Enantioselective Hydration of Non-CoA Enoyl-Thioesters by Enoyl-CoA Hydratase (ECH): Activation of the Active Site Oxyanion Hole with 3',5'-Adenosine-Diphosphate Enables Competent Catalysis.

Subhadra Dalwani, Pradip Kumar Mondal, Werner Schmitz, Rik K Wierenga, Petri M Pihko

Abstract read

In one paragraph

Article in JACS Au, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

5 authors.

Subhadra DalwaniFaculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, Oulu FI-90014, Finland.ORCID https://orcid.org/0000-0001-8281-9463

Pradip Kumar MondalDepartment of Chemistry and NanoScience Center, University of Jyväskylä, P.O.Box 35, Jyväskylä FI-40014, Finland.

Werner SchmitzInstitute of Biochemistry and Molecular Biology, University of Würzburg, Würzburg DE-97070, Germany.

Rik K WierengaFaculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, Oulu FI-90014, Finland.ORCID https://orcid.org/0000-0001-6554-471X

Petri M PihkoDepartment of Chemistry and NanoScience Center, University of Jyväskylä, P.O.Box 35, Jyväskylä FI-40014, Finland.ORCID https://orcid.org/0000-0003-0126-0974

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thioester chemistry is exploited in Nature by many CoA-dependent enzymes. However, the covalent nature of CoA attachment largely prevents the use of these enzymes in many applications. Replacing the CoA moiety with simpler, truncated fragments, such as its pantetheine (PAN) moiety, is also hampered by the lack of understanding of the function of the CoA moiety in enzymatic conversions. Herein, we describe the utilization of the enzyme (2

Indexed as

hydratase reactionsoxa-Michael additionpantetheinethioesters

Identifiers

PMID42063829

DOI10.1021/jacsau.6c00054

PMCPMC13126182

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