Evidence map›Paper›PMID 38569221›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2024

Rationally Engineering pH Adaptation of Acid-Induced Arginine Decarboxylase from Escherichia coli to Alkaline Environments to Efficiently Biosynthesize Putrescine.

Li Wang, Bo Ding, Xiangyang Hu, Guohui Li, Yu Deng

Open access · goldAbstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.1field-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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. De novo biosynthesis of putrescine from glucose using engineeredSynthetic and systems biotechnology · 2026
    Article
  3. Article
  4. Article
  5. 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

5 authors at 1 institution in 1 country.

Li WangNational Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangsu Provincial Research Center for Bioactive Product Processing Technology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China.ORCID 0000-0003-0694-1912
Bo DingNational Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangsu Provincial Research Center for Bioactive Product Processing Technology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China.
Xiangyang HuNational Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangsu Provincial Research Center for Bioactive Product Processing Technology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China.
Guohui LiNational Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangsu Provincial Research Center for Bioactive Product Processing Technology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China.ORCID 0000-0001-5173-3819
Yu DengNational Engineering Research Center of Cereal Fermentation and Food Biomanufacturing, Jiangsu Provincial Research Center for Bioactive Product Processing Technology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu, 214122, China.
Jiangnan University · CN

Funding

China Postdoctoral Science Foundation 2020M681485China Postdoctoral Science Foundation 2021T140277Jiangsu Planned Projects for Postdoctoral Research Funds 2020Z012National Key Research and Development Program of China 2021YFC2100700National Natural Science Foundation of China 21877053National Natural Science Foundation of China 22008088Natural Science Foundation of Jiangsu Province BK20220089Tianjin Synthetic Biotechnology Innovation Capacity Improvement Project TSBICIP-KJGG-015
6 · The paper itself

Abstract

Acid-induced arginine decarboxylase AdiA is a typical homo-oligomeric protein biosynthesizing alkaline nylon monomer putrescine. However, upon loss of the AdiA decamer oligomeric state at neutral and alkaline conditions the activity also diminishes, obstructing the whole-cell biosynthesis of alkaline putrescine. Here, a structure cohesion strategy is proposed to change the pH adaptation of AdiA to alkaline environments based on the rational engineering of meridional and latitudinal oligomerization interfaces. After integrating substitutions of E467K at the latitudinal interface and H736E at the meridional channel interface, the structural stability of AdiA decamer and its substrate transport efficiency at neutral and alkaline conditions are improved. Finally, E467K_H736E is well adapted to neutral and alkaline environments (pH 7.0-9.0), and its enzymatic activity is 35-fold higher than that of wild AdiA at pH 8.0. Using E467K_H736E in the putrescine synthesis pathway, the titer of putrescine is up to 128.9 g·L

Indexed as

Carboxy-LyasesEscherichia coliPutrescineHydrogen-Ion Concentrationarginine decarboxylaseCarboxy-LyasesPutrescinearginine decarboxylasebiocatalysispH adaptationprotein engineeringputrescine

Identifiers

PMID38569221
PMCPMC11186044
OpenAlexW4393852279

What OpenQuestion holds

Textmetadata
LicenceCC BY
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 OpenQuestion graph.