Evidence map›Paper›PMID 34235532›Full record

ArticleOrganic & biomolecular chemistry2021

Biocatalytic enantioselective hydroaminations enabling synthesis of

Mohammad Z Abidin, Thangavelu Saravanan, Laura Bothof, Pieter G Tepper, Andy-Mark W H Thunnissen, Gerrit J Poelarends

Open access · hybridAbstract read
In one paragraph

Article in Organic & biomolecular chemistry, 2021. 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
0.2field-weighted citation impact, top 51% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. Engineered C-N Lyases for Stereoselective Synthesis of Tertiary Amines.Angewandte Chemie (International ed. in English) · 2025
    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

6 authors at 3 institutions in 5 countries.

Mohammad Z AbidinDepartment of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands. g.j.poelarends.rug.nl and Department of Animal Product Technology, Faculty of Animal Science, Gadjah Mada University, Bulaksumur, Yogyakarta, 55281, Indonesia.ORCID 0000-0002-1966-833X
Thangavelu SaravananDepartment of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands. g.j.poelarends.rug.nl and School of Chemistry, University of Hyderabad, P.O. Central University, Hyderabad-500046, India. tsaravanan@uohyd.ac.in.ORCID 0000-0002-0792-9811
Laura BothofDepartment of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands. g.j.poelarends.rug.nl.ORCID 0000-0003-3966-443X
Pieter G TepperDepartment of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands. g.j.poelarends.rug.nl.
Andy-Mark W H ThunnissenMolecular Enzymology Group, Groningen Institute of Biomolecular Sciences and Biotechnology, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.ORCID 0000-0002-1915-9850
Gerrit J PoelarendsDepartment of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands. g.j.poelarends.rug.nl.ORCID 0000-0002-6917-6368
University of Groningen · NLBiotechnology Institute · USUniversitas Gadjah Mada · ID

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-Substituted l-aspartic acids are important chiral building blocks for pharmaceuticals and food additives. Here we report the asymmetric synthesis of various N-arylalkyl-substituted l-aspartic acids using ethylenediamine-N,N'-disuccinic acid lyase (EDDS lyase) as a biocatalyst. This C-N lyase shows a broad non-natural amine substrate scope and outstanding enantioselectivity, allowing the efficient addition of structurally diverse arylalkylamines to fumarate to afford the corresponding N-arylalkyl-substituted l-aspartic acids in good isolated yield (up to 79%) and with excellent enantiopurity (>99% ee). These results further demonstrate that C-N lyases working in reverse constitute an extremely powerful synthetic tool to prepare difficult noncanonical amino acids.

Indexed as

Aspartic AcidBiocatalysisAminationMolecular StructureStereoisomerismAspartic Acid

Identifiers

PMID34235532
PMCPMC8317194
OpenAlexW3173593049

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.