Evidence map›Paper›PMID 24614932›Full record

ArticlePloS one2014

Engineering of pyranose dehydrogenase for increased oxygen reactivity.

Iris Krondorfer, Katharina Lipp, Dagmar Brugger, Petra Staudigl, Christoph Sygmund, Dietmar Haltrich, Clemens K Peterbauer

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
4.7field-weighted citation impact, top 6% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Innovation and tinkering in the evolution of oxidases.Protein science : a publication of the Protein Society · 2022
    Review
  4. Article
  5. Review
  6. Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass.Microbiology and molecular biology reviews : MMBR · 2018
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

7 authors at 2 institutions in 1 country.

Iris KrondorferFood Biotechnology Laboratory, Department of Food Science and Technology, University of Natural Resources and Life Sciences, Vienna, Austria.
Katharina LippFood Biotechnology Laboratory, Department of Food Science and Technology, University of Natural Resources and Life Sciences, Vienna, Austria; University of Applied Sciences Wiener Neustadt - Campus Tulln, Tulln, Austria.
Dagmar BruggerFood Biotechnology Laboratory, Department of Food Science and Technology, University of Natural Resources and Life Sciences, Vienna, Austria.
Petra StaudiglFood Biotechnology Laboratory, Department of Food Science and Technology, University of Natural Resources and Life Sciences, Vienna, Austria.
Christoph SygmundFood Biotechnology Laboratory, Department of Food Science and Technology, University of Natural Resources and Life Sciences, Vienna, Austria.
Dietmar HaltrichFood Biotechnology Laboratory, Department of Food Science and Technology, University of Natural Resources and Life Sciences, Vienna, Austria.
Clemens K PeterbauerFood Biotechnology Laboratory, Department of Food Science and Technology, University of Natural Resources and Life Sciences, Vienna, Austria.
BOKU University · ATFachhochschule Wiener Neustadt · AT

Funding

Austrian Science Fund FWF P 22094Austrian Science Fund FWF W 1224
6 · The paper itself

Abstract

Pyranose dehydrogenase (PDH), a member of the GMC family of flavoproteins, shows a very broad sugar substrate specificity but is limited to a narrow range of electron acceptors and reacts extremely slowly with dioxygen as acceptor. The use of substituted quinones or (organo)metals as electron acceptors is undesirable for many production processes, especially of food ingredients. To improve the oxygen reactivity, site-saturation mutagenesis libraries of twelve amino acids around the active site of Agaricus meleagris PDH were expressed in Saccharomyces cerevisiae. We established high-throughput screening assays for oxygen reactivity and standard dehydrogenase activity using an indirect Amplex Red/horseradish peroxidase and a DCIP/D-glucose based approach. The low number of active clones confirmed the catalytic role of H512 and H556. Only one position was found to display increased oxygen reactivity. Histidine 103, carrying the covalently linked FAD cofactor in the wild-type, was substituted by tyrosine, phenylalanine, tryptophan and methionine. Variant H103Y was produced in Pichia pastoris and characterized and revealed a five-fold increase of the oxygen reactivity.

Indexed as

AgaricusCarbohydrate DehydrogenasesCatalytic DomainChemical PrecipitationElectronsElectrophoresis, Polyacrylamide GelGenetic EngineeringHigh-Throughput Screening AssaysKineticsMutagenesis, Site-DirectedMutant ProteinsOxygenRecombinant ProteinsSaccharomyces cerevisiaeTemperatureCarbohydrate DehydrogenasesMutant ProteinsOxygenRecombinant Proteins

Identifiers

PMID24614932
PMCPMC3948749
OpenAlexW1964021249

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.