors at 2 institutions in 1 country.

Marie Sofie MøllerEnzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, 2800, Kongens Lyngby, Denmark. mariesofiemoller@gmail.com.
Anette HenriksenGlobal Research Unit, Department of Large Protein Biophysics and Formulation, Novo Nordisk A/S, Novo Nordisk Park, 2760, Måløv, Denmark.
Birte SvenssonEnzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, 2800, Kongens Lyngby, Denmark.
Technical University of Denmark · DKNovo Nordisk (Denmark) · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Glucan debranching enzymes hydrolyse α-1,6-linkages in starch/glycogen, thereby, playing a central role in energy metabolism in all living organisms. They belong to glycoside hydrolase families GH13 and GH57 and several of these enzymes are industrially important. Nine GH13 subfamilies include α-glucan debranching enzymes; isoamylase and glycogen debranching enzymes (GH13_11); pullulanase type I/limit dextrinase (GH13_12-14); pullulan hydrolase (GH13_20); bifunctional glycogen debranching enzyme (GH13_25); oligo-1 and glucan-1,6-α-glucosidases (GH13_31); pullulanase type II (GH13_39); and α-amylase domains (GH13_41) in two-domain amylase-pullulanases. GH57 harbours type II pullulanases. Specificity differences, domain organisation, carbohydrate binding modules, sequence motifs, three-dimensional structures and specificity determinants are discussed. The phylogenetic analysis indicated that GH13_39 enzymes could represent a "missing link" between the strictly α-1,6-specific debranching enzymes and the enzymes with dual specificity and α-1,4-linkage preference.

Indexed as

GlucansGlycogenGlycoside HydrolasesIndustryStructural Homology, ProteinGlucansGlycogenGlycoside HydrolasespullulanaseCarbohydrate binding modulesDomain architectureGlycoside hydrolase family 13 subfamiliesMulti-domain three-dimensional structurePhylogenySequence motifs and determinantsStructure–function relationshipSubstrate specificity

Identifiers

PMID27137180
PMCPMC11108273
OpenAlexW2346206834

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.