Evidence map›Paper›PMID 40916641›Full record

ReviewBMB reports2026

Reverse beta-oxidation for biochemical production: insights into the functional properties of key enzymes.

Areum Lee, Hyeoncheol Francis Son

Abstract readReview
In one paragraph

Review in BMB reports, 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

2 authors.

Areum LeeSchool of Biological Sciences and Technology, Chonnam National University, Gwangju 61186, Korea.
Hyeoncheol Francis SonSchool of Biological Sciences and Technology, Chonnam National University, Gwangju 61186; Institute of Synthetic Biology for Carbon Neutralization, Chonnam National University, Gwangju 61186; Institute of Systems Biology and Life Science Informatics, Chonnam National University, Gwangju 61186, Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The reverse β-oxidation (rBOX) pathway is emerging as a promising alternative to fossil fuel-based chemical production, providing a versatile platform for the synthesis of various valueadded biochemicals. Efficient application of rBOX depends on the selection of enzymes with high catalytic activity, suitable substrate specificity, and strong functional compatibility within the pathway. In this review, we focus on the structural and biochemical characteristics of four key enzymes-thiolase, 3-hydroxyacyl-CoA dehydrogenase, enoyl-CoA hydratase, and enoyl-CoA reductase-and explore how their individual features and combinations influence pathway performance. We then summarize previous studies that highlight the importance of enzyme cooperation in achieving optimal production outcomes. These insights provide valuable guidance for the rational design of rBOX-based biosynthetic pathways tailored to specific chemical targets. [BMB Reports 2026; 59(4): 209-218].

Indexed as

Enoyl-CoA HydrataseOxidation-ReductionSubstrate SpecificityEnoyl-CoA Hydratase

Identifiers

PMID40916641
PMCPMC13126070

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.