Evidence map›Paper›PMID 41638429›Full record

ArticleThe Journal of biological chemistry2026

Dissecting a two-domain alginate lyase of family PL6 reveals a mechanistic basis for substrate specificity and enzyme activity.

Mikkel Madsen, Mette E Rønne, Agnes B Petersen, Tobias Tandrup, Bo Pilgaard, Jesper Holck, Finn L Aachmann, Casper Wilkens, Leesa J Klau, Birte Svensson

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Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

10 authors.

Mikkel MadsenEnzyme and Protein Chemistry, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark. Electronic address: m.madsen_bio@outlook.com.
Mette E RønneEnzyme and Protein Chemistry, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark; Applied Molecular Enzyme Chemistry, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark.
Agnes B PetersenDepartment of Biotechnology and Food Science, Norwegian Biopolymer Laboratory (NOBIPOL), NTNU Norwegian University of Science and Technology, Trondheim, Norway.
Tobias TandrupEnzyme and Protein Chemistry, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark.
Bo PilgaardEnzyme Discovery, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark.
Jesper HolckEnzyme Technology, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark.
Finn L AachmannDepartment of Biotechnology and Food Science, Norwegian Biopolymer Laboratory (NOBIPOL), NTNU Norwegian University of Science and Technology, Trondheim, Norway.
Casper WilkensStructural Enzymology, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark.
Leesa J KlauDepartment of Biotechnology and Food Science, Norwegian Biopolymer Laboratory (NOBIPOL), NTNU Norwegian University of Science and Technology, Trondheim, Norway.
Birte SvenssonEnzyme and Protein Chemistry, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kongens Lyngby, Denmark. Electronic address: bis@bio.dtu.dk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alginate lyases (ALs) cleave 4-O-glycosidic linkages in alginate, composed of mannuronate (M) and guluronate (G) residues via β-elimination with preference for either one or several M-M, M-G, G-M, G-G linkages. ALs in polysaccharide lyase family 6 (PL6) present different specificities and modes of action and contain either one or two parallel β-helix domains. About half of almost 600 PL6 sequences are of the two-domain type, all located in the phyla Pseudomonadota and Bacteroidota. Here, functional roles are described for the N- and C-terminal domains (NTD and CTD) using BoPL6, a two-domain AL from the human gut bacterium Bacteroides ovatus CP926, which is specific for G in subsite +1. The NTD contains the catalytic site, but BoPL6-NTD markedly preferred the model substrate polyMG and cleaved M-G bonds in endo-mode, whereas the NTD + CTD mixture, similarly to BoPL6, acted with highest activity on model substrate polyG in exo-mode, verified by time-resolved

Indexed as

BacteroidesPolysaccharide-LyasesProtein DomainsSubstrate Specificitypoly(beta-D-mannuronate) lyasePolysaccharide-Lyasesalginate lyasecarbohydrateenzyme mechanismmode of actionparallel β-helix domainsphylogeneticsprotein domainstructure–function relationshipsubstrate specificityβ-elimination

Identifiers

PMID41638429
PMCPMC12992946

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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.