Evidence map›Paper›PMID 39562580›Full record

ArticleNature communications2024

Tuning architectural organization of eukaryotic P450 system to boost bioproduction in Escherichia coli.

Yikui Li, Jie Li, Wei-Kang Chen, Yang Li, Sheng Xu, Linwei Li, Bing Xia, Ren Wang

Abstract 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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Integrated biosynthesis of the lignan (-)-pluviatolide in resting and growingFrontiers in bioengineering and biotechnology · 2026
    Article
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.

Yikui Li *Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China.ORCID 0000-0002-6879-1238
Jie Li *Institute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China.
Wei-Kang ChenInstitute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China.
Yang LiInstitute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China.
Sheng XuInstitute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China.
Linwei LiInstitute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China.
Bing XiaInstitute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China.
Ren WangInstitute of Botany, Jiangsu Province and Chinese Academy of Sciences, Nanjing, 210014, China. rwang@cnbg.net.ORCID 0000-0001-6724-0744

Funding

National Natural Science Foundation of China (National Science Foundation of China) 31600074National Natural Science Foundation of China (National Science Foundation of China) 31770387Natural Science Foundation of Jiangsu Province (Jiangsu Provincial Natural Science Foundation) BK20160599
6 · The paper itself

Abstract

Eukaryotic cytochrome P450 enzymes, generally colocalizing with their redox partner cytochrome P450 reductase (CPR) on the cytoplasmic surface of organelle membranes, often perform poorly in prokaryotic cells, whether expressed with CPR as a tandem chimera or free-floating individuals, causing a low titer of heterologous chemicals. To improve their biosynthetic performance in Escherichia coli, here, we architecturally design self-assembled alternatives of eukaryotic P450 system using reconstructed P450 and CPR, and create a set of N-termini-bridged P450-CPR heterodimers as the counterparts of eukaryotic P450 system with N-terminus-guided colocalization. The covalent counterparts show superior and robust biosynthetic performance, and the N-termini-bridged architecture is validated to improve the biosynthetic performance of both plant and human P450 systems. Furthermore, the architectural configuration of protein assemblies has an inherent effect on the biosynthetic performance of N-termini-bridged P450-CPR heterodimers. The results suggest that spatial architecture-guided protein assembly could serve as an efficient strategy for improving the biosynthetic performance of protein complexes, particularly those related to eukaryotic membranes, in prokaryotic and even eukaryotic hosts.

Indexed as

Cytochrome P-450 Enzyme SystemEscherichia coliNADPH-Ferrihemoprotein ReductaseHumansOxidation-ReductionProtein MultimerizationCytochrome P-450 Enzyme SystemNADPH-Ferrihemoprotein Reductase

Identifiers

PMID39562580
PMCPMC11577030

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.