Evidence map›Paper›PMID 37081856›Full record

ArticleChemCatChem2023

The Discovery of Imine Reductases and their Utilisation for the Synthesis of Tetrahydroisoquinolines.

Max Cárdenas-Fernández, Rebecca Roddan, Eve M Carter, Helen C Hailes, John M Ward

Open access · hybridAbstract read
In one paragraph

Article in ChemCatChem, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

6 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. 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

5 authors at 2 institutions in 1 country.

Max Cárdenas-FernándezDepartment of Biochemical Engineering University College London Gower Street, Bernard Katz Building London WC1E 6BT UK.
Rebecca RoddanDepartment of Chemistry University College London 20 Gordon Street London WC1H 0AJ UK.ORCID 0000-0002-9406-9011
Eve M CarterDepartment of Chemistry University College London 20 Gordon Street London WC1H 0AJ UK.
Helen C HailesDepartment of Chemistry University College London 20 Gordon Street London WC1H 0AJ UK.ORCID 0000-0001-5574-4742
John M WardDepartment of Biochemical Engineering University College London Gower Street, Bernard Katz Building London WC1E 6BT UK.ORCID 0000-0002-4415-5544
University College London · GBUniversity of Kent · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Imine reductases (IREDs) are NADPH-dependent enzymes with significant biocatalytic potential for the synthesis of primary, secondary, and tertiary chiral amines. Their applications include the reduction of cyclic imines and the reductive amination of prochiral ketones. In this study, twenty-nine novel IREDs were revealed through genome mining. Imine reductase activities were screened at pH 7 and 9 and in presence of either NADPH or NADH; some IREDs showed good activities at both pHs and were able to accept both cofactors. IREDs with Asn and Glu at the key 187 residue showed preference for NADH. IREDs were also screened against a series of dihydroisoquinolines to synthesise tetrahydroisoquinolines (THIQs), bioactive alkaloids with a wide range of therapeutic properties. Selected IREDs showed high stereoselectivity, as well high THIQ yields (>90 %) when coupled to a glucose-6-phosphate dehydrogenase for NADPH cofactor recycling.

Indexed as

activity screeningImine reductasesphylogenetic analysisreductive aminationtetrahydroisoquinolines

Identifiers

PMID37081856
PMCPMC10107726
OpenAlexW4311474415

What OpenQuestion holds

Textmetadata
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.