Evidence map›Paper›PMID 28004799›Full record

ArticleScientific reports2016

Controlled Orientation of Active Sites in a Nanostructured Multienzyme Complex.

Sung In Lim, Byungseop Yang, Younghan Jung, Jaehyun Cha, Jinhwan Cho, Eun-Sil Choi, Yong Hwan Kim, Inchan Kwon

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

4 citing papers in PubMed, 22 citations in OpenAlex.

  1. Construction of a COChemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  2. Review
  3. Review
  4. Enzyme Fusions in Biocatalysis: Coupling Reactions by Pairing Enzymes.Chembiochem : a European journal of chemical biology · 2019
    Review
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

8 authors at 4 institutions in 2 countries.

Sung In LimDepartment of Chemical Engineering, University of Virginia, VA 22904, United States.
Byungseop YangSchool of Materials Science and Engineering, Gwangju Institute of Science and Technology (GIST), Gwangju, 61005, Republic of Korea.
Younghan JungSchool of Materials Science and Engineering, Gwangju Institute of Science and Technology (GIST), Gwangju, 61005, Republic of Korea.
Jaehyun ChaSchool of Materials Science and Engineering, Gwangju Institute of Science and Technology (GIST), Gwangju, 61005, Republic of Korea.
Jinhwan ChoSchool of Materials Science and Engineering, Gwangju Institute of Science and Technology (GIST), Gwangju, 61005, Republic of Korea.
Eun-Sil ChoiSchool of Materials Science and Engineering, Gwangju Institute of Science and Technology (GIST), Gwangju, 61005, Republic of Korea.
Yong Hwan KimSchool of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea.
Inchan KwonDepartment of Chemical Engineering, University of Virginia, VA 22904, United States.
Gwangju Institute of Science and Technology · KRChonnam National University · KRUlsan National Institute of Science and Technology · KRUniversity of Virginia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multistep cascade reactions in nature maximize reaction efficiency by co-assembling related enzymes. Such organization facilitates the processing of intermediates by downstream enzymes. Previously, the studies on multienzyme nanocomplexes assembled on DNA scaffolds demonstrated that closer interenzyme distance enhances the overall reaction efficiency. However, it remains unknown how the active site orientation controlled at nanoscale can have an effect on multienzyme reaction. Here, we show that controlled alignment of active sites promotes the multienzyme reaction efficiency. By genetic incorporation of a non-natural amino acid and two compatible bioorthogonal chemistries, we conjugated mannitol dehydrogenase to formate dehydrogenase with the defined active site arrangement with the residue-level accuracy. The study revealed that the multienzyme complex with the active sites directed towards each other exhibits four-fold higher relative efficiency enhancement in the cascade reaction and produces 60% more D-mannitol than the other complex with active sites directed away from each other.

Indexed as

Binding SitesCatalytic DomainDNAFormate DehydrogenasesKineticsMannitolMannitol DehydrogenasesMethanocaldococcusMultienzyme ComplexesNanostructuresOxygenProbabilityPseudomonas fluorescensSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationThiobacillusDNAFormate DehydrogenasesMannitolMannitol DehydrogenasesMultienzyme ComplexesOxygen

Identifiers

PMID28004799
PMCPMC5177890
OpenAlexW2561010798

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.