Evidence map›Paper›PMID 40815161›Full record

ArticleACS synthetic biology2025

Directed Evolution of Branched-Chain α-Keto Acid Decarboxylase for 3-Hydroxypropionic Acid Production in

Chuang Wang, René C L Olsthoorn, Huub J M de Groot

Abstract read
In one paragraph

Article in ACS synthetic biology, 2025. 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

3 authors.

Chuang WangLeiden Institute of Chemistry, Leiden University, Leiden 2300 RA, The Netherlands.
René C L OlsthoornLeiden Institute of Chemistry, Leiden University, Leiden 2300 RA, The Netherlands.
Huub J M de GrootLeiden Institute of Chemistry, Leiden University, Leiden 2300 RA, The Netherlands.ORCID 0000-0002-8796-1212

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

3-Hydroxypropionic acid (3-HP) serves as a crucial platform chemical with diverse applications across various industries. In this study, the oxaloacetate pathway was utilized for 3-HP production. This pathway involves the decarboxylation of oxaloacetate into malonic semialdehyde, catalyzed by branched-chain α-keto acid decarboxylase (KdcA), which is subsequently reduced to 3-HP by dehydrogenases. Directed evolution of KdcA was carried out to enhance its catalytic efficiency toward oxaloacetate, resulting in a KdcA

Indexed as

Carboxy-LyasesDirected Molecular EvolutionEscherichia coliLactic AcidOxaloacetic AcidEscherichia coli ProteinsMutationCarboxy-LyasesEscherichia coli Proteinshydracrylic acidLactic AcidOxaloacetic Acid3-hydroxypropionatebranched-chain α-keto acid decarboxylasedirected evolutionEscherichia colioxaloacetate pathway

Identifiers

PMID40815161
PMCPMC12455653

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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.