Evidence map›Paper›PMID 28450969›Full record

ArticleChemCatChem2017

Characterization of Carboxylic Acid Reductases as Enzymes in the Toolbox for Synthetic Chemistry.

William Finnigan, Adam Thomas, Holly Cromar, Ben Gough, Radka Snajdrova, Joseph P Adams, Jennifer A Littlechild, Nicholas J Harmer

Abstract read
In one paragraph

Article in ChemCatChem, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
–field-weighted citation impact
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

43 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Metabolic Engineering ofJournal of microbiology and biotechnology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Complete Genome Sequence of Nocardia iowensis DSM 45197Microbiology resource announcements · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Enzymkatalysierte späte Modifizierungen: Besser spät als nie.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021
    Review
  19. Enzymatic Late-Stage Modifications: Better Late Than Never.Angewandte Chemie (International ed. in English) · 2021
    Review
  20. Microbial synthesis of vanillin from waste poly(ethylene terephthalate).Green chemistry : an international journal and green chemistry resource : GC · 2021
    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

8 authors.

William FinniganBiosciences, College of Life and Environmental Sciences University of Exeter, Stocker Road Devon Exeter EX4 4QD UK.
Adam ThomasBiosciences, College of Life and Environmental Sciences University of Exeter, Stocker Road Devon Exeter EX4 4QD UK.
Holly CromarBiosciences, College of Life and Environmental Sciences University of Exeter, Stocker Road Devon Exeter EX4 4QD UK.
Ben GoughBiosciences, College of Life and Environmental Sciences University of Exeter, Stocker Road Devon Exeter EX4 4QD UK.
Radka SnajdrovaSynthetic Chemistry, AC-API Chem-UK, GlaxoSmithKline R&D Ltd Medicines Research Centre Gunnels Wood Road Stevenage Hertfordshire SG1 2NY UK.
Joseph P AdamsSynthetic Chemistry, AC-API Chem-UK, GlaxoSmithKline R&D Ltd Medicines Research Centre Gunnels Wood Road Stevenage Hertfordshire SG1 2NY UK.
Jennifer A LittlechildBiosciences, College of Life and Environmental Sciences University of Exeter, Stocker Road Devon Exeter EX4 4QD UK.
Nicholas J HarmerBiosciences, College of Life and Environmental Sciences University of Exeter, Stocker Road Devon Exeter EX4 4QD UK.ORCID 0000-0002-4073-0505

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carboxylic acid reductase enzymes (CARs) meet the demand in synthetic chemistry for a green and regiospecific route to aldehydes from their respective carboxylic acids. However, relatively few of these enzymes have been characterized. A sequence alignment with members of the ANL (Acyl-CoA synthetase/ NRPS adenylation domain/Luciferase) superfamily of enzymes shed light on CAR functional dynamics. Four unstudied enzymes were selected by using a phylogenetic analysis of known and hypothetical CARs, and for the first time, a thorough biochemical characterization was performed. Kinetic analysis of these enzymes with various substrates shows that they have a broad but similar substrate specificity. Electron-rich acids are favored, which suggests that the first step in the proposed reaction mechanism, attack by the carboxylate on the α-phosphate of adenosine triphosphate (ATP), is the step that determines the substrate specificity and reaction kinetics. The effects of pH and temperature provide a clear operational window for the use of these CARs, whereas an investigation of product inhibition by NADP

Indexed as

biocatalysiscarboxylic acidsenzymesgreen chemistryreduction

Identifiers

PMID28450969
PMCPMC5396282

What OpenQuestion holds

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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.