ArticleCatalysis science & technology2025
Characterizing Y224 conformational flexibility in FtmOx1-catalysis using
Xinye Wang, Lingyun Yang, Shenlin Wang, Jun Wang, Kelin Li, Nathchar Naowarojna, Yi Ju, Ke Ye, Yuchen Han, Wupeng Yan and 3 more
Abstract read
In one paragraphArticle in Catalysis science & technology, 2025. 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 itWhat 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 registryThe 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 literatureWho cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what moneyAuthors and funding
13 authors.
Xinye WangState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology Shanghai 200237 China liuxueting@ecust.edu.cn lizhang@ecust.edu.cn.
Lingyun YangiHuman Institute, Shanghaitech University Shanghai 201210 China.
Shenlin WangState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology Shanghai 200237 China liuxueting@ecust.edu.cn lizhang@ecust.edu.cn.
Jun WangSchool of Life Sciences and Biotechnology, Shanghai Jiao Tong University Shanghai 200240 China yanwupeng@sjtu.edu.cn.
Kelin LiDepartment of Chemistry, Boston University Boston Massachusetts 02215 USA pinghua@bu.edu.
Nathchar NaowarojnaProgram of Chemistry, Faculty of Science and Technology, Sakon Nakhon Rajabhat University Sakon Nakhon 47000 Thailand.
Yi JuState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology Shanghai 200237 China liuxueting@ecust.edu.cn lizhang@ecust.edu.cn.
Ke YeState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology Shanghai 200237 China liuxueting@ecust.edu.cn lizhang@ecust.edu.cn.
Yuchen HanState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology Shanghai 200237 China liuxueting@ecust.edu.cn lizhang@ecust.edu.cn.
Wupeng YanSchool of Life Sciences and Biotechnology, Shanghai Jiao Tong University Shanghai 200240 China yanwupeng@sjtu.edu.cn.
Xueting LiuState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology Shanghai 200237 China liuxueting@ecust.edu.cn lizhang@ecust.edu.cn.ORCID https://orcid.org/0000-0002-1322-8253 Lixin ZhangState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology Shanghai 200237 China liuxueting@ecust.edu.cn lizhang@ecust.edu.cn.
Funding
Alkaloid Biosynthetic StudiesR01GM140040 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI LIU, PINGHUA · 2021 to 2024
$1.4MNIGMS NIH HHS R01 GM140040
6 · The paper itselfAbstract
α-Ketoglutarate-dependent non-haem iron (αKG-NHFe) enzymes play a crucial role in natural product biosynthesis, and in some cases exhibiting multifunctional catalysis capability. This study focuses on αKG-NHFe enzyme FtmOx1, which catalyzes endoperoxidation, dealkylation, and alcohol oxidation reactions in verruculogen biosynthesis. We explore the hypothesis that the conformational dynamics of the active site Y224 confer the multifunctional activities of FtmOx1-catalysis. Utilizing Y224-to-3,5-difluorotyrosine-substituted FtmOx1, produced
Identifiers
PMID39669701
PMCPMC11629144
What OpenQuestion holds
Textmetadata
LicenceCC BY-NC
Read underepoch 390