Evidence map›Paper›PMID 42238545›Full record

ArticleEngineering microbiology2026

Structure-guided surface engineering to improve the catalytic activity of ethylene-forming enzyme.

Mengyuan Wang, Zhuanglin Shen, Lian Wu, Weixue Huang, Jiahai Zhou, Yang Gu

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Engineering microbiology, 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
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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

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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

6 authors.

Mengyuan WangShenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China.
Zhuanglin ShenShenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China.
Lian WuState Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China.
Weixue HuangState Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China.
Jiahai ZhouShenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China.
Yang GuUniversity of Chinese Academy of Sciences, Beijing 100049, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ethylene-forming enzyme (EFE) is a member of the mononuclear non-heme Fe(II)- and 2-oxoglutarate-dependent oxygenase superfamily, which can oxidize 2-oxoglutarate to form ethylene in an arginine-dependent reaction. While significant enzyme engineering efforts have targeted the active site and surface of EFE, to date, no variant with substantially improved activity has been reported. To enhance catalytic activity and broaden the application potential of EFE, this study developed a surface engineering strategy based on structural analysis and potentially new l-Arg binding information. The resulting variant, E213T, exhibited a 1.5-fold increase in catalytic activity and a 2.4-fold elevation in

Indexed as

Catalytic activityEthylene-forming enzymeStructure-guidedSurface engineering

Identifiers

PMID42238545
PMCPMC13226243

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Registered trials

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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.