Evidence map›Paper›PMID 42185663›Full record

ArticleBiotechnology letters2026

Expanding the cofactor range of aldehyde reductase YqhD by mutating key amino acids.

Xiaohui Wu, Yinghan Hu, Yanzhe Huang, Lingyun Zhang, Yan Xue, Hailong Cao, Xueying Wang, Yongjin J Zhou

Abstract read
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In one paragraph

Article in Biotechnology letters, 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

8 authors.

Xiaohui WuDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, PR China.
Yinghan HuDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, PR China.
Yanzhe HuangDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, PR China.
Lingyun ZhangDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, PR China.
Yan XueDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, PR China.
Hailong CaoZhongke Heyi (Dalian) Agricultural Technology Co., Ltd, Dalian, 116023, PR China.
Xueying WangDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, PR China. wangxueying@dicp.ac.cn.
Yongjin J ZhouDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, PR China.

Funding

Dalian Institute of Chemical Physics, CAS DICP I202523National Natural Science Foundation of China 22377125Strategic Priority Research Program of the Chinese Academy of Sciences XDC0120102
6 · The paper itself

Abstract

YqhD is a broad-substrate aldehyde reductase that natively prefers NADPH and is widely used in alcohol biosynthesis. However, insufficient NADPH supply and low cofactor regeneration efficiency limit its catalytic performance. To address this limitation, we engineered YqhD through structure-guided semi-rational design and obtained a mutant G37D with markedly improved dual-cofactor compatibility with NADPH and NADH. With butanal and 3-hydroxypropionaldehyde as substrates, G37D exhibited 2.6- and 4.8-fold increases in catalytic efficiency (k

Indexed as

Aldehyde ReductaseBacterial ProteinsCoenzymesAmino AcidsKineticsMolecular Dynamics SimulationMutationNADNADPPropylene GlycolsProtein EngineeringSubstrate Specificity1,3-propanediolAldehyde ReductaseAmino AcidsBacterial ProteinsCoenzymesNADNADPPropylene GlycolsAldehyde reductaseDual-cofactor specificityEnzyme modificationSemi-rational design

Identifiers

PMID42185663

What OpenQuestion holds

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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.