Evidence map›Paper›PMID 42232029›Full record

ArticleChem & bio engineering2026

Enhancing Diastereoselectivity of l‑Threonine Aldolase by Strengthening Kinetic Control To Mitigate Thermodynamic Equilibrium.

Wenlong Zheng, Sai Fang, Chennuo Zhu, Liu Yang, Yan Meng, Lirong Yang, Jianping Wu

Abstract read
In one paragraph

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

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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

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

7 authors.

Wenlong ZhengZhejiang Key Laboratory of Intelligent Manufacturing for Functional Chemicals, ZJU-Hangzhou Global Scientific and Technological Innovation Center, Zhejiang University, Hangzhou 311215, China.
Sai FangInstitute of Bioengineering, College of Chemical and Biological Engineering, Zhejiang University, Hangzhou 310058, China.
Chennuo ZhuInstitute of Bioengineering, College of Chemical and Biological Engineering, Zhejiang University, Hangzhou 310058, China.
Liu YangInstitute of Bioengineering, College of Chemical and Biological Engineering, Zhejiang University, Hangzhou 310058, China.
Yan MengInstitute of Bioengineering, College of Chemical and Biological Engineering, Zhejiang University, Hangzhou 310058, China.
Lirong YangZhejiang Key Laboratory of Intelligent Manufacturing for Functional Chemicals, ZJU-Hangzhou Global Scientific and Technological Innovation Center, Zhejiang University, Hangzhou 311215, China.ORCID https://orcid.org/0000-0002-6378-8451
Jianping WuZhejiang Key Laboratory of Intelligent Manufacturing for Functional Chemicals, ZJU-Hangzhou Global Scientific and Technological Innovation Center, Zhejiang University, Hangzhou 311215, China.ORCID https://orcid.org/0000-0002-9924-7307

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The reaction catalyzed by l-threonine aldolase (LTA) for the formation of β-hydroxy-α-amino acids is governed by both kinetic and thermodynamic control, causing the diastereoselectivity of LTA to gradually decrease as the reaction progresses. This hinders the enzyme's industrial application. To address this, we proposed a strategy to enhance kinetic control via substrate tunnel engineering, thereby mitigating the influence of thermodynamic equilibrium. We investigated hotspot amino acid residues in the substrate tunnel using the VR-3M mutant from

Indexed as

kinetic controll-threonine aldolasesubstrate tunnelthermodynamic equilibrium

Identifiers

PMID42232029
PMCPMC13223680

What OpenQuestion holds

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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.