Evidence map›Paper›PMID 32494734›Full record

ArticleScience advances2020

Characterization of imine reductases in reductive amination for the exploration of structure-activity relationships.

Sarah L Montgomery, Ahir Pushpanath, Rachel S Heath, James R Marshall, Ulrike Klemstein, James L Galman, David Woodlock, Serena Bisagni, Christopher J Taylor, J Mangas-Sanchez and 3 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

23 citing papers in PubMed, 70 citations in OpenAlex.

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  4. Cupin-Type Dimethylsulfoniopropionate Lyase from Pelagibacter ubique (DddKAngewandte Chemie (International ed. in English) · 2025
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  15. Review
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  17. New Trends and Future Opportunities in the Enzymatic Formation of C-C, C-N, and C-O bonds.Chembiochem : a European journal of chemical biology · 2022
    Review
  18. Article
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  20. 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

13 authors at 2 institutions in 1 country.

Sarah L MontgomerySchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.ORCID 0000-0003-3703-4338
Ahir PushpanathJohnson Matthey, 28 Cambridge Science Park, Milton Road, Cambridge CB4 0FP, UK.
Rachel S HeathSchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.ORCID 0000-0003-1910-8268
James R MarshallSchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.ORCID 0000-0002-4581-9832
Ulrike KlemsteinSchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.
James L GalmanSchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.ORCID 0000-0003-2076-2806
David WoodlockJohnson Matthey, 28 Cambridge Science Park, Milton Road, Cambridge CB4 0FP, UK.ORCID 0000-0001-8839-6641
Serena BisagniJohnson Matthey, 28 Cambridge Science Park, Milton Road, Cambridge CB4 0FP, UK.ORCID 0000-0002-9710-0125
Christopher J TaylorSchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.ORCID 0000-0001-9343-2766
J Mangas-SanchezSchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.ORCID 0000-0002-3364-1512
J I RamsdenSchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.
Beatriz DominguezJohnson Matthey, 28 Cambridge Science Park, Milton Road, Cambridge CB4 0FP, UK.
Nicholas J TurnerSchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.ORCID 0000-0003-1910-8268
University of Manchester · GBJohnson Matthey (United Kingdom) · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Imine reductases (IREDs) have shown great potential as catalysts for the asymmetric synthesis of industrially relevant chiral amines, but a limited understanding of sequence activity relationships makes rational engineering challenging. Here, we describe the characterization of 80 putative and 15 previously described IREDs across 10 different transformations and confirm that reductive amination catalysis is not limited to any particular subgroup or sequence motif. Furthermore, we have identified another dehydrogenase subgroup with chemoselectivity for imine reduction. Enantioselectivities were determined for the reduction of the model substrate 2-phenylpiperideine, and the effect of changing the reaction conditions was also studied for the reductive aminations of 1-indanone, acetophenone, and 4-methoxyphenylacetone. We have performed sequence-structure analysis to help explain clusters in activity across a phylogenetic tree and to inform rational engineering, which, in one case, has conferred a change in chemoselectivity that had not been previously observed.

Identifiers

PMID32494734
PMCPMC7244260
OpenAlexW3028127883

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

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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.