Evidence map›Paper›PMID 38684703›Full record

ArticleNature communications2024

Discovering a mitochondrion-localized BAHD acyltransferase involved in calystegine biosynthesis and engineering the production of 3β-tigloyloxytropane.

Junlan Zeng, Xiaoqiang Liu, Zhaoyue Dong, Fangyuan Zhang, Fei Qiu, Mingyu Zhong, Tengfei Zhao, Chunxian Yang, Lingjiang Zeng, Xiaozhong Lan and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.6field-weighted citation impact, top 13% of its field
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

11 citing papers in PubMed, 14 citations in OpenAlex.

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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

15 authors at 4 institutions in 2 countries.

Junlan ZengIntegrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City, State Key Laboratory of Resource Insects, SWU-TAAHC Medicinal Plant Joint R&D Centre, School of Life Sciences, Southwest University, Chongqing, 400715, China.ORCID http://orcid.org/0000-0002-0062-1873
Xiaoqiang LiuIntegrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City, State Key Laboratory of Resource Insects, SWU-TAAHC Medicinal Plant Joint R&D Centre, School of Life Sciences, Southwest University, Chongqing, 400715, China.
Zhaoyue DongCollege of Pharmaceutical Sciences, Southwest University, Chongqing, 400715, China.
Fangyuan ZhangIntegrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City, State Key Laboratory of Resource Insects, SWU-TAAHC Medicinal Plant Joint R&D Centre, School of Life Sciences, Southwest University, Chongqing, 400715, China.
Fei QiuIntegrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City, State Key Laboratory of Resource Insects, SWU-TAAHC Medicinal Plant Joint R&D Centre, School of Life Sciences, Southwest University, Chongqing, 400715, China.
Mingyu ZhongIntegrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City, State Key Laboratory of Resource Insects, SWU-TAAHC Medicinal Plant Joint R&D Centre, School of Life Sciences, Southwest University, Chongqing, 400715, China.
Tengfei ZhaoIntegrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City, State Key Laboratory of Resource Insects, SWU-TAAHC Medicinal Plant Joint R&D Centre, School of Life Sciences, Southwest University, Chongqing, 400715, China.
Chunxian YangIntegrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City, State Key Laboratory of Resource Insects, SWU-TAAHC Medicinal Plant Joint R&D Centre, School of Life Sciences, Southwest University, Chongqing, 400715, China.
Lingjiang ZengIntegrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City, State Key Laboratory of Resource Insects, SWU-TAAHC Medicinal Plant Joint R&D Centre, School of Life Sciences, Southwest University, Chongqing, 400715, China.
Xiaozhong LanTAAHC-SWU Medicinal Plant Joint R&D Centre, The Provincial and Ministerial Co-founded Collaborative Innovation Center for R&D in Xizang Characteristic Agricultural and Animal Husbandry Resources, Xizang Agricultural and Animal Husbandry College, Nyingchi, 860000, China.
Hongbo ZhangKey Laboratory of Synthetic Biology of Ministry of Agriculture and Rural Affairs, Tobacco Research Institute of Chinese Academy of Agricultural Sciences, Qingdao, 266101, China.
Junhui ZhouState Key Laboratory of Dao-di Herbs, National Resource Center for Chinese Materia Medica, China Academy of Chinese Medical Sciences, Beijing, 100700, China.
Min ChenCollege of Pharmaceutical Sciences, Southwest University, Chongqing, 400715, China.
Kexuan TangIntegrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City, State Key Laboratory of Resource Insects, SWU-TAAHC Medicinal Plant Joint R&D Centre, School of Life Sciences, Southwest University, Chongqing, 400715, China.
Zhihua LiaoIntegrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City, State Key Laboratory of Resource Insects, SWU-TAAHC Medicinal Plant Joint R&D Centre, School of Life Sciences, Southwest University, Chongqing, 400715, China. zhliao@swu.edu.cn.ORCID http://orcid.org/0000-0002-1283-4649
Southwest University · CNAnimal Husbandry and Veterinary Department · INChinese Academy of Medical Sciences & Peking Union Medical College · CNTobacco Research Institute · CN

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32370277Natural Science Foundation of Chongqing (Natural Science Foundation of Chongqing Municipality) cstc2021jcyj-msxmX0571
6 · The paper itself

Abstract

Solanaceous plants produce tropane alkaloids (TAs) via esterification of 3α- and 3β-tropanol. Although littorine synthase is revealed to be responsible for 3α-tropanol esterification that leads to hyoscyamine biosynthesis, the genes associated with 3β-tropanol esterification are unknown. Here, we report that a BAHD acyltransferase from Atropa belladonna, 3β-tigloyloxytropane synthase (TS), catalyzes 3β-tropanol and tigloyl-CoA to form 3β-tigloyloxytropane, the key intermediate in calystegine biosynthesis and a potential drug for treating neurodegenerative disease. Unlike other cytosolic-localized BAHD acyltransferases, TS is localized to mitochondria. The catalytic mechanism of TS is revealed through molecular docking and site-directed mutagenesis. Subsequently, 3β-tigloyloxytropane is synthesized in tobacco. A bacterial CoA ligase (PcICS) is found to synthesize tigloyl-CoA, an acyl donor for 3β-tigloyloxytropane biosynthesis. By expressing TS mutant and PcICS, engineered Escherichia coli synthesizes 3β-tigloyloxytropane from tiglic acid and 3β-tropanol. This study helps to characterize the enzymology and chemodiversity of TAs and provides an approach for producing 3β-tigloyloxytropane.

Indexed as

AcyltransferasesMitochondriaTropanesEscherichia coliMolecular Docking SimulationMutagenesis, Site-DirectedNicotianaPlant ProteinsAcyltransferasesPlant ProteinsTropanes

Identifiers

PMID38684703
PMCPMC11058270
OpenAlexW4396239213

What OpenQuestion holds

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LicenceCC BY
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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.