Evidence map›Paper›PMID 28885767›Full record

ArticleChembiochem : a European journal of chemical biology2017

Creating Oxidase-Peroxidase Fusion Enzymes as a Toolbox for Cascade Reactions.

Dana I Colpa, Nikola Lončar, Mareike Schmidt, Marco W Fraaije

Open access · bronzeAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
8.1field-weighted citation impact, top 3% 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

9 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Enzyme Fusions in Biocatalysis: Coupling Reactions by Pairing Enzymes.Chembiochem : a European journal of chemical biology · 2019
    Review
  8. Article
  9. Creating Oxidase-Peroxidase Fusion Enzymes as a Toolbox for Cascade Reactions.Chembiochem : a European journal of chemical biology · 2017
    Article
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

4 authors at 1 institution in 1 country.

Dana I ColpaMolecular Enzymology Group, University of Groningen, Nijenborgh 4, 9747AG, Groningen, The Netherlands.
Nikola LončarGroningen Enzyme and Cofactor Collection (GECCO), University of Groningen, Nijenborgh 4, 9747AG, Groningen, The Netherlands.
Mareike SchmidtMolecular Enzymology Group, University of Groningen, Nijenborgh 4, 9747AG, Groningen, The Netherlands.
Marco W FraaijeMolecular Enzymology Group, University of Groningen, Nijenborgh 4, 9747AG, Groningen, The Netherlands.ORCID 0000-0001-6346-5014
University of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A set of bifunctional oxidase-peroxidases has been prepared by fusing four distinct oxidases to a peroxidase. Although such fusion enzymes have not been observed in nature, they could be expressed and purified in good yields. Characterization revealed that the artificial enzymes retained the capability to bind the two required cofactors and were catalytically active as oxidase and peroxidase. Peroxidase fusions of alditol oxidase and chitooligosaccharide oxidase could be used for the selective detection of xylitol and cellobiose with a detection limit in the low-micromolar range. The peroxidase fusions of eugenol oxidase and 5-hydroxymethylfurfural oxidase could be used for dioxygen-driven, one-pot, two-step cascade reactions to convert vanillyl alcohol into divanillin and eugenol into lignin oligomers. The designed oxidase-peroxidase fusions represent attractive biocatalysts that allow efficient biocatalytic cascade oxidations that only require molecular oxygen as an oxidant.

Indexed as

BenzaldehydesBenzyl AlcoholsCellobioseEugenolLigninMolecular StructureOxidoreductasesPeroxidaseXylitolBenzaldehydesBenzyl AlcoholsCellobioseEugenolLigninOxidoreductasesPeroxidasevanillinvanillyl alcoholXylitolbiocatalysisdomino reactionsenzymesprotein engineeringsensors

Identifiers

PMID28885767
PMCPMC5708271
OpenAlexW2752012772

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.