Evidence map›Paper›PMID 32402113›Full record

ArticleAngewandte Chemie (International ed. in English)2020

Engineering Orthogonal Methyltransferases to Create Alternative Bioalkylation Pathways.

Abigail J Herbert, Sarah A Shepherd, Victoria A Cronin, Matthew R Bennett, Rehana Sung, Jason Micklefield

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

22 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Selective Biocatalytic N-Methylation of Unsaturated Heterocycles.Angewandte Chemie (International ed. in English) · 2022
    Article
  8. Review
  9. Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022
    Review
  10. 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
  11. Article
  12. From Natural Methylation to Versatile Alkylations Using Halide Methyltransferases.Chembiochem : a European journal of chemical biology · 2021
    Review
  13. Review
  14. Enzymkatalysierte späte Modifizierungen: Besser spät als nie.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021
    Review
  15. Enzymatic Late-Stage Modifications: Better Late Than Never.Angewandte Chemie (International ed. in English) · 2021
    Review
  16. Review
  17. Review
  18. A bicyclicRSC chemical biology · 2021
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Abigail J HerbertDepartment of Chemistry and Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Sarah A ShepherdDepartment of Chemistry and Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Victoria A CroninDepartment of Chemistry and Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Matthew R BennettDepartment of Chemistry and Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Rehana SungDepartment of Chemistry and Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Jason MicklefieldDepartment of Chemistry and Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.ORCID 0000-0001-8951-4873
University of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K00199X/1
6 · The paper itself

Abstract

S-adenosyl-l-methionine (SAM)-dependent methyltransferases (MTs) catalyse the methylation of a vast array of small metabolites and biomacromolecules. Recently, rare carboxymethylation pathways have been discovered, including carboxymethyltransferase enzymes that utilise a carboxy-SAM (cxSAM) cofactor generated from SAM by a cxSAM synthase (CmoA). We show how MT enzymes can utilise cxSAM to catalyse carboxymethylation of tetrahydroisoquinoline (THIQ) and catechol substrates. Site-directed mutagenesis was used to create orthogonal MTs possessing improved catalytic activity and selectivity for cxSAM, with subsequent coupling to CmoA resulting in more efficient and selective carboxymethylation. An enzymatic approach was also developed to generate a previously undescribed co-factor, carboxy-S-adenosyl-l-ethionine (cxSAE), thereby enabling the stereoselective transfer of a chiral 1-carboxyethyl group to the substrate.

Indexed as

Crystallography, X-RayHumansMethyltransferasesMethyltransferasesbioalkylationbiotransformationscarboxymethylationenzyme cofactorsmethyltransferases

Identifiers

PMID32402113
PMCPMC7496830
OpenAlexW3024283326

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.