Evidence map›Paper›PMID 32315503›Full record

ReviewChembiochem : a European journal of chemical biology2020

Recent Applications of Carbon-Nitrogen Lyases in Asymmetric Synthesis of Noncanonical Amino Acids and Heterocyclic Compounds.

Jielin Zhang, Mohammad Z Abidin, Thangavelu Saravanan, Gerrit J Poelarends

Open access · hybridAbstract readReview
In one paragraph

Review in Chembiochem : a European journal of chemical biology, 2020. 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
0.8field-weighted citation impact, top 31% 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, 16 citations in OpenAlex.

  1. Cupin-Type Dimethylsulfoniopropionate Lyase from Pelagibacter ubique (DddKAngewandte Chemie (International ed. in English) · 2025
    Article
  2. Engineered C-N Lyases for Stereoselective Synthesis of Tertiary Amines.Angewandte Chemie (International ed. in English) · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Review
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

4 authors at 3 institutions in 5 countries.

Jielin ZhangDepartment of Chemical and Pharmaceutical Biology Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV, Groningen, The Netherlands.
Mohammad Z AbidinDepartment of Chemical and Pharmaceutical Biology Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV, Groningen, The Netherlands.
Thangavelu SaravananDepartment of Chemical and Pharmaceutical Biology Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV, Groningen, The Netherlands.
Gerrit J PoelarendsDepartment of Chemical and Pharmaceutical Biology Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV, Groningen, The Netherlands.ORCID 0000-0002-6917-6368
University of Groningen · NLChina Pharmaceutical University · CNUniversitas Gadjah Mada · ID

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbon-nitrogen (C-N) lyases are enzymes that normally catalyze the cleavage of C-N bonds. Reversing this reaction towards carbon-nitrogen bond formation can be a powerful approach to prepare valuable compounds that could find applications in everyday life. This review focuses on recent (last five years) applications of native and engineered C-N lyases, either as stand-alone biocatalysts or as part of multienzymatic and chemoenzymatic cascades, in enantioselective synthesis of noncanonical amino acids and dinitrogen-fused heterocycles, which are useful tools for neurobiological research and important synthetic precursors to pharmaceuticals and food additives.

Indexed as

Amino AcidsBiocatalysisCarbon-Nitrogen LyasesHeterocyclic CompoundsMolecular StructureStereoisomerismAmino AcidsCarbon-Nitrogen LyasesHeterocyclic Compoundsamino acidsbiocatalysisenzymesheterocycleslyases

Identifiers

PMID32315503
PMCPMC7586795
OpenAlexW3016391301

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.