Evidence map›Paper›PMID 42554928›Full record

ReviewApplied biochemistry and biotechnology2026

Transaminases engineering and their cascade systems for natural product synthesis.

Yi-Xin Li, Chao Lin, Zi-Yu Guan, Yu-Si Zhang, Ya-Ping Xue, Zhi-Qiang Liu, Cong-Qiang Zhang, Li-Qun Jin, Yu-Guo Zheng

Abstract readReview
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In one paragraph

Review in Applied biochemistry and biotechnology, 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

9 authors.

Yi-Xin LiState Key Laboratory of Green Chemical Synthesis and Conversion, Zhejiang University of Technology, Hangzhou, 310014, P.R. China.
Chao LinState Key Laboratory of Green Chemical Synthesis and Conversion, Zhejiang University of Technology, Hangzhou, 310014, P.R. China.
Zi-Yu GuanState Key Laboratory of Green Chemical Synthesis and Conversion, Zhejiang University of Technology, Hangzhou, 310014, P.R. China.
Yu-Si ZhangState Key Laboratory of Green Chemical Synthesis and Conversion, Zhejiang University of Technology, Hangzhou, 310014, P.R. China.
Ya-Ping XueState Key Laboratory of Green Chemical Synthesis and Conversion, Zhejiang University of Technology, Hangzhou, 310014, P.R. China.
Zhi-Qiang LiuState Key Laboratory of Green Chemical Synthesis and Conversion, Zhejiang University of Technology, Hangzhou, 310014, P.R. China.
Cong-Qiang ZhangAgency for Science, Technology and Research (A*STAR), Singapore Institute of Food and Biotechnology Innovation (SIFBI), 31 Biopolis Way, Nanos, 138669, Singapore. congqiang_zhang@a-star.edu.sg.
Li-Qun JinState Key Laboratory of Green Chemical Synthesis and Conversion, Zhejiang University of Technology, Hangzhou, 310014, P.R. China. jlq@zjut.edu.cn.
Yu-Guo ZhengState Key Laboratory of Green Chemical Synthesis and Conversion, Zhejiang University of Technology, Hangzhou, 310014, P.R. China.

Funding

National Natural Science Foundation of China 22478352Zhejiang Xinmiao Talents Program 2026XMGD037
6 · The paper itself

Abstract

Transaminases (TAs) represent a class of enzymes that enable highly stereoselective amination reactions under mild conditions, providing an exceptionally powerful and versatile green chemistry tool for the synthesis of chiral amines and nitrogen-containing compounds. However, most current reviews on transaminases focus on the efficient synthesis of chiral amines, whereas the efficient synthesis of complex natural products has rarely been reported. This review systematically discusses the characteristics of different types of transaminases, covering their underlying catalytic mechanisms, the dynamics and roles of the cofactor involved, and key enzymatic properties that are critical for their function and practical applicability. Recent advances in protein engineering strategies and in the design of multi-enzyme cascade systems are also discussed. A particular focus is directed toward representative applications of transaminase-mediated multi-enzyme cascade systems in natural product synthesis. Based on a systematic review of recent advances in transaminase research, this review focuses on their representative applications in multi‑enzyme cascade systems for natural product synthesis, providing a comprehensive and referenceable framework for green synthetic strategies.

Indexed as

Multi-enzyme cascade systemNatural productsProtein engineeringTransaminase

Identifiers

What Socratic holds

Textmetadata
Read underepoch 390

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 Socratic graph.