Evidence map›Paper›PMID 26810201›Full record

ReviewApplied microbiology and biotechnology2016

Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities.

Kateryna Fesko

Open access · hybridAbstract readReview
In one paragraph

Review in Applied microbiology and biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 87 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
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  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Enzymatic Synthesis of l-Applied and environmental microbiology · 2021
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Biocatalytic synthesis of α-amino ketones.Synlett : accounts and rapid communications in synthetic organic chemistry · 2019
    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

1 author at 1 institution in 1 country.

Kateryna FeskoInstitute of Organic Chemistry, Graz University of Technology, Stremayrgasse 9, A-8010, Graz, Austria. kateryna.lypetska@tugraz.at.
Graz University of Technology · AT

Funding

Austrian Science Fund FWF T 735
6 · The paper itself

Abstract

Threonine aldolases have emerged as a powerful tool for asymmetric carbon-carbon bond formation. These enzymes catalyse the unnatural aldol condensation of different aldehydes and glycine to produce highly valuable β-hydroxy-α-amino acids with complete stereocontrol at the α-carbon and moderate specificity at the β-carbon. A range of microbial threonine aldolases has been recently recombinantly produced by several groups and their biochemical properties were characterized. Numerous studies have been conducted to improve the reaction protocols to enable higher conversions and investigate the substrate scope of enzymes. However, the application of threonine aldolases in organic synthesis is still limited due to often moderate yields and low diastereoselectivities obtained in the aldol reaction. This review briefly summarizes the screening techniques recently applied to discover novel threonine aldolases as well as enzyme engineering and mutagenesis studies which were accomplished to improve the catalytic activity and substrate specificity. Additionally, the results from new investigations on threonine aldolases including crystal structure determinations and structural-functional characterization are reviewed.

Indexed as

Mass ScreeningProtein EngineeringAldehydesGlycineGlycine HydroxymethyltransferaseSubstrate SpecificityAldehydesGlycineGlycine HydroxymethyltransferaseAldol reactionsBiocatalysisEnzyme engineeringScreeningThreonine aldolase

Identifiers

PMID26810201
PMCPMC4761611
OpenAlexW2260619470

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.