Evidence map›Paper›PMID 40977070›Full record

ArticleChemistryOpen2025

Buffer-Mediated Catalyst-Free Strecker Reaction Toward Enzymatic Implementation.

Péter Magyar, Szilárd Újvári, Zsófia Molnár, Zoltán Orgován, Diána Balogh-Weiser, Blanka Eszter Nagy, Diana Maria Scrob, László Poppe, Péter Ábrányi-Balogh

Abstract read
In one paragraph

Article in ChemistryOpen, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

9 authors.

Péter MagyarMedicinal Chemistry Research Group, HUN-REN Research Centre for Natural Sciences, Magyar tudósok körútja 2, Budapest, 1117, Hungary.
Szilárd ÚjváriMedicinal Chemistry Research Group, HUN-REN Research Centre for Natural Sciences, Magyar tudósok körútja 2, Budapest, 1117, Hungary.
Zsófia MolnárDepartment of Organic Chemistry and Technology, Faculty of Chemical Technology and Biotechnology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest, 1111, Hungary.
Zoltán OrgovánMedicinal Chemistry Research Group, HUN-REN Research Centre for Natural Sciences, Magyar tudósok körútja 2, Budapest, 1117, Hungary.
Diána Balogh-WeiserDepartment of Organic Chemistry and Technology, Faculty of Chemical Technology and Biotechnology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest, 1111, Hungary.
Blanka Eszter NagyEnzymology and Applied Biocatalysis Research Center, Faculty of Chemistry and Chemical Engineering, Babeş-Bolyai University of Cluj-Napoca, Arany János str. 11, Cluj-Napoca, 400028, Romania.
Diana Maria ScrobEnzymology and Applied Biocatalysis Research Center, Faculty of Chemistry and Chemical Engineering, Babeş-Bolyai University of Cluj-Napoca, Arany János str. 11, Cluj-Napoca, 400028, Romania.
László PoppeDepartment of Organic Chemistry and Technology, Faculty of Chemical Technology and Biotechnology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest, 1111, Hungary.
Péter Ábrányi-BaloghMedicinal Chemistry Research Group, HUN-REN Research Centre for Natural Sciences, Magyar tudósok körútja 2, Budapest, 1117, Hungary.ORCID 0000-0002-9284-5160

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A systematic investigation of the catalyst-free Strecker reaction is conducted in aqueous buffer, offering an efficient and green alternative that leads to α-aminonitriles without the need of chromatography. Optimization reveals that low pH and high buffer concentration significantly enhance conversion, with yields up to 97%. Broad substrate scope is demonstrated with various aldehydes, ketones, and amines, leading to key intermediates for natural and unnatural amino acids. Potassium cyanide and acetone cyanohydrin are established, latter as a safer and effective cyanide source, and reactions are conducted also in buffer-methyl tert-butyl ether mixed solvent further improving the methodology. It is hypothesized that, based on the similarity to cyanohydrin formation, the hydroxynitrile lyases (HNLs) might transform imines to aminonitriles. Adding AtHNL and HbHNL further accelerates the reaction suggesting an undiscovered reactivity of these enzymes.

Indexed as

Aldehyde-LyasesNitrilesAldehydesAminesAmino AcidsBuffersCatalysisHydrogen-Ion ConcentrationKetonesAldehyde-LyasesAldehydesAminesAmino AcidsBufferscyanohydrinKetonesNitrilesaqueous conditionscatalyst‐freehydroxynitrile lyaseStrecker reaction

Identifiers

PMID40977070
PMCPMC12680554

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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.