Evidence map›Paper›PMID 42218266›Full record

ArticleScientific reports2026

One-site polarity switch enhances catalytic efficiency and stability of D-allulose 3-epimerase via flexibility-rigidity rebalancing.

Fina Amreta Laksmi, Yudhi Nugraha, Kenny Lischer, Khaerunnisa, David Herawan, Ario Betha Juanssilfero, Des Saputro Wibowo, Isa Nuryana, Syahputra Wibowo, Keni Vidilaseris and 1 more

Abstract read
In one paragraph

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

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Fina Amreta LaksmiDirectorate of Laboratory Management, Research Facilities, and Science Technology Parks, Deputy for Infrastructure Research and Innovation, National Research and Innovation Agency, Jalan Raya Bogor KM 46, Cibinong, Bogor, West Java, 16911, Indonesia. fina.amreta.laksmi@gmail.com.ORCID http://orcid.org/0000-0001-6887-2276
Yudhi NugrahaResearch Center for Molecular Biology Eijkman, National Research and Innovation Agency, Jalan Raya Bogor KM 46, Cibinong , Bogor, West Java, 16911, Indonesia.ORCID http://orcid.org/0000-0003-1186-4093
Kenny LischerBioprocess Engineering, Department of Chemical Engineering, Faculty of Engineering, Universitas Indonesia, Depok, West Java, 16424, Indonesia. lischer.kenny@ui.ac.id.ORCID http://orcid.org/0000-0001-8725-4836
KhaerunnisaBiotechnology Program, Graduate School, IPB University, Bogor, West Java, Indonesia.ORCID http://orcid.org/0009-0009-4400-5077
David HerawanChemical Engineering, Department of Chemical Engineering, Faculty of Engineering, Universitas Indonesia, Depok, West Java, 16424, Indonesia.ORCID http://orcid.org/0009-0009-7440-6357
Ario Betha JuanssilferoResearch Center for Environmental and Clean Technology, National Research and Innovation Agency, Jalan Raya Bogor KM 46, Cibinong, Bogor, West Java, 16911, Indonesia.ORCID http://orcid.org/0000-0002-6837-9681
Des Saputro WibowoResearch Center for Applied Microbiology, National Research and Innovation Agency, Jalan Raya Bogor KM 46, Cibinong, Bogor, West Java, 16911, Indonesia.ORCID http://orcid.org/0009-0009-7363-7612
Isa NuryanaResearch Center for Applied Microbiology, National Research and Innovation Agency, Jalan Raya Bogor KM 46, Cibinong, Bogor, West Java, 16911, Indonesia.ORCID http://orcid.org/0000-0002-6128-7661
Syahputra WibowoResearch Center for Molecular Biology Eijkman, National Research and Innovation Agency, Jalan Raya Bogor KM 46, Cibinong , Bogor, West Java, 16911, Indonesia.
Keni VidilaserisMolecular and Integrative Biosciences Research Programme, Faculty of Biological and Environmental Sciences, University of Helsinki, 00014, Helsinki, Finland.ORCID http://orcid.org/0000-0002-6453-6600
Mulyorini RahayuningsihBiotechnology Program, Graduate School, IPB University, Bogor, West Java, Indonesia.

Funding

Indonesia Toray Science Foundation Fiscal year 2022Research and innovation for advanced Indonesia (RIIM) programme, the National Research and Innovation Agency (BRIN) and Indonesia Endowment Fund for Education (LPDP) NKB-945/UN2.RST/HKP.05.00/2024
6 · The paper itself

Abstract

The structural foundation of enzyme efficiency frequently resides in the subtle equilibrium between localized flexibility and overarching rigidity. This study presents evidence that a singular amino acid alteration (E35H) in Arthrobacter psychrolactophilus D-allulose 3-epimerase (ApDAEase) enhances catalytic efficiency by 1.4 times relative to the wild-type, attributed to a 1.3-fold reduction in K

Indexed as

ArthrobacterCarbohydrate EpimerasesAmino Acid SubstitutionCatalysisCatalytic DomainEnzyme StabilityHydrogen BondingKineticsMolecular Dynamics SimulationCarbohydrate EpimerasesArthrobacter psychrolactophilusCatalytic activityd-allulosed-allulose 3-epimeraseRational mutationThermostability

Identifiers

PMID42218266
PMCPMC13458763

What OpenQuestion holds

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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.