Evidence map›Paper›PMID 34882252›Full record

ArticleApplied microbiology and biotechnology2022

Two novel cyanobacterial α-dioxygenases for the biosynthesis of fatty aldehydes.

In Jung Kim, Yannik Brack, Thomas Bayer, Uwe T Bornscheuer

Open access · hybridAbstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Review
  3. Enzymatic reactions towards aldehydes: An overview.Flavour and fragrance journal · 2023
    Review
  4. An enzymatic tandem reaction to produce odor-active fatty aldehydes.Applied microbiology and biotechnology · 2022
    Article
  5. 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

4 authors at 2 institutions in 1 country.

In Jung KimDepartment of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Yannik BrackDepartment of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Thomas BayerDepartment of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany.
Uwe T BornscheuerDepartment of Biotechnology and Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, 17489, Greifswald, Germany. uwe.bornscheuer@uni-greifswald.de.ORCID http://orcid.org/0000-0003-0685-2696
Universität Greifswald · DEUniversitätsmedizin Greifswald · DE

Funding

Austrian Science Fund FWF J 4231Fachagentur Nachwachsende Rohstoffe 22001617FWF J4231-B21Innovative Research Group Project of the National Natural Science Foundation of China NRF-2020R1A6A3A03039153
6 · The paper itself

Abstract

α-Dioxygenases (α-DOXs) are known as plant enzymes involved in the α-oxidation of fatty acids through which fatty aldehydes, with a high commercial value as flavor and fragrance compounds, are synthesized as products. Currently, little is known about α-DOXs from non-plant organisms. The phylogenic analysis reported here identified a substantial number of α-DOX enzymes across various taxa. Here, we report the functional characterization and Escherichia coli whole-cell application of two novel α-DOXs identified from cyanobacteria: CalDOX from Calothrix parietina and LepDOX from Leptolyngbya sp. The catalytic behavior of the recombinantly expressed CalDOX and LepDOX revealed that they are heme-dependent like plant α-DOXs but exhibit activities toward medium carbon fatty acids ranging from C10 to C14 unlike plant α-DOXs. The in-depth molecular investigation of cyanobacterial α-DOXs and their application in an E. coli whole system employed in this study is useful not only for the understanding of the molecular function of α-DOXs, but also for their industrial utilization in fatty aldehyde biosynthesis.Key points• Two novel α-dioxygenases from Cyanobacteria are reported• Both enzymes prefer medium-chain fatty acids• Both enzymes are useful for fatty aldehyde biosynthesis.

Indexed as

CyanobacteriaDioxygenasesAldehydesEscherichia coliFatty AcidsAldehydesDioxygenasesFatty Acidsfatty aldehydeAroma compoundsCyanobacteriaFatty acidFatty aldehydeα-Dioxygenase

Identifiers

PMID34882252
PMCPMC8720084
OpenAlexW4200435631

What OpenQuestion holds

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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.