Evidence map›Paper›PMID 41618615›Full record

ArticlePlant biotechnology journal2026

Engineering of 10-Deacetylbaccatin III-10-β-O-Acetyltransferase From Taxus Species for Efficient Acetylating Non-Natural Substrates Into Taxol in Nicotiana benthamiana.

Tian-Jiao Chen, Jing-Jing Chen, Xiao-Yan Sun, Ting Gong, Jin-Ling Yang, Ping Zhu

Abstract read
In one paragraph

Article in Plant biotechnology journal, 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

6 authors.

Tian-Jiao ChenState Key Laboratory of Bioactive Substance and Function of Natural Medicines, NHC Key Laboratory of Biosynthesis of Natural Products, CAMS Key Laboratory of Enzyme and Biocatalysis of Natural Drugs, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, China.
Jing-Jing ChenState Key Laboratory of Bioactive Substance and Function of Natural Medicines, NHC Key Laboratory of Biosynthesis of Natural Products, CAMS Key Laboratory of Enzyme and Biocatalysis of Natural Drugs, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, China.
Xiao-Yan SunState Key Laboratory of Bioactive Substance and Function of Natural Medicines, NHC Key Laboratory of Biosynthesis of Natural Products, CAMS Key Laboratory of Enzyme and Biocatalysis of Natural Drugs, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, China.
Ting GongState Key Laboratory of Bioactive Substance and Function of Natural Medicines, NHC Key Laboratory of Biosynthesis of Natural Products, CAMS Key Laboratory of Enzyme and Biocatalysis of Natural Drugs, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, China.
Jin-Ling YangState Key Laboratory of Bioactive Substance and Function of Natural Medicines, NHC Key Laboratory of Biosynthesis of Natural Products, CAMS Key Laboratory of Enzyme and Biocatalysis of Natural Drugs, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, China.
Ping ZhuState Key Laboratory of Bioactive Substance and Function of Natural Medicines, NHC Key Laboratory of Biosynthesis of Natural Products, CAMS Key Laboratory of Enzyme and Biocatalysis of Natural Drugs, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, China.

Funding

Beijing Natural Science Foundation 7244470CAMS Innovation Fund for Medical Sciences CIFMS2021-I2M-1-029CAMS Innovation Fund for Medical Sciences CIFMS2024-I2M-TS-013National Key Research and Development Program of China 2020YFA0908003National Natural Science Foundation of China 31270796National Natural Science Foundation of China 81573325Special Research Fund for Central Universities, Peking Union Medical College 3332024064
6 · The paper itself

Abstract

7-β-xylosyl-10-deacetyltaxol (XDT) is much more abundant than the anticancer drug Taxol in Taxus species and is usually regarded as the by-product of Taxol. It could be enzymatically transformed into 10-deacetyltaxol (DT), and the latter could be further converted into Taxol. The enzyme 10-deacetylbaccatin III-10-β-O-acetyltransferase (DBAT) can acetylate the non-natural substrate DT into Taxol, but the conversion efficiency was extremely low. Herein, we globally redesigned DBAT

Indexed as

AcetyltransferasesNicotianaPaclitaxelProtein EngineeringTaxoidsTaxusAcetylationPlant Proteins10-deacetylbaccatine IIIAcetyltransferasesPaclitaxelPlant ProteinsTaxoids10‐deacetylbaccatin III‐10‐β‐O‐acetyltransferase10‐deacetyltaxol7‐β‐xylosyl‐10‐deacetyltaxoldirected evolutionNicotiana benthamianaTaxol biosynthesisvirtual design

Identifiers

PMID41618615
PMCPMC13110168

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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.