Evidence map›Paper›PMID 36049111›Full record

ArticleChembiochem : a European journal of chemical biology2022

Lipase-Catalysed Enzymatic Kinetic Resolution of Aromatic Morita-Baylis-Hillman Derivatives by Hydrolysis and Transesterification.

Nompumelelo P Mathebula, Roger A Sheldon, Moira L Bode

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

Article in Chembiochem : a European journal of chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Efficient synthesis of clascoteroneBiodesign research · 2025
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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

3 authors at 1 institution in 2 countries.

Nompumelelo P MathebulaMolecular Sciences Institute School of Chemistry, University of the Witwatersrand Private Bag X3, PO WITS, Johannesburg, 2050, South Africa.
Roger A SheldonMolecular Sciences Institute School of Chemistry, University of the Witwatersrand Private Bag X3, PO WITS, Johannesburg, 2050, South Africa.ORCID 0000-0001-6867-2119
Moira L BodeMolecular Sciences Institute School of Chemistry, University of the Witwatersrand Private Bag X3, PO WITS, Johannesburg, 2050, South Africa.ORCID 0000-0002-4153-5584
University of the Witwatersrand · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acylated Morita-Baylis-Hillman (MBH) adducts were synthesised and subjected to enzymatic kinetic resolution (EKR) by hydrolysis employing various lipase enzymes: from P. fluorescens, P. cepacia (PCL), C. antarctica A (CAL-A), C. antarctica B (CAL-B) and Novozyme 435. In a number of instances enantiopure Morita-Baylis-Hillman acetates or butyrates and their corresponding hydrolysed MBH adducts were obtained with ee values of >90 %, at ca. 50 % conversion, corresponding to enantiomeric ratio (E) values of >200. Enantioselective transesterification reactions on MBH adducts was achieved using acyl anhydrides in THF or the greener organic solvent 2-MeTHF in the presence of CAL-A. This is the first report of successful lipase-catalysed EKR of aromatic MBH adducts by transesterification in organic medium.

Indexed as

LipaseCatalysisEsterificationHydrolysisStereoisomerismLipaseenzymatic kinetic resolutionlipasesmolecular modellingMorita-Baylis-HillmanMosher derivativesPCL

Identifiers

PMID36049111
PMCPMC9828654
OpenAlexW4294068892

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.