Evidence map›Paper›PMID 28937665›Full record

ArticleNature chemistry2017

A reductive aminase from Aspergillus oryzae.

Godwin A Aleku, Scott P France, Henry Man, Juan Mangas-Sanchez, Sarah L Montgomery, Mahima Sharma, Friedemann Leipold, Shahed Hussain, Gideon Grogan, Nicholas J Turner

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Nature chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
17.5field-weighted citation impact, top 1% 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

101 citing papers in PubMed, 382 citations in OpenAlex.

  1. Article
  2. Article
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  4. Biocatalytic Radical C(spResearch square · 2026
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  7. Article
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  9. Engineered C-N Lyases for Stereoselective Synthesis of Tertiary Amines.Angewandte Chemie (International ed. in English) · 2025
    Article
  10. Article
  11. High-ThroughputACS central science · 2025
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. In situ characterization of amine-forming enzymes shows altered oligomeric state.Protein science : a publication of the Protein Society · 2025
    Article
  19. Article
  20. Review

41 more citing papers are in PubMed but not listed here.

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

10 authors at 2 institutions in 1 country.

Godwin A AlekuSchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.
Scott P FranceSchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.
Henry ManYork Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, YO10 5DD, UK.
Juan Mangas-SanchezSchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.ORCID 0000-0002-3364-1512
Sarah L MontgomerySchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.ORCID 0000-0003-3703-4338
Mahima SharmaYork Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, YO10 5DD, UK.
Friedemann LeipoldSchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.
Shahed HussainSchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.
Gideon GroganYork Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, YO10 5DD, UK.
Nicholas J TurnerSchool of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK.ORCID 0000-0002-8708-0781
University of Manchester · GBUniversity of York · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reductive amination is one of the most important methods for the synthesis of chiral amines. Here we report the discovery of an NADP(H)-dependent reductive aminase from Aspergillus oryzae (AspRedAm, Uniprot code Q2TW47) that can catalyse the reductive coupling of a broad set of carbonyl compounds with a variety of primary and secondary amines with up to >98% conversion and with up to >98% enantiomeric excess. In cases where both carbonyl and amine show high reactivity, it is possible to employ a 1:1 ratio of the substrates, forming amine products with up to 94% conversion. Steady-state kinetic studies establish that the enzyme is capable of catalysing imine formation as well as reduction. Crystal structures of AspRedAm in complex with NADP(H) and also with both NADP(H) and the pharmaceutical ingredient (R)-rasagiline are reported. We also demonstrate preparative scale reductive aminations with wild-type and Q240A variant biocatalysts displaying total turnover numbers of up to 32,000 and space time yields up to 3.73 g l

Indexed as

AminationAminesAminohydrolasesAspergillus oryzaeBiocatalysisModels, MolecularMolecular StructureMutationOxidation-ReductionAminesAminohydrolases

Identifiers

PMID28937665
OpenAlexW2619829249

What OpenQuestion holds

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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.